|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-768 |
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: 1339.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFASIAAGGSAKKEGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLA 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 259 SADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGETTVASINDGEELLATDEAFDVL 338
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 339 GFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQ 418
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 419 VYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQE 498
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 499 EYKKEGIEWEFIDFGMDLQACIDLIEKP-MGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRaiKGKPESHFS 577
Cdd:cd01377 401 EYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK--PKKSEAHFI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 578 LVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNgkggkgGGSKKKGSSFQTVSALHRENL 657
Cdd:cd01377 479 LKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGG------GKKKKKGGSFRTVSQLHKEQL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 658 NKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIPEGQF 737
Cdd:cd01377 553 NKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD 632
|
650 660 670
....*....|....*....|....*....|.
gi 163644331 738 iDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01377 633 -DGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
99-768 |
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: 1264.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFASIAAGGS-AKKEGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKL 257
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 258 ASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGETTVASINDGEELLATDEAFDV 337
Cdd:cd14913 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 338 LGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQ 417
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 418 QVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQ 497
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 498 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRAIKGKPESHFS 577
Cdd:cd14913 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 578 LVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDngkGGKGGGSKKKGSSFQTVSALHRENL 657
Cdd:cd14913 481 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADAD---SGKKKVAKKKGSSFQTVSALFRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 658 NKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIPEGQF 737
Cdd:cd14913 558 NKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQF 637
|
650 660 670
....*....|....*....|....*....|.
gi 163644331 738 IDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14913 638 IDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
99-768 |
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: 1210.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFASIAA-GGSAKKEGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKL 257
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAiGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 258 ASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGETTVASINDGEELLATDEAFDV 337
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 338 LGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQ 417
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 418 QVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQ 497
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 498 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRAIKGKPESHFS 577
Cdd:cd14917 401 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 578 LVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDngkGGKGGGSKKKGSSFQTVSALHRENL 657
Cdd:cd14917 481 LIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAP---IEKGKGKAKKGSSFQTVSALHRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 658 NKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIPEGQF 737
Cdd:cd14917 558 NKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 637
|
650 660 670
....*....|....*....|....*....|.
gi 163644331 738 IDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14917 638 IDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
100-768 |
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: 1199.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 180 SGAGKTVNTKRVIQYFASIAAGGSAKKEGAE-----KKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGAS 254
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDGPGKKAQflatkTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 255 GKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGETTVASINDGEELLATDEA 334
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 335 FDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQ 414
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 415 NVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFV 494
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 495 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRAIKG-KPE 573
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKrKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 574 SHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNGKGGKGGGSKKKGSSFQTVSALH 653
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEDPKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 654 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIP 733
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 163644331 734 EGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14927 642 DDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
99-768 |
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: 1191.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFASIAA-GGSAKKEGAE-KKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGK 256
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAiGDRSKKENPNaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 257 LASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGETTVASINDGEELLATDEAFD 336
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 337 VLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNV 416
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 417 QQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLE 496
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 497 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRAIKGKPESHF 576
Cdd:cd14916 401 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 577 SLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGteSDNGKGGKGGGSKKKGSSFQTVSALHREN 656
Cdd:cd14916 481 SLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYAS--ADTGDSGKGKGGKKKGSSFQTVSALHREN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 657 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIPEGQ 736
Cdd:cd14916 559 LNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQ 638
|
650 660 670
....*....|....*....|....*....|..
gi 163644331 737 FIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14916 639 FIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
99-768 |
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: 1139.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFASIAAGGSAKKEGAEKK--GTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGK 256
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKmqGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 257 LASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGETTVASINDGEELLATDEAFD 336
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 337 VLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNV 416
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 417 QQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLE 496
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 497 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRAIKGKPESHF 576
Cdd:cd14923 401 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 577 SLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNgKGGKGGGSKKKGSSFQTVSALHREN 656
Cdd:cd14923 481 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGD-SGGSKKGGKKKGSSFQTVSAVFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 657 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIPEGQ 736
Cdd:cd14923 560 LNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 163644331 737 FIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14923 640 FIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
99-768 |
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: 1125.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFASIAAGGSAKK-EGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKL 257
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKeESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 258 ASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGETTVASINDGEELLATDEAFDV 337
Cdd:cd14918 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 338 LGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQ 417
Cdd:cd14918 241 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 418 QVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQ 497
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 498 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRAIKGKPESHFS 577
Cdd:cd14918 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 578 LVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNgkgGKGGGSKKKGSSFQTVSALHRENL 657
Cdd:cd14918 481 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADS---GAKKGAKKKGSSFQTVSALFRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 658 NKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIPEGQF 737
Cdd:cd14918 558 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQF 637
|
650 660 670
....*....|....*....|....*....|.
gi 163644331 738 IDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14918 638 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
99-768 |
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: 1122.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFASIAAGGSAKKEGA---EKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASG 255
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAasgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 256 KLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGETTVASINDGEELLATDEAF 335
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 336 DVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQN 415
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 416 VQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVL 495
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 496 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRAIKGKPESH 575
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 576 FSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFAnyAGTESDNGKGGKGGGSKKKGSSFQTVSALHRE 655
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFS--GGQTAEAEGGGGKKGGKKKGSSFQTVSALFRE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 656 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIPEG 735
Cdd:cd14915 559 NLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 638
|
650 660 670
....*....|....*....|....*....|...
gi 163644331 736 QFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14915 639 QFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-768 |
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: 1121.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFASIAAGGSAKKE---GAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASG 255
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEeatSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 256 KLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGETTVASINDGEELLATDEAF 335
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 336 DVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQN 415
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 416 VQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVL 495
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 496 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRAIKGKPESH 575
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 576 FSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDngKGGKGGGSKKKGSSFQTVSALHRE 655
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAE--EGGGKKGGKKKGSSFQTVSALFRE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 656 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIPEG 735
Cdd:cd14910 559 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 638
|
650 660 670
....*....|....*....|....*....|...
gi 163644331 736 QFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14910 639 QFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-768 |
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: 1105.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFASIAAGGSAKKE---GAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASG 255
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEeitSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 256 KLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGETTVASINDGEELLATDEAF 335
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 336 DVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQN 415
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 416 VQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVL 495
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 496 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRAIKGKPESH 575
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 576 FSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNGKGGKGGGSKKKGSSFQTVSALHRE 655
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 656 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIPEG 735
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 163644331 736 QFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-768 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1055.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 87 IEDMAMFTFLHEPAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 167 TDRENQSILITGESGAGKTVNTKRVIQYFASIAAGGSakkegAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKF 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGS-----AGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 247 IRIHFGASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITnNPYDYAYISQ-GETTVASINDG 325
Cdd:pfam00063 156 IEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLSQsGCYTIDGIDDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 326 EELLATDEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKV 405
Cdd:pfam00063 235 EEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 406 GNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQ-PRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKL 484
Cdd:pfam00063 315 GRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 485 QQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKASDSTFKAKLYDNHlGKSNNFQ 563
Cdd:pfam00063 395 QQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 564 KPRAIKgkpESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNGKGGKGGGS-KKK 642
Cdd:pfam00063 473 KPRLQG---ETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTPkRTK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 643 GSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQ 722
Cdd:pfam00063 550 KKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQ 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 163644331 723 RYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:pfam00063 630 RYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-768 |
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: 1048.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFASIAAGGSAKKegaeKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLA 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKK----KLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 259 SADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKpELLEMLLITNNPYDYAYISQGETTVASINDGEELLATDEAFDVL 338
Cdd:cd14929 157 SADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 339 GFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQ 418
Cdd:cd14929 236 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 419 VYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQE 498
Cdd:cd14929 316 VTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 499 EYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRAIKGKPESHFSL 578
Cdd:cd14929 396 EYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHFEL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 579 VHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESdngKGGKGGGSKKKGSSFQTVSALHRENLN 658
Cdd:cd14929 476 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDS---AIQFGEKKRKKGASFQTVASLHKENLN 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 659 KLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIPEGQFI 738
Cdd:cd14929 553 KLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFV 632
|
650 660 670
....*....|....*....|....*....|
gi 163644331 739 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14929 633 SSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-780 |
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: 1012.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 80 NPPKFDKIEDMAMFTFLHEPAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISD 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 160 NAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASIAAGGsakkegaEKKGTLEDQIIQANPALEAFGNAKTIRNDN 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSN-------TEVGSVEDQILESNPILEAFGNAKTLRNNN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 240 SSRFGKFIRIHFGASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNnPYDYAYISQGET-T 318
Cdd:smart00242 154 SSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGGClT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 319 VASINDGEELLATDEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEA-DGTEDGDKVAYLMGLNSADLIKG 397
Cdd:smart00242 233 VDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTvKDKEELSNAAELLGVDPEELEKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 398 LCHPRVKVGNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCI 477
Cdd:smart00242 313 LTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 478 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKASDSTFKAKLYdNHL 556
Cdd:smart00242 393 NYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN-QHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 557 GKSNNFQKPRaikGKPESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESdngkggkg 636
Cdd:smart00242 471 KKHPHFSKPK---KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAG-------- 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 637 ggskkKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRIL 716
Cdd:smart00242 540 -----SKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLP 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 163644331 717 YGDFKQRYRILNPAAIPEGQFiDSRKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGQLEEMRD 780
Cdd:smart00242 615 FDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
100-768 |
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: 1007.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 180 SGAGKTVNTKRVIQYFASIaagGSAKKEGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLAS 259
Cdd:cd14934 82 SGAGKTENTKKVIQYFANI---GGTGKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 260 ADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGETTVASINDGEELLATDEAFDVLG 339
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 340 FTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQV 419
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 420 YYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQEE 499
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 500 YKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRAIKGK-PESHFSL 578
Cdd:cd14934 399 YKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAHFEL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 579 VHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESdngkggkgGGSKKKGSSFQTVSALHRENLN 658
Cdd:cd14934 479 VHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAG--------SKKQKRGSSFMTVSNFYREQLN 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 659 KLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIPEGqFI 738
Cdd:cd14934 551 KLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FV 629
|
650 660 670
....*....|....*....|....*....|
gi 163644331 739 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14934 630 DNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-768 |
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: 1004.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFASIAAGgSAKKEGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLA 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGAS-KKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 259 SADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGETTVASINDGEELLATDEAFDVL 338
Cdd:cd14909 160 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 339 GFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQ 418
Cdd:cd14909 240 GFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 419 VYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQE 498
Cdd:cd14909 320 VTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 499 EYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRAIK-GKPESHFS 577
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAAHFA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 578 LVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDngKGGKGGGSKKKGSSFQTVSALHRENL 657
Cdd:cd14909 480 IAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGG--GEQAKGGRGKKGGGFATVSSAYKEQL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 658 NKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIPEGQf 737
Cdd:cd14909 558 NSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE- 636
|
650 660 670
....*....|....*....|....*....|.
gi 163644331 738 iDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14909 637 -DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1438 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 845.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 36 ECFVPDPDEEYVKASIVSREGDKVTVQTEKRK----TVTVKEADIH--PQNPPKFDKIEDMAMFTFLHEPAVLFNLKERY 109
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKEAFNKGKVTEEGKKedgeSVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 110 AAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTK 189
Cdd:COG5022 91 NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 190 RVIQYFASIAAGGSakkegaEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLASADIETYLLEK 269
Cdd:COG5022 171 RIMQYLASVTSSST------VEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 270 SRVTFQLKAERDYHIFYQILSQrKPELLEMLLITNNPYDYAYISQGE-TTVASINDGEELLATDEAFDVLGFTQEEKNGI 348
Cdd:COG5022 245 SRVVHQNKNERNYHIFYQLLAG-DPEELKKLLLLQNPKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDEEEQDQI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 349 YKLIGAIMHFGNMKFKqKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQVYYAIGALAK 428
Cdd:COG5022 324 FKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 429 SVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWE 508
Cdd:COG5022 403 ALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWS 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 509 FIDFgMDLQACIDLIEK--PMGIMSILEEECMFPKASDSTFKAKLYDN-HLGKSNNFQKPRAIKGKpeshFSLVHYAGTV 585
Cdd:COG5022 483 FIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVKHYAGDV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 586 DYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNgkggkgggskkkgsSFQTVSALHRENLNKLMTNLR 665
Cdd:COG5022 558 EYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIESKG--------------RFPTLGSRFKESLNSLMSTLN 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 666 STHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIPEGQFI---DSRK 742
Cdd:COG5022 624 STQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDTKN 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 743 GAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGQLEEMRDDRLSLIISGIQARSRGLLARVEFQKIVERRDALLVIQWNVRA 822
Cdd:COG5022 704 AVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRL 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 823 FMGVKNWPWMKLFFKIKPLLKSAEAEKEMAnmkdEFAKLKEAYAKSEARRKELEEKMvsllqekndlqlqvqaEQDNLCD 902
Cdd:COG5022 784 RRLVDYELKWRLFIKLQPLLSLLGSRKEYR----SYLACIIKLQKTIKREKKLRETE----------------EVEFSLK 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 903 AEErcdqlIKNKIQLEAKAKELTERLEDEEEMnAELTAKKRKLEDECSELKKDIDDLE-LTLAKVEKEKHATENKVKNLT 981
Cdd:COG5022 844 AEV-----LIQKFGRSLKAKKRFSLLKKETIY-LQSAQRVELAERQLQELKIDVKSISsLKLVNLELESEIIELKKSLSS 917
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 982 EEMAALDDIIAKLTKEKKALQEAH---QQTLDdlQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLE 1058
Cdd:COG5022 918 DLIENLEFKTELIARLKKLLNNIDleeGPSIE--YVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELK 995
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1059 G---DLKLTQESLMDLENDKQQLEERLKKKDFEISqlNGKIEDEQTICIQLQKKLKELQaRIEELEEELEAERAARAKVE 1135
Cdd:COG5022 996 NfkkELAELSKQYGALQESTKQLKELPVEVAELQS--ASKIISSESTELSILKPLQKLK-GLLLLENNQLQARYKALKLR 1072
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1136 KQRADLARELEEISERLE-EAGGATAAQIEMNKKREAEFQKLRRDLeeatlqheaTAATLRKKQADSVAELGEQ-IDNLQ 1213
Cdd:COG5022 1073 RENSLLDDKQLYQLESTEnLLKTINVKDLEVTNRNLVKPANVLQFI---------VAQMIKLNLLQEISKFLSQlVNTLE 1143
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1214 RVKQKLekEKSELRLELDDVVSNMEHVVKTKAnLEKMTRSLEDQMNEYKTKYEEGQRCIND-FTMQKSKLQSENGELSRQ 1292
Cdd:COG5022 1144 PVFQKL--SVLQLELDGLFWEANLEALPSPPP-FAALSEKRLYQSALYDEKSKLSSSEVNDlKNELIALFSKIFSGWPRG 1220
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1293 LEEKDSL--VSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEE-EQEAKAELQR-GMSKANS 1368
Cdd:COG5022 1221 DKLKKLIseGWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVlPATINSLLQYiNVGLFNA 1300
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1369 EVAQ---WRTKYETDAIQRTEELEEAKKK-----LAQRLQETEEAVEAVNAKCSSLEKTKHRLQ-------NEIEDLMVD 1433
Cdd:COG5022 1301 LRTKassLRWKSATEVNYNSEELDDWCREfeisdVDEELEELIQAVKVLQLLKDDLNKLDELLDacyslnpAEIQNLKSR 1380
|
....*
gi 163644331 1434 LERSN 1438
Cdd:COG5022 1381 YDPAD 1385
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-768 |
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: 836.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKR-SEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 178 GESGAGKTVNTKRVIQYFASIAAGGSAKkeGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKL 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSK--SSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 258 ASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLIT---NNPYDYAYISQGE-TTVASINDGEELLATDE 333
Cdd:cd00124 159 VGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLElllSYYYLNDYLNSSGcDRIDGVDDAEEFQELLD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 334 AFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREE--QAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVT 411
Cdd:cd00124 239 ALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETIT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 412 KGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSL--DTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFN 489
Cdd:cd00124 319 KPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 490 HHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRai 568
Cdd:cd00124 399 QHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR-- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 569 kgKPESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVkllsmlfanyagtesdngkggkgggskkkgssfqt 648
Cdd:cd00124 476 --KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ----------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 649 vsalHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILN 728
Cdd:cd00124 519 ----FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILA 594
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 163644331 729 PAAiPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd00124 595 PGA-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-768 |
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: 794.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 180 SGAGKTVNTKRVIQYFASIAAGGSAKKEGAEKK--------GTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHF 251
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPavnpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 252 GASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLItNNPYDYAYISQGETTVASINDGEELLAT 331
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 332 DEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVT 411
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 412 KGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLD-TKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNH 490
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 491 HMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLgksnnfQKPRAIKG 570
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMKT 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 571 --KPESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLF--ANYAGTeSDNGKGGKGGGSKKKGSSF 646
Cdd:cd14911 475 dfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWkdAEIVGM-AQQALTDTQFGARTRKGMF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 647 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRI 726
Cdd:cd14911 554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 163644331 727 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14911 634 LTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-768 |
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: 767.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 180 SGAGKTVNTKRVIQYFASIAAGGSAKKEGAeKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLAS 259
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVASSHKGRKDHN-IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 260 ADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLItnNPYD-YAYISQGETTVASINDGEELLATDEAFDVL 338
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL--EGFNnYRFLSNGYIPIPGQQDKDNFQETMEAMHIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 339 GFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQ 418
Cdd:cd14920 239 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 419 VYYAIGALAKSVYEKMFLWMVVRINQSLDTKQpRQ--YFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLE 496
Cdd:cd14920 319 ADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 497 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDSTFKAKLyDNHLGKSNNFQKPRAIKGKPE 573
Cdd:cd14920 398 QEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLKDKAD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 574 shFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGT-----ESDNGKGGKGGGSKKKGSSFQT 648
Cdd:cd14920 477 --FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIvgldqVTGMTETAFGSAYKTKKGMFRT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 649 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILN 728
Cdd:cd14920 555 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 163644331 729 PAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14920 635 PNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
100-768 |
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: 719.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 180 SGAGKTVNTKRVIQYFASIAAGGSAKKEGAE---KKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGK 256
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 257 LASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPyDYAYISQGETTVASINDGEELLATDEAFD 336
Cdd:cd14932 162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYS-KYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 337 VLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNV 416
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 417 QQVYYAIGALAKSVYEKMFLWMVVRINQSLD-TKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVL 495
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 496 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDSTFKAKLYdNHLGKSNNFQKPRaiKGKP 572
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPK--KLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 573 ESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANY---AGTES-DNGKGGKGGGSKKKGSSFQT 648
Cdd:cd14932 478 DADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdriVGLDKvAGMGESLHGAFKTRKGMFRT 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 649 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILN 728
Cdd:cd14932 558 VGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 637
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 163644331 729 PAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14932 638 PNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
99-768 |
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: 698.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 178 GESGAGKTVNTKRVIQYFASIaaGGSAKKEGAekkgtLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKL 257
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATV--GGSSSGETQ-----VEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 258 ASADIETYLLEKSRVTFQLKAERDYHIFYQILSQR-KPELLEMLLITNNpyDYAYISQGE-TTVASINDGEELLATDEAF 335
Cdd:cd01380 154 IGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKELHLGSAE--DFFYTNQGGsPVIDGVDDAAEFEETRKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 336 DVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQN 415
Cdd:cd01380 232 TLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 416 VQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQP--RQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMF 493
Cdd:cd01380 312 LQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 494 VLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNN-FQKPRAIKGKp 572
Cdd:cd01380 392 KLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKhFKKPRFSNTA- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 573 eshFSLVHYAGTVDYNINNWLVKNKDPLNEtvvglfqkstvKLLSMLfanyagTESDNGKggkgggskkkgssfQTVSAL 652
Cdd:cd01380 470 ---FIVKHFADDVEYQVEGFLEKNRDTVSE-----------EHLNVL------KASKNRK--------------KTVGSQ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 653 HRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAi 732
Cdd:cd01380 516 FRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK- 594
|
650 660 670
....*....|....*....|....*....|....*.
gi 163644331 733 pEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01380 595 -EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
100-768 |
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: 682.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 180 SGAGKTVNTKRVIQYFASIAAGGSAKKEgAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLAS 259
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVASSHKGKKD-TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 260 ADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPyDYAYISQGETTVASINDGEELLATDEAFDVLG 339
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFN-NYTFLSNGFVPIPAAQDDEMFQETLEAMSIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 340 FTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQV 419
Cdd:cd14921 240 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 420 YYAIGALAKSVYEKMFLWMVVRINQSLD-TKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQE 498
Cdd:cd14921 320 DFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 499 EYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDSTFKAKLYDNHlGKSNNFQKPRAIKGKPEsh 575
Cdd:cd14921 400 EYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKDKTE-- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 576 FSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANY---AGTE--SDNGKGGKGGGSKKKGSSFQTVS 650
Cdd:cd14921 477 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdriVGLDqmAKMTESSLPSASKTKKGMFRTVG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 651 ALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPA 730
Cdd:cd14921 557 QLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 636
|
650 660 670
....*....|....*....|....*....|....*...
gi 163644331 731 AIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14921 637 AIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 681.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 180 SGAGKTVNTKRVIQYFASIAAGGSAKKEgaekKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLAS 259
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVASSHKSKKD----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 260 ADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLItnNPYD-YAYISQGETTVASINDGEELLATDEAFDVL 338
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 339 GFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQ 418
Cdd:cd14919 236 GIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 419 VYYAIGALAKSVYEKMFLWMVVRINQSLD-TKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQ 497
Cdd:cd14919 316 ADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 498 EEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDSTFKAKLYDNHlGKSNNFQKPRAIKGKPEs 574
Cdd:cd14919 396 EEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDKAD- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 575 hFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNGKGGKGGGS-----KKKGSSFQTV 649
Cdd:cd14919 474 -FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETAlpgafKTRKGMFRTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 650 SALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNP 729
Cdd:cd14919 553 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 632
|
650 660 670
....*....|....*....|....*....|....*....
gi 163644331 730 AAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14919 633 NSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
100-768 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 679.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 180 SGAGKTVNTKRVIQYFASIAAGGSAKKE---GAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGK 256
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVASSHKTKKDqnsLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 257 LASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPyDYAYISQGETTVASINDGEELLATDEAFD 336
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYN-NYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 337 VLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNV 416
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 417 QQVYYAIGALAKSVYEKMFLWMVVRINQSLD-TKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVL 495
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 496 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDSTFKAKLYDNHlGKSNNFQKPRaiKGKP 572
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPK--KLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 573 ESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANY---AGTESDNGKGGKGGGSKKKGSSFQTV 649
Cdd:cd15896 478 EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVdriVGLDKVSGMSEMPGAFKTRKGMFRTV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 650 SALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNP 729
Cdd:cd15896 558 GQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 637
|
650 660 670
....*....|....*....|....*....|....*....
gi 163644331 730 AAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd15896 638 NAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 667.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 180 SGAGKTVNTKRVIQYFASIAAGGSAKKEGAeKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLAS 259
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVASSPKGRKEPG-VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 260 ADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYdYAYISQGETTVASiNDGEELLATDEAFDVLG 339
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 340 FTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQV 419
Cdd:cd14930 239 FSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 420 YYAIGALAKSVYEKMFLWMVVRINQSLDtKQPRQ--YFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQ 497
Cdd:cd14930 319 DFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 498 EEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDSTFKAKLYDNHlGKSNNFQKPRAIKGKPEs 574
Cdd:cd14930 398 EEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHLRDQAD- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 575 hFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANY---AGTESDNGKGGKGGGSKKKGSSFQTVSA 651
Cdd:cd14930 476 -FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVegiVGLEQVSSLGDGPPGGRPRRGMFRTVGQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 652 LHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAA 731
Cdd:cd14930 555 LYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 634
|
650 660 670
....*....|....*....|....*....|....*..
gi 163644331 732 IPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14930 635 IPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-768 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 650.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 180 SGAGKTVNTKRVIQYFASIAAGGSAKKEGAEkkgtleDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLAS 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVERVK------DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 260 ADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGETTVASINDGEELLATDEAFDVLG 339
Cdd:cd01378 156 GHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 340 FTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEdGDKVAYLMGLNSADLIKGLCHPRVKVGNEW---VTKGQNV 416
Cdd:cd01378 236 FTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISDTSV-LDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 417 QQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQ-YFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHhmFVL 495
Cdd:cd01378 315 EQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE--LTL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 496 --EQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFP-KASDSTFKAKLyDNHLGKSNNFQKPRAIKGK 571
Cdd:cd01378 393 kaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHFEL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 572 PESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANyaGTESDNGKGGKgggskkkgssfqTVSA 651
Cdd:cd01378 471 RRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE--GVDLDSKKRPP------------TAGT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 652 LHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAA 731
Cdd:cd01378 537 KFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKT 616
|
650 660 670
....*....|....*....|....*....|....*..
gi 163644331 732 IPEGQFIDsRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01378 617 WPAWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
100-768 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 632.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 180 SGAGKTVNTKRVIQYFASIAAggsakkegaeKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLAS 259
Cdd:cd01381 82 SGAGKTESTKLILQYLAAISG----------QHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 260 ADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITnNPYDYAYISQGETTVAS-INDGEELLATDEAFDVL 338
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG-DASDYYYLTQGNCLTCEgRDDAAEFADIRSAMKVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 339 GFTQEEKNGIYKLIGAIMHFGNMKFKQKQRE--EQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNV 416
Cdd:cd01381 231 MFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 417 QQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYF---IGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMF 493
Cdd:cd01381 311 EQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 494 VLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDSTFKAKLYDNHlGKSNNFQKPRAikgKP 572
Cdd:cd01381 391 KLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKPKS---DL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 573 ESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNGKGGkgggskkkgssfQTVSAL 652
Cdd:cd01381 466 NTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKS------------PTLSSQ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 653 HRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPaAI 732
Cdd:cd01381 534 FRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP-GI 612
|
650 660 670
....*....|....*....|....*....|....*.
gi 163644331 733 PEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01381 613 PPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
99-768 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 624.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRgkKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFASIAAGGSAkkegaekkgtLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLA 258
Cdd:cd01383 79 ESGAGKTETAKIAMQYLAALGGGSSG----------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKIC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 259 SADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITnNPYDYAYISQGET-TVASINDGEELLATDEAFDV 337
Cdd:cd01383 149 GAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLK-SASEYKYLNQSNClTIDGVDDAKKFHELKEALDT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 338 LGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQ 417
Cdd:cd01383 228 VGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 418 QVYYAIGALAKSVYEKMFLWMVVRINQSLDT-KQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLE 496
Cdd:cd01383 308 QAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 497 QEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDSTFKAKLyDNHLgKSNnfqkpRAIKGKPESH 575
Cdd:cd01383 388 QEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHL-KSN-----SCFKGERGGA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 576 FSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLsMLFAnyAGTESDNGKGGKGGGSKKKGSSFQTVSALHRE 655
Cdd:cd01383 460 FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLP-QLFA--SKMLDASRKALPLTKASGSDSQKQSVATKFKG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 656 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIPEG 735
Cdd:cd01383 537 QLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSAS 616
|
650 660 670
....*....|....*....|....*....|...
gi 163644331 736 QFIDSRKGAekLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01383 617 QDPLSTSVA--ILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-768 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 607.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 180 SGAGKTVNTKRVIQYFASIAAGGSakkegaekkgTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLAS 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS----------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 260 ADIETYLLEKSRVTFQLKAERDYHIFYQILS--QRKPELLEmLLITNNPYDYAYISQ-GETTVASINDGEELLATDEAFD 336
Cdd:cd14883 152 AIIQDYLLEQSRITFQAPGERNYHVFYQLLAgaKHSKELKE-KLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRLAMN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 337 VLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAE-ADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQN 415
Cdd:cd14883 231 VLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 416 VQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVL 495
Cdd:cd14883 311 VQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 496 EQEEYKKEGIEWEFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKASDSTFKAKLYDNHlGKSNNFQKPRaiKGKPES 574
Cdd:cd14883 391 EQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPD--RRRWKT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 575 HFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFA--NYAGTESDNGKGGKGGGSKKKGSSFQTVSAL 652
Cdd:cd14883 467 EFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTypDLLALTGLSISLGGDTTSRGTSKGKPTVGDT 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 653 HRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAI 732
Cdd:cd14883 547 FKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRAR 626
|
650 660 670
....*....|....*....|....*....|....*..
gi 163644331 733 PEGQfiDSRKGAEK-LLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14883 627 SADH--KETCGAVRaLMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-768 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 587.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 178 GESGAGKTVNTKRVIQYFASIaaGGSAKKEGAekkgTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKL 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYM--GGRAVTEGR----SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 258 ASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLItNNPYDYAYISQGET-TVASINDGEELLATDEAFD 336
Cdd:cd01384 155 SGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKL-KDPKQFHYLNQSKCfELDGVDDAEEYRATRRAMD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 337 VLGFTQEEKNGIYKLIGAIMHFGNMKFKqkqREEQAEADGTEDG------DKVAYLMGLNSADLIKGLCHPRVKVGNEWV 410
Cdd:cd01384 234 VVGISEEEQDAIFRVVAAILHLGNIEFS---KGEEDDSSVPKDEksefhlKAAAELLMCDEKALEDALCKRVIVTPDGII 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 411 TKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNH 490
Cdd:cd01384 311 TKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 491 HMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDSTFKAKLYDNhLGKSNNFQKPRaik 569
Cdd:cd01384 391 HVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPK--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 570 gKPESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNgkggkgggskkkGSSFQTV 649
Cdd:cd01384 466 -LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGTSS------------SSKFSSI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 650 SALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNP 729
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAP 612
|
650 660 670
....*....|....*....|....*....|....*....
gi 163644331 730 AAIpeGQFIDSRKGAEKLLGSLDIdhNQYKFGHTKVFFK 768
Cdd:cd01384 613 EVL--KGSDDEKAACKKILEKAGL--KGYQIGKTKVFLR 647
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-768 |
8.50e-169 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 529.73 E-value: 8.50e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFASIAagGSAkkegaekkGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLA 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVA--GST--------NGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRIC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 259 SADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLlitNNPYDYAYISQGET-TVASINDGEELLATDEAFDV 337
Cdd:cd14872 151 GASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGW---GSSAAYGYLSLSGCiEVEGVDDVADFEEVVLAMEQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 338 LGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGD---KVAYLMGLNSADLIKGLCHPRVKVgnewvtKGQ 414
Cdd:cd14872 228 LGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDvlkEVATLLGVDAATLEEALTSRLMEI------KGC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 415 NV-------QQVYYAIGALAKSVYEKMFLWMVVRINQSLD-TKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQ 486
Cdd:cd14872 302 DPtripltpAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 487 FFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSnnFQKP 565
Cdd:cd14872 382 HFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS--TFVY 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 566 RAIKGKPEShFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNGKggkgggskkkgss 645
Cdd:cd14872 459 AEVRTSRTE-FIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGDQKTSKV------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 646 fqTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYR 725
Cdd:cd14872 525 --TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYR 602
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 163644331 726 ILnPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14872 603 FL-VKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-768 |
1.99e-168 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 529.35 E-value: 1.99e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 178 GESGAGKTVNTKRVIQYFASIAAGgsakkegaekkgtLED----QIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGA 253
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGG-------------LNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 254 SGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLlitNNPYDYAYIsqGETTVASI---NDGEELLA 330
Cdd:cd14903 148 NGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFL---DSANECAYT--GANKTIKIegmSDRKHFAR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 331 TDEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAE--ADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNE 408
Cdd:cd14903 223 TKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 409 WVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFF 488
Cdd:cd14903 303 VYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 489 NHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRAI 568
Cdd:cd14903 383 TQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 569 KgkpeSHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNGKGGKGGGSKKKGSSF-- 646
Cdd:cd14903 462 R----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALtt 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 647 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRI 726
Cdd:cd14903 538 TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 163644331 727 LNPAAipEGQFIDSRKGAEKLLGSLDIDH-NQYKFGHTKVFFK 768
Cdd:cd14903 618 FLPEG--RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
100-768 |
1.30e-167 |
|
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: 527.42 E-value: 1.30e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYML----TDRENQSI 174
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIqsgvLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 175 LITGESGAGKTVNTKRVIQYFASIAAG--------GSAKKEGAEKK-GTLEDQIIQANPALEAFGNAKTIRNDNSSRFGK 245
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARITSGfaqgasgeGEAASEAIEQTlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 246 FIRIHFGASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNnPYDYAYISQGETTVASINDG 325
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 326 EELLATDEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDG-DKVAYLMGLNSADLIKGLCHPRVK 404
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTLQSlKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 405 VGNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKL 484
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 485 QQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILE--EECMFPKAS--DSTFKAKLYDNHLGKS 559
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgKVNGKPGIFItlDDCWRFKGEeaNKKFVSQLHASFGRKS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 560 NNFQKPRAIKGKP---------ESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMlfanyagtesdn 630
Cdd:cd14890 480 GSGGTRRGSSQHPhfvhpkfdaDKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIREV------------ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 631 gkggkgggskkkgssfqTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKG 710
Cdd:cd14890 548 -----------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQG 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 163644331 711 FPNRILYGDFKQRYRILNPAAIPEGQFIdsrkgaEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14890 611 FALREEHDSFFYDFQVLLPTAENIEQLV------AVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
94-768 |
7.52e-167 |
|
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: 524.51 E-value: 7.52e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 94 TFLHepavlfNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQ 172
Cdd:cd01382 2 TLLN------NIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 173 SILITGESGAGKTVNTKRVIQYFASIaaGGSakkegaeKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFG 252
Cdd:cd01382 76 SIIVSGESGAGKTESTKYILRYLTES--WGS-------GAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 253 ASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLitnnpydyayisqgetTVASINDGEELLATD 332
Cdd:cd01382 147 EKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 333 EAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDK----VAYLMGLNSADLIKGLCHpRVKVGNE 408
Cdd:cd01382 211 KAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKSEQsleyAAELLGLDQDELRVSLTT-RVMQTTR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 409 WVTKGQ------NVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQpRQYFIGVLDIAGFEIFDFNTFEQLCINFTNE 482
Cdd:cd01382 290 GGAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 483 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDSTFKAKLYDNHLgksNN 561
Cdd:cd01382 369 KLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK---NH 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 562 F--QKPRaiKGKPESH--------FSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNg 631
Cdd:cd01382 445 FrlSIPR--KSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDS- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 632 kggkggGSKKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGF 711
Cdd:cd01382 522 ------KQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGF 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 163644331 712 PNRILYGDFKQRYRILNPAAIPEgqfIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01382 596 PSRTSFHDLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-768 |
1.18e-165 |
|
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: 522.33 E-value: 1.18e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNQEVVVAYRgKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 178 GESGAGKTVNTKRVIQYFASiaAGGSAKKegaeKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHF------ 251
Cdd:cd14888 80 GESGAGKTESTKYVMKFLAC--AGSEDIK----KRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklksk 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 252 ---GASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLIT-NNPYDYAYISQ------------- 314
Cdd:cd14888 154 rmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEeNDEKLAKGADAkpisidmssfeph 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 315 ---------GETTVASINDGEELLATDEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQA---EADGTEDGDK 382
Cdd:cd14888 234 lkfryltksSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTDDLEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 383 VAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLD-TKQPRQYFIGVLDI 461
Cdd:cd14888 314 VASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGVLDI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 462 AGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLI-EKPMGIMSILEEECMFP 540
Cdd:cd14888 394 FGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEECFVP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 541 KASDSTFKAKLYDNHLGkSNNFQKpraIKGKPEShFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLF 620
Cdd:cd14888 473 GGKDQGLCNKLCQKHKG-HKRFDV---VKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLF 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 621 ANYAGTESDngkggkgggSKKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGV 700
Cdd:cd14888 548 SAYLRRGTD---------GNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGV 618
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163644331 701 LEGIRICRKGFPNRILYGDFKQRYRILNPaaipegqfidsrkgaekllGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14888 619 LQAVQVSRAGYPVRLSHAEFYNDYRILLN-------------------GEGKKQLSIWAVGKTLCFFK 667
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1925 |
3.78e-165 |
|
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: 535.14 E-value: 3.78e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 848 EKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAKELTER 927
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 928 LEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQ 1007
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1008 TLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDF 1087
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1088 EISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATAAQIEMNK 1167
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1168 KREAEFQKLRRDLEEATLQHEATAATLRKKQADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNMEHVVKTKANL 1247
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1248 EKMTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKA 1327
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1328 KSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQETEEAVE 1407
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1408 AVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKLK 1487
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1488 NSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEF 1567
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1568 SQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKS 1647
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1648 VHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLN 1727
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1728 QKKKLETDISQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAM 1807
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1808 KGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKAYKRAAEEA 1887
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 163644331 1888 EEQANTNLSKFRKIQHELDEAEERADIAESQVNKLRAK 1925
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
100-768 |
7.11e-164 |
|
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: 517.00 E-value: 7.11e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 180 SGAGKTVNTKRVIQYFASIAAGGSAkkegaekkgTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFgASGKLAS 259
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVNQRRNN---------LVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 260 ADIETYLLEKSRVTFQLKAERDYHIFYQIL-----SQRKPELLEmllitnNPYDYAYISQGETT-VASINDGEELLATDE 333
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLaglpaQLRQKYGLQ------EAEKYFYLNQGGNCeIAGKSDADDFRRLLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 334 AFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQRE---EQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWV 410
Cdd:cd01387 226 AMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 411 TKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNH 490
Cdd:cd01387 306 FTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 491 HMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDSTFKAKLYDNHlGKSNNFQKPRAik 569
Cdd:cd01387 386 HVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPRM-- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 570 GKPEshFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNGKGGKGGGSKKKGSSFQTV 649
Cdd:cd01387 462 PLPE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGKGRFVTMKPRTPTV 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 650 SALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNP 729
Cdd:cd01387 540 AARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVA 619
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 163644331 730 AAIPEGQFIDSRkgaEKLLGSLD--IDHNQYKFGHTKVFFK 768
Cdd:cd01387 620 LKLPRPAPGDMC---VSLLSRLCtvTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
105-768 |
3.44e-158 |
|
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: 500.65 E-value: 3.44e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 105 LKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGK 184
Cdd:cd01379 7 LQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGESGAGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 185 TVNTKRVIQYFASIaaggsakkeGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLASADIET 264
Cdd:cd01379 87 TESANLLVQQLTVL---------GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 265 YLLEKSRVTFQLKAERDYHIFYQI---LSQRKpELLEMLLITNNPYDYAYISQGETTVASINDG--EELLATDEAFDVLG 339
Cdd:cd01379 158 YLLEKSRVVHQAIGERNFHIFYYIyagLAEDK-KLAKYKLPENKPPRYLQNDGLTVQDIVNNSGnrEKFEEIEQCFKVIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 340 FTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQ----AEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQN 415
Cdd:cd01379 237 FTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 416 VQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQP---RQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHM 492
Cdd:cd01379 317 VEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSasdEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 493 FVLEQEEYKKEGIEWEFIDFGmDLQACID-LIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHlgKSNNFQKPRAIkgk 571
Cdd:cd01379 397 FAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYWRPKSN--- 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 572 pESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSmlfanyagtesdngkggkgggskkkgssfQTVSA 651
Cdd:cd01379 471 -ALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR-----------------------------QTVAT 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 652 LHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRIL--NP 729
Cdd:cd01379 521 YFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLafKW 600
|
650 660 670
....*....|....*....|....*....|....*....
gi 163644331 730 AAIPEGqfidSRKGAEKLLGSLDIDHnqYKFGHTKVFFK 768
Cdd:cd01379 601 NEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-766 |
3.70e-155 |
|
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: 493.15 E-value: 3.70e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAY------RGKKRSEAPPHIFSISDNAYQYMLTDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 171 --NQSILITGESGAGKTVNTKRVIQYFASIAAGGSAKKEGAEKKgTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIR 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERE-NVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 249 IHFGASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPyDYAYISQGETTVA--SINDGE 326
Cdd:cd14901 160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVE-EYKYLNSSQCYDRrdGVDDSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 327 ELLATDEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREeqAEADGTEDGDKVAY---LMGLNSADLIKGLCHPRV 403
Cdd:cd14901 239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGE--GGTFSMSSLANVRAacdLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 404 KVGNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQP--RQYFIGVLDIAGFEIFDFNTFEQLCINFTN 481
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 482 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDlQACIDLIE-KPMGIMSILEEECMFPKASDSTFKAKLYDNhLGKSN 560
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 561 NFQKPRAIKGKpeSHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSmlfanyagtesdngkggkgggsk 640
Cdd:cd14901 475 SFSVSKLQQGK--RQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS----------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 641 kkgssfQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 720
Cdd:cd14901 530 ------STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAF 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 163644331 721 KQRYRILNPAAIPEGQFIDSRKGAEKLLGSLDI----DHNQYKFGHTKVF 766
Cdd:cd14901 604 VHTYSCLAPDGASDTWKVNELAERLMSQLQHSElnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
102-768 |
8.28e-155 |
|
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: 493.43 E-value: 8.28e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 102 LFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESG 181
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 182 AGKTVNTKRVIQYFASIAAGGSAKkegaekkgTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLASAD 261
Cdd:cd01385 84 SGKTESTNFLLHHLTALSQKGYGS--------GVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 262 IETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITnNPYDYAYISQGET-TVASINDGEELLATDEAFDVLGF 340
Cdd:cd01385 156 VEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLK-QPEDYHYLNQSDCyTLEGEDEKYEFERLKQAMEMVGF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 341 TQEEKNGIYKLIGAIMHFGNMKFKQK--QREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQ 418
Cdd:cd01385 235 LPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 419 VYYAIGALAKSVYEKMFLWMVVRINQSL----DTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFV 494
Cdd:cd01385 315 AIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 495 LEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDSTFKAKlYDNHLGKSNNFQKPRaikgKPE 573
Cdd:cd01385 395 LEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ----VME 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 574 SHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLF------------------ANYAGTESDNGKGGK 635
Cdd:cd01385 469 PAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIgidpvavfrwavlraffrAMAAFREAGRRRAQR 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 636 GGGSKKKGSSFQTVSALHREN--------------LNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVL 701
Cdd:cd01385 549 TAGHSLTLHDRTTKSLLHLHKkkkppsvsaqfqtsLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGML 628
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163644331 702 EGIRICRKGFPNRILYGDFKQRYRILnpaaIPEGQfIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01385 629 ETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
105-768 |
1.36e-152 |
|
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: 486.19 E-value: 1.36e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 105 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNqevVVAYRGKKRSEA-----PPHIFSISDNAYQYMLTDR----ENQSI 174
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYD---VPGFDSQRKEEAtasspPPHVFSIAERAYRAMKGVGkgqgTPQSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 175 LITGESGAGKTVNTKRVIQYFASI---AAGGSAKKEGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHF 251
Cdd:cd14892 84 VVSGESGAGKTEASKYIMKYLATAsklAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 252 GASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPyDYAYISQGE-TTVASINDGEELLA 330
Cdd:cd14892 164 NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAE-SFLFLNQGNcVEVDGVDDATEFKQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 331 TDEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQ--KQREEQAEADGTEDGDKVAYLMGLNSADLIKGLChPRVKVGne 408
Cdd:cd14892 243 LRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLV-TQTTST-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 409 wvTKGQNVQ------QVYYAIGALAKSVYEKMFLWMVVRINQS----------LDTKQPRQYFIGVLDIAGFEIFDFNTF 472
Cdd:cd14892 320 --ARGSVLEikltarEAKNALDALCKYLYGELFDWLISRINAChkqqtsgvtgGAASPTFSPFIGILDIFGFEIMPTNSF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 473 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEK-PMGIMSILEEECMFP-KASDSTFKAK 550
Cdd:cd14892 398 EQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 551 LYDNHLGKSNNFQKPRAikgkPESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTvkllsmlfanyagtesdn 630
Cdd:cd14892 477 YHQTHLDKHPHYAKPRF----ECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS------------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 631 gkggkgggskkkgsSFqtvsalhRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKG 710
Cdd:cd14892 535 --------------KF-------RTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREG 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 163644331 711 FPNRILYGDFKQRYRIL-----NPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14892 594 FPIRRQFEEFYEKFWPLarnkaGVAASPDACDATTARKKCEEIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
100-768 |
5.16e-150 |
|
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: 478.91 E-value: 5.16e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQyFASIAAGGSAKKEGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLA 258
Cdd:cd14873 82 ESGAGKTESTKLILK-FLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 259 SADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITnNPYDYAYISQ-GETTVASINDGEELLATDEAFDV 337
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLNQsGCVEDKTISDQESFREVITAMEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 338 LGFTQEEKNGIYKLIGAIMHFGNMKFkqkqreeqAEADGTEDGDKVAY-----LMGLNSADLIKGLCHPRVKVGNEWVTK 412
Cdd:cd14873 240 MQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKTALgrsaeLLGLDPTQLTDALTQRSMFLRGEEILT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 413 GQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQyFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHM 492
Cdd:cd14873 312 PLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 493 FVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHlgkSNN--FQKPRAikg 570
Cdd:cd14873 391 FSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH---ANNhfYVKPRV--- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 571 kPESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFanyagtESDNGKGGKGGGSKKKGSSFQTVS 650
Cdd:cd14873 464 -AVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF------EHVSSRNNQDTLKCGSKHRRPTVS 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 651 ALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNP- 729
Cdd:cd14873 537 SQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRn 616
|
650 660 670
....*....|....*....|....*....|....*....
gi 163644331 730 AAIPEgqfiDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14873 617 LALPE----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
101-768 |
3.28e-146 |
|
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: 467.63 E-value: 3.28e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 101 VLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKK-RSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 180 SGAGKTVNTKRVIQYFASIAagGSAKkegaekkGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLAS 259
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKLS--PSDD-------SDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 260 ADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLItNNPYDYAYISQGETTVASINDGEELLATDEAFDVL- 338
Cdd:cd14897 154 AKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELEYYRQMFHDLt 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 339 ------GFTQEEKNGIYKLIGAIMHFGNMKFkqkqrEEQAEADGTEDGDK-----VAYLMGLNSADLIKGLCHPRVKVGN 407
Cdd:cd14897 233 nimkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTIRG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 408 EWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYF-----IGVLDIAGFEIFDFNTFEQLCINFTNE 482
Cdd:cd14897 308 ERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCINLSNE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 483 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDSTFKAKLyDNHLGKSNN 561
Cdd:cd14897 388 RLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 562 FQKPraIKGKPEshFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYagtesdngkggkgggskk 641
Cdd:cd14897 466 YVAS--PGNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY------------------ 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 642 kgssfqtvsalHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFK 721
Cdd:cd14897 524 -----------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFV 592
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 163644331 722 QRYRILNPAAIPegqfidSRKGAE-KLLGSLDIDHNQ-YKFGHTKVFFK 768
Cdd:cd14897 593 KRYKEICDFSNK------VRSDDLgKCQKILKTAGIKgYQFGKTKVFLK 635
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-768 |
6.75e-141 |
|
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: 453.63 E-value: 6.75e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 178 GESGAGKTVNTKRVIQYFASIAAGgsakkegaeKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKL 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGG---------RKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 258 ASADIETYLLEKSRVTFQLKAERDYHIFYQILSQ-RKPELLEMLLITNNPYDYAYISQGETTVASINDGEELLATDEAFD 336
Cdd:cd14904 152 IGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 337 VLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGtEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNV 416
Cdd:cd14904 232 LIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNG-SQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 417 QQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQY-FIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVL 495
Cdd:cd14904 311 VEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 496 EQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNH--LGKSNNFQKPRAIKgkpe 573
Cdd:cd14904 391 VEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR---- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 574 SHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNGKGGKGGGSKKkgssfQTVSALH 653
Cdd:cd14904 466 TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEGKSGKGTKAP-----KSLGSQF 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 654 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIP 733
Cdd:cd14904 541 KTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMH 620
|
650 660 670
....*....|....*....|....*....|....*.
gi 163644331 734 EGqfiDSRKGAEKLLGSLDIDHN-QYKFGHTKVFFK 768
Cdd:cd14904 621 SK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
101-768 |
1.03e-138 |
|
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: 447.94 E-value: 1.03e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 101 VLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNQEVVVAYRGK--------KRSEAPPHIFSISDNAYQYMLTDREN 171
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 172 QSILITGESGAGKTVNTKRVIQYFASIAA----------GGSAKKEGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSS 241
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltLTSSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 242 RFGKFIRIHFG-ASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNP--YDYAYISQGET- 317
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLsgDRYDYLKKSNCy 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 318 TVASINDGEELLATDEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQ--REEQAEADGTEDGDKVAYLMGLNSADLI 395
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 396 KGLCHPRVKVGNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSL--------DTKQPRQYFIGVLDIAGFEIF 467
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 468 DFNTFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF--IDFgMDLQACIDLIEK-PMGIMSILEEECMFPKASD 544
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 545 STFKAKLYDNHlGKSNNFQKPRAIKgkpESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFanya 624
Cdd:cd14907 482 EKLLNKIKKQH-KNNSKLIFPNKIN---KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF---- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 625 gTESDNGKGGKGGGSKKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGI 704
Cdd:cd14907 554 -SGEDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESI 632
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 163644331 705 RICRKGFPNRILYGDFKQRYRILNpaaipegqfidsrkgaekllgsldidhNQYKFGHTKVFFK 768
Cdd:cd14907 633 RVRKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
105-768 |
1.80e-138 |
|
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: 447.05 E-value: 1.80e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 105 LKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYML----TDRENQSILITGES 180
Cdd:cd14889 7 LKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVISGES 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 181 GAGKTVNTKRVIQYFASIAAGGSakkegaekkgTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFgASGKLASA 260
Cdd:cd14889 87 GAGKTESTKLLLRQIMELCRGNS----------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 261 DIETYLLEKSRVTFQLKAERDYHIFYQI---LSQRKPELLEMLlitnNPYDYAYISQG---ETTVASIndGEELLATDEA 334
Cdd:cd14889 156 KINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLL----DPGKYRYLNNGagcKREVQYW--KKKYDEVCNA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 335 FDVLGFTQEEKNGIYKLIGAIMHFGNMKFkQKQREEQAEADGTEDG--DKVAYLMGLNSADLIKGLCHPRVKVGNEWVTK 412
Cdd:cd14889 230 MDMVGFTEQEEVDMFTILAGILSLGNITF-EMDDDEALKVENDSNGwlKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 413 GQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLdtkQPRQYF------IGVLDIAGFEIFDFNTFEQLCINFTNEKLQQ 486
Cdd:cd14889 309 HHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQACINLANEQLQY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 487 FFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDL-IEKPMGIMSILEEECMFPKASDSTFKAKLyDNHLGKSNNFQKP 565
Cdd:cd14889 386 FFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGKS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 566 RAIKGKpeshFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFA---NYAGTESDNGKGGKGGGSKKK 642
Cdd:cd14889 464 RSKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTatrSRTGTLMPRAKLPQAGSDNFN 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 643 GSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQ 722
Cdd:cd14889 540 STRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAE 619
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 163644331 723 RYRIL-NPAAIPegqfiDSRKGAEKLLGSLDIdhNQYKFGHTKVFFK 768
Cdd:cd14889 620 RYKILlCEPALP-----GTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
101-733 |
2.08e-136 |
|
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: 440.13 E-value: 2.08e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 101 VLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNQEVVVAY-----------RGKKRSEAPPHIFSISDNAYQYM--- 165
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 166 -LTDRENQSILITGESGAGKTVNTKRVIQYFASIAAGGSAKKEGAEKKG-TLEDQIIQANPALEAFGNAKTIRNDNSSRF 243
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTsGIAAKVLQTNILLESFGNARTLRNDNSSRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 244 GKFIRIHFGASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILsqrkpellemllitnnpydyayISQGETTVASIN 323
Cdd:cd14900 163 GKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMA----------------------IGASEAARKRDM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 324 DGEELlatdEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDG-------DKVAYLMGLNSADLIK 396
Cdd:cd14900 221 YRRVM----DAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 397 GLCHPRVKVGNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSL-----DTKQPRQYFIGVLDIAGFEIFDFNT 471
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 472 FEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDSTFKAK 550
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLASK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 551 LYdNHLGKSNNFQKPRAIKGKpeSHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQkstvkllsmlfanYAGTesdn 630
Cdd:cd14900 456 LY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV-------------YGLQ---- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 631 gkggkgggskkkgssfqtvsalHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKG 710
Cdd:cd14900 516 ----------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAG 573
|
650 660
....*....|....*....|...
gi 163644331 711 FPNRILYGDFKQRYRILNPAAIP 733
Cdd:cd14900 574 FPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-729 |
2.75e-135 |
|
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: 438.96 E-value: 2.75e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYR--GKKRS---EAP----PHIFSISDNAYQYMLTD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 169 RENQSILITGESGAGKTVNTKRVIQYFASIAAGGS-AKKEGAE-KKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKF 246
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEgAPNEGEElGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 247 IRIHFGASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQIL------SQRKPELLEMLLITNN-PYDYAYISQGET-T 318
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeEHEKYEFHDGITGGLQlPNEFHYTGQGGApD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 319 VASINDGEELLATDEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAY---LMGLNSADLI 395
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 396 KGLCHPRVKVGNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSL--DTKQPRQYFIGVLDIAGFEIFDFNTFE 473
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 474 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFP-KASDSTFKAKL 551
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 552 YDNHLGKSNN-------FQKPRAIKGKpeSHFSLVHYAGTVDYNI-NNWLVKNKDPLNETVVGLFQKSTvkllsmlfany 623
Cdd:cd14908 480 YETYLPEKNQthsentrFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESGQ----------- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 624 agtesdngkggkgggskkkgssfqtvsaLHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEG 703
Cdd:cd14908 547 ----------------------------QFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEA 598
|
650 660
....*....|....*....|....*.
gi 163644331 704 IRICRKGFPNRILYGDFKQRYRILNP 729
Cdd:cd14908 599 VRVARSGYPVRLPHKDFFKRYRMLLP 624
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-768 |
6.31e-134 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 433.70 E-value: 6.31e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAA--WMIYTYSGLFCVTVNPYKWLPvyNQEVVvAYRGKKRSEAPPHIFSISDNAYQYMLTDRE---NQS 173
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDKS-DYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 174 ILITGESGAGKTVNTKRVIQYFASIAAGGSAKKEGAEKKG---------TLEDQIIQANPALEAFGNAKTIRNDNSSRFG 244
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSskkrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 245 KFIRIHFGASG-KLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITnNPYDYAYISQ-GETTVASI 322
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLL-SPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 323 NDGEELLATDEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKqKQREEQAEADGTEDGDK-----VAYLMGLNSADLIKG 397
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFD-EEDTSEGEAEIASESDKealatAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 398 LCHPRVKVGNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFD-FNTFEQLC 476
Cdd:cd14891 316 ITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 477 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLI-EKPMGIMSILEEECMFPKASDSTFKAKLYDNH 555
Cdd:cd14891 396 INYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 556 lGKSNNFQKPRAiKGKPEShFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMlfanyagtesdngkggk 635
Cdd:cd14891 475 -KRHPCFPRPHP-KDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSAKFSDQM----------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 636 gggskkkgssfqtvsalhrenlNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRI 715
Cdd:cd14891 535 ----------------------QELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRV 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 163644331 716 LYGDFKQRYRILNPAAI------PEGQFIdsrkgaEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14891 593 TYAELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-729 |
1.89e-132 |
|
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: 432.39 E-value: 1.89e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNQEVVVAYR--------GKKRSEAPPHIFSISDNAYQYML-TD 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 169 RENQSILITGESGAGKTVNTKRVIQYFASIAAGGSAKKEGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIR 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 249 IHFGASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNpYDYAYISQGETTVA-----SIN 323
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKG-GKYELLNSYGPSFArkravADK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 324 DGEELLATDEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAE---ADGTEDGDKVAYLMGLNSADLIKGLCH 400
Cdd:cd14902 240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATavtAASRFHLAKCAELMGVDVDKLETLLSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 401 PRVKVGNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLD-------TKQPRQYF--IGVLDIAGFEIFDFNT 471
Cdd:cd14902 320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsISDEDEELatIGILDIFGFESLNRNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 472 FEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLqACIDLIE-KPMGIMSILEEECMFPKASDSTFKAK 550
Cdd:cd14902 400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNA-ACLALFDdKSNGLFSLLDQECLMPKGSNQALSTK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 551 LYDNHLgksnnfqkpraikgkPESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFA--NYAGTES 628
Cdd:cd14902 479 FYRYHG---------------GLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGAdeNRDSPGA 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 629 DNGKGGKGGGSKKKGSsfqTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICR 708
Cdd:cd14902 544 DNGAAGRRRYSMLRAP---SVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIAR 620
|
650 660
....*....|....*....|.
gi 163644331 709 KGFPNRILYGDFKQRYRILNP 729
Cdd:cd14902 621 HGYSVRLAHASFIELFSGFKC 641
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
41-821 |
1.55e-125 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 416.35 E-value: 1.55e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 41 DPDEEYVKASIV-SREGDKVTVQ---TEKRKTVTVKEADIHPQNPP-KFDKIEDMAMFTFLHEPAVLFNLKERYAAWMIY 115
Cdd:PTZ00014 47 DPDLMFAKCLVLpGSTGEKLTLKqidPPTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 116 TYSGLFCVTVNPYKWLPVYNQEVVVAYR-GKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQY 194
Cdd:PTZ00014 127 TTADPLLVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRY 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 195 FASIAAGgsakkegaEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLASADIETYLLEKSRVTF 274
Cdd:PTZ00014 207 FASSKSG--------NMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 275 QLKAERDYHIFYQILSQRKPELLEMLLITNNPyDYAYISQGETTVASINDGEELLATDEAFDVLGFTQEEKNGIYKLIGA 354
Cdd:PTZ00014 279 QEDDERSYHIFYQLLKGANDEMKEKYKLKSLE-EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 355 IMHFGNMKFKQKQREEQAEADGTEDGD-----KVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQVYYAIGALAKS 429
Cdd:PTZ00014 358 VLLLGNVEIEGKEEGGLTDAAAISDESlevfnEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 430 VYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF 509
Cdd:PTZ00014 438 VYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEE 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 510 IDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHlgKSNNFQKPRaiKGKPESHFSLVHYAGTVDYNI 589
Cdd:PTZ00014 518 LEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNL--KNNPKYKPA--KVDSNKNFVIKHTIGDIQYCA 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 590 NNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESdngkggkgggskkKGSSFQTVSALHRENLNKLMTNLRSTHP 669
Cdd:PTZ00014 594 SGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG-------------KLAKGQLIGSQFLNQLDSLMSLINSTEP 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 670 HFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNpAAIPEGQFIDSRKGAEKLLG 749
Cdd:PTZ00014 661 HFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLE 739
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 163644331 750 SLDIDHNQYKFGHTKVFFKAGLLGQLEEMRDDRLSL---IISGIQARSRGLLARVEFQKIVErrdALLVIQWNVR 821
Cdd:PTZ00014 740 RSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwepLVSVLEALILKIKKKRKVRKNIK---SLVRIQAHLR 811
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-768 |
1.13e-123 |
|
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: 404.93 E-value: 1.13e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFASIaaggsakkeGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFgASGKLA 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL---------YQDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 259 SADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLItNNPYDYAYISQGET-TVASINDGEELLATDEAFDV 337
Cdd:cd14896 151 GASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 338 LGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGD--KVAYLMGLnSADLIKGLCHPRVKVGN-EWVTKGQ 414
Cdd:cd14896 230 LGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQV-PPERLEGAVTHRVTETPyGRVSRPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 415 NVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYF--IGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHM 492
Cdd:cd14896 309 PVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 493 FVLEQEEYKKEGIEWEFIDfGMDLQACIDLI-EKPMGIMSILEEECMFPKASDSTFKAKLYDNHlGKSNNFQKPRAikgk 571
Cdd:cd14896 389 LAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQL---- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 572 PESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFanyagtesdngkgGKGGGSKKKGSSFQTVSA 651
Cdd:cd14896 463 PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLF-------------QEAEPQYGLGQGKPTLAS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 652 LHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILnpAA 731
Cdd:cd14896 530 RFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGAL--GS 607
|
650 660 670
....*....|....*....|....*....|....*..
gi 163644331 732 IPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14896 608 ERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
99-768 |
2.39e-122 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 403.18 E-value: 2.39e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNqevVVAYRGK--KRSEAPPHIFSISDNAYQYMLT-------D 168
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 169 RENQSILITGESGAGKTVNTKRVIQYFASIAAGGSAKKEGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIR 248
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 249 IHFG-----ASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPE-LLEMLLITNNPYDYAYISQGETTVAS- 321
Cdd:cd14895 158 MFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGGQCYQRNd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 322 -INDGEELLATDEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGT------------------EDGDK 382
Cdd:cd14895 238 gVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAasapcrlasaspssltvqQHLDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 383 VAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQY-------- 454
Cdd:cd14895 318 VSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnkaankd 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 455 ---FIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIM 530
Cdd:cd14895 398 ttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPSGIF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 531 SILEEECMFPKASDSTFKAKLYdNHLGKSNNFQKPRaiKGKPESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQK 610
Cdd:cd14895 477 SLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGK 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 611 STVKLLSMLFANYAGTESDNGKGGKGGGSKKKGSSFQT-VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENP 689
Cdd:cd14895 554 TSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMA 633
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644331 690 LVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIPegqfidSRKGAEKLLGSLDIDHNQykFGHTKVFFK 768
Cdd:cd14895 634 KVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNA------SDATASALIETLKVDHAE--LGKTRVFLR 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-768 |
3.49e-118 |
|
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: 389.35 E-value: 3.49e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRG-KKRSEAPPHIFSIS----DNAYQYmltdRENQS 173
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTArralENLHGV----NKSQT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 174 ILITGESGAGKTVNTKRVIQYFASiAAGGSAKkegaekkGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGA 253
Cdd:cd14876 77 IIVSGESGAGKTEATKQIMRYFAS-AKSGNMD-------LRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVAS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 254 SGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLE--MLLITNnpyDYAYISQGETTVASINDGEELLAT 331
Cdd:cd14876 149 EGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSkyHLLGLK---EYKFLNPKCLDVPGIDDVADFEEV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 332 DEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAY-----LMGLNSADLIKGLCHPRVKVG 406
Cdd:cd14876 226 LESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISNESLEVFkeacsLLFLDPEALKRELTVKVTKAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 407 NEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQ 486
Cdd:cd14876 306 GQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 487 FFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHlgKSNNFQKPr 566
Cdd:cd14876 386 NFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKL--KSNGKFKP- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 567 aIKGKPESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANyagtesdngkggkGGGSKKKGSSF 646
Cdd:cd14876 463 -AKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG-------------VVVEKGKIAKG 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 647 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRI 726
Cdd:cd14876 529 SLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKF 608
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 163644331 727 LNPaAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14876 609 LDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
101-729 |
3.34e-111 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 369.95 E-value: 3.34e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 101 VLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNQEVVVAYRGKKRSEA-PPHIFSISDNAYQYMLTDRE--NQSILI 176
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 177 TGESGAGKTVNTKRVIQYFASIAAGgSAKKEGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGK 256
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAAS-PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 257 LASADIETYLLEKSRVTFQLKAERDYHIFYQILS-QRKPELLEMLLITNNpyDYAYISQGETTVasinDGEELLATDEAF 335
Cdd:cd14880 162 MTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKgASADERLQWHLPEGA--AFSWLPNPERNL----EEDCFEVTREAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 336 DVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQA--EADGTEDGDKV-AYLMGLNSADLIKGLCHPRVKVGNEwvtk 412
Cdd:cd14880 236 LHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqPMDDTKESVRTsALLLKLPEDHLLETLQIRTIRAGKQ---- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 413 gqnvQQVYYAI----------GALAKSVYEKMFLWMVVRINQSLDTKQPR-QYFIGVLDIAGFEIFDFNTFEQLCINFTN 481
Cdd:cd14880 312 ----QQVFKKPcsraecdtrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYAN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 482 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASD-----STFKAKLYDNH 555
Cdd:cd14880 388 EKLQQHFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSaaqlqTRIESALAGNP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 556 LGKSNNFQKpraikgkpESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFAnyagteSDNGKGGK 635
Cdd:cd14880 467 CLGHNKLSR--------EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFP------ANPEEKTQ 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 636 GGGSKKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRI 715
Cdd:cd14880 533 EEPSGQSRAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRV 612
|
650
....*....|....
gi 163644331 716 LYGDFKQRYRILNP 729
Cdd:cd14880 613 SHQNFVERYKLLRR 626
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
100-725 |
1.56e-107 |
|
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: 361.34 E-value: 1.56e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNQEVVVAYR-------GKKRSEA---PPHIFSISDNAYQYMLTD 168
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 169 RENQSILITGESGAGKTVNTKRVIQYFASIAAGGSAKKEGAEK--------KGTLEDQIIQANPALEAFGNAKTIRNDNS 240
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESisppaspsRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 241 SRFGKFIRIHF-GASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQR----KPELLEMLLITNNPYDYAYISQG 315
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 316 ETTVA--SINDGEELLATDEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQ--KQREEQAEAD---------GTEDG-D 381
Cdd:cd14899 242 LCSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADearvmssttGAFDHfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 382 KVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSL--------------- 446
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 447 DTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDlQACIDLIE-K 525
Cdd:cd14899 402 DDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 526 PMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNNFQKPRAIKGKPESHFSLVHYAGTVDYNINNWLVKNKDPLNETVV 605
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 606 GLFQKSTVKLLSMLFANYAGTESDNGKGGKGGGSKKKGSSFQTVSALH-----RENLNKLMTNLRSTHPHFVRCIIPNET 680
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSvgtqfKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 163644331 681 KTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYR 725
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
105-768 |
1.91e-106 |
|
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: 355.73 E-value: 1.91e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 105 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNQEVVVAYRGKKRS-----EAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFASIAAGGSAKKEGAekkgtledqIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLA 258
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTDVQSL---------ILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 259 SADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYdYAYISQGET-TVASINDGEELLATDEAFDV 337
Cdd:cd14886 158 GGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASKCyDAPGIDDQKEFAPVRSQLEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 338 LgFTQEEKNGIYKLIGAIMHFGNMKFKQKQR---EEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQ 414
Cdd:cd14886 237 L-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 415 NVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFV 494
Cdd:cd14886 316 TQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 495 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKP-MGIMSILEEECMFPKASDSTFKAKLyDNHLgKSNNFqkpraIKGKPE 573
Cdd:cd14886 396 SEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSF-----IPGKGS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 574 S-HFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAgTESDNGKGgkgggskkkgssfQTVSAL 652
Cdd:cd14886 468 QcNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIP-NEDGNMKG-------------KFLGST 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 653 HRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRIL---NP 729
Cdd:cd14886 534 FQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 163644331 730 AAIPEGQfiDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14886 614 SSQNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
101-728 |
1.18e-105 |
|
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: 355.83 E-value: 1.18e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 101 VLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNQEVVVAYRGKKR-SEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFasIAAGGSAKKEGAE---KKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGAS- 254
Cdd:cd14906 83 ESGSGKTEASKTILQYL--INTSSSNQQQNNNnnnNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 255 GKLASADIETYLLEKSRVTFQL-KAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGETTVASI--------NDG 325
Cdd:cd14906 161 GKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 326 EELLATDEAFDVL-------GFTQEEKNGIYKLIGAIMHFGNMKFKQKQ---REEQAEADGTEDGDKVAYLMGLNSADLI 395
Cdd:cd14906 241 NNKTESIESFQLLkqsmesmSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 396 KGLCHPRVKVGNEWVT--KGQNVQQVYYAIGALAKSVYEKMFLWMVVRIN----QSLDTKQPRQY-------FIGVLDIA 462
Cdd:cd14906 321 QALLNRNLKAGGRGSVycRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINrkfnQNTQSNDLAGGsnkknnlFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 463 GFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPK 541
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 542 ASDSTFKAKlYDNHLGKSNNFQKPRAIKGKpeshFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFa 621
Cdd:cd14906 480 GSEQSLLEK-YNKQYHNTNQYYQRTLAKGT----LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLF- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 622 nyagtesdNGKGGKGGGSKKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVL 701
Cdd:cd14906 554 --------QQQITSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVL 625
|
650 660
....*....|....*....|....*..
gi 163644331 702 EGIRICRKGFPNRILYGDFKQRYRILN 728
Cdd:cd14906 626 NTIKVRKMGYSYRRDFNQFFSRYKCIV 652
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
101-768 |
2.38e-101 |
|
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: 341.40 E-value: 2.38e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 101 VLFNLKERYAAWMI-YTYSGLFCVTVNPYKWLPvYNQEVvvaYRGKKRSEA-----PPHIFSISDNAY-QYMLTDRENQS 173
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMP-FNSEE---ERKKYLALPdprllPPHIWQVAHKAFnAIFVQGLGNQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 174 ILITGESGAGKTVNTKRVIQYFASIA---AGGSAKKEGAEKkgtLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIH 250
Cdd:cd14875 79 VVISGESGSGKTENAKMLIAYLGQLSymhSSNTSQRSIADK---IDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 251 F-GASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGETTV------ASIN 323
Cdd:cd14875 156 FdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKTLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 324 DGEELLATDEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEdGDKVAYLMGLNSADLIKGLChprV 403
Cdd:cd14875 236 DAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETP-FLTACRLLQLDPAKLRECFL---V 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 404 KVGNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQ--PRQYFIGVLDIAGFEIFDFNTFEQLCINFTN 481
Cdd:cd14875 312 KSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQLCINYAN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 482 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSN 560
Cdd:cd14875 392 ESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 561 NFQKPraiKGKPESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNgkggkgggsk 640
Cdd:cd14875 471 YFVLP---KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRK---------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 641 kkgssfQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 720
Cdd:cd14875 538 ------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQF 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 163644331 721 -KQRYRILNPAAIPEGQFIDSRKGAEKLLGSLDIDHN----QYKFGHTKVFFK 768
Cdd:cd14875 612 cRYFYLIMPRSTASLFKQEKYSEAAKDFLAYYQRLYGwakpNYAVGKTKVFLR 664
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
101-768 |
2.70e-101 |
|
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: 342.37 E-value: 2.70e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 101 VLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 181 GAGKTVNTKRVIQYFASIaAGGSAKKEGAEKkgtledqiIQA-NPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLAS 259
Cdd:cd01386 83 GSGKTTNCRHILEYLVTA-AGSVGGVLSVEK--------LNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 260 ADIETYLLEKSRVTFQLKAERDYHIFYQIL-----SQRKPELLEMLLITNNPYDYAYISQGETTVASindgEELLATDEA 334
Cdd:cd01386 154 ASIQTLLLERSRVARRPEGESNFNVFYYLLagadaALRTELHLNQLAESNSFGIVPLQKPEDKQKAA----AAFSKLQAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 335 FDVLGFTQEEKNGIYKLIGAIMHFGN---MKFKQKQREEQAEadgTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVT 411
Cdd:cd01386 230 MKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFAR---PEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQST 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 412 ---------------KGQNVQQvyyAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFN------ 470
Cdd:cd01386 307 tssgqesparsssggPKLTGVE---ALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrga 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 471 TFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEK---------------PMGIMSILEE 535
Cdd:cd01386 384 TFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLDE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 536 ECMFPKASDSTFKAKLYdNHLGKSNNFQKPRAIKGKPES-HFSLVHYAGT--VDYNINNWLVKNK-DPLNETVVGLFQKS 611
Cdd:cd01386 464 EALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQES 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 612 TVKLLSM----LFANyagtesdngkggkgggskkkgSSFQtvsalhrenLNKLMTNLRSTHPHFVRCIIPN------ETK 681
Cdd:cd01386 543 QKETAAVkrksPCLQ---------------------IKFQ---------VDALIDTLRRTGLHFVHCLLPQhnagkdERS 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 682 TPGAMEN------PLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPA----AIPEGQFIDSRKGAEKLLGSL 751
Cdd:cd01386 593 TSSPAAGdelldvPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltkkLGLNSEVADERKAVEELLEEL 672
|
730
....*....|....*..
gi 163644331 752 DIDHNQYKFGHTKVFFK 768
Cdd:cd01386 673 DLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-743 |
2.34e-92 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 312.60 E-value: 2.34e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKwlPVYNQEVVVAYRgKKRSEAPPHIFSISDNAYQYMLTdRENQSILITGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 180 SGAGKTVNTKRVIQYFAsiaaggsakkEGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFgaSGKLAS 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLV----------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKITG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 260 ADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKpellemLLITNNPYDYAYISQGETTVasINDGEELLATDEAFDVLG 339
Cdd:cd14898 146 AKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMTCSAMKSLG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 340 FTQEEKngIYKLIGAIMHFGNMKFKQkqrEEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQV 419
Cdd:cd14898 218 IANFKS--IEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 420 YYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQyfIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQEE 499
Cdd:cd14898 293 RTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGM 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 500 YKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFP--KASDSTFKAKLYDNHLgksnnfqkpraIKGKPESHFS 577
Cdd:cd14898 371 YKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAwgNVKNLLVKIKKYLNGF-----------INTKARDKIK 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 578 LVHYAGTVDYNINNWLVKNKdplnetvvglfQKSTVKLLSMLFANYAGTESDngkggkgggskkkgssfqtVSALHRENL 657
Cdd:cd14898 439 VSHYAGDVEYDLRDFLDKNR-----------EKGQLLIFKNLLINDEGSKED-------------------LVKYFKDSM 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 658 NKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPAAIpegQF 737
Cdd:cd14898 489 NKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLF---EV 565
|
....*.
gi 163644331 738 IDSRKG 743
Cdd:cd14898 566 VDYRKG 571
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
100-727 |
4.80e-90 |
|
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: 308.28 E-value: 4.80e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYR---GKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 176
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 177 TGESGAGKTVNTKRVIQYFASIAAggsakkegaEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGK 256
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTCRAS---------SSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 257 -LASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLItNNPYDYAYISQGE----TTVASINDGEELLAT 331
Cdd:cd14878 153 hLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHL-NNLCAHRYLNQTMredvSTAERSLNREKLAVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 332 DEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKVGNEWVT 411
Cdd:cd14878 232 KQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 412 KGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSL----DTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQF 487
Cdd:cd14878 312 RRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 488 FNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACID-LIEKPMGIMSILEEECMFPKASDSTFKAKLyDNHLGKSNNFQKPR 566
Cdd:cd14878 392 INEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPSGFLSLLDEESQMIWSVEPNLPKKL-QSLLESSNTNAVYS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 567 AIK---GKPESH-----FSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFanyagtesdngkggkggg 638
Cdd:cd14878 471 PMKdgnGNVALKdqgtaFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF------------------ 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 639 skkkGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYG 718
Cdd:cd14878 533 ----QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFS 608
|
....*....
gi 163644331 719 DFKQRYRIL 727
Cdd:cd14878 609 DFLSRYKPL 617
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
101-768 |
7.80e-88 |
|
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: 301.55 E-value: 7.80e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 101 VLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEvvvaYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 181 GAGKTVNTKRVIQYFASiaaggsAKKEGAEKKGTLEDqiiqANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLASA 260
Cdd:cd14937 79 GSGKTEASKLVIKYYLS------GVKEDNEISNTLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 261 DIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPyDYAYISQGETTVASINDGEELLATDEAFDVLGF 340
Cdd:cd14937 149 SIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 341 TqEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDG-----DKVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQN 415
Cdd:cd14937 228 H-DMKDDLFLTLSGLLLLGNVEYQEIEKGGKTNCSELDKNnlelvNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 416 VQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVL 495
Cdd:cd14937 307 VEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 496 EQEEYKKEGIEWEFIDFGMDlQACIDLIEKPMGIMSILEEECMFPKASDSTFkAKLYDNHLGKSNNFQkprAIKGKPESH 575
Cdd:cd14937 387 ETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYA---STKKDINKN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 576 FSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDNGKggkgggskkkgssfQTVSALHRE 655
Cdd:cd14937 462 FVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRK--------------NLITFKYLK 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 656 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRIcRKGFPNRILYGDFKQRYRILNPAAIPEG 735
Cdd:cd14937 528 NLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDS 606
|
650 660 670
....*....|....*....|....*....|...
gi 163644331 736 QFIDSRKGAEKLLGSLDIDhnQYKFGHTKVFFK 768
Cdd:cd14937 607 SLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-768 |
1.70e-87 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 303.11 E-value: 1.70e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAA--------WMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 171 NQSILITGESGAGKTVNTKRVIQYFASIaaggSAKKEGAEKKGtLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIH 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAV----SDRRHGADSQG-LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 251 FGASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQiLSQRKPELLEMLLITNNPYDYAYisqgettvasinDGEELLA 330
Cdd:cd14887 156 FTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYA-LCNAAVAAATQKSSAGEGDPEST------------DLRRITA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 331 TDEAFDVLGFTQEEkngIYKLIGAIMHFGNMKFKQKQREEQAEA-----------DGTEDGDKVAYLMGLNSADLIKGLC 399
Cdd:cd14887 223 AMKTVGIGGGEQAD---IFKLLAAILHLGNVEFTTDQEPETSKKrkltsvsvgceETAADRSHSSEVKCLSSGLKVTEAS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 400 HPRVK-----VGNEWVTKGQN-------------------VQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQY- 454
Cdd:cd14887 300 RKHLKtvarlLGLPPGVEGEEmlrlalvsrsvretrsffdLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPSEs 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 455 -------------FIGVLDIAGFEIF---DFNTFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFI--DFGMDL 516
Cdd:cd14887 380 dsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSF 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 517 QACIDLIEKP------------------------MGIMSILEEE-CMFPKASDSTFKAKLYDNHLGK----SNNFQKPRA 567
Cdd:cd14887 460 PLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKNITP 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 568 IKGKPESHFSLVHYAGTVDYNINNWLVKNKDPLNETvvglfqkstvklLSMLFANYAGTESDNGKGGKGGGSKKKGSSfQ 647
Cdd:cd14887 540 ALSRENLEFTVSHFACDVTYDARDFCRANREATSDE------------LERLFLACSTYTRLVGSKKNSGVRAISSRR-S 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 648 TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRIL 727
Cdd:cd14887 607 TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETK 686
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 163644331 728 NPAAIPEgqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14887 687 LPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
105-767 |
9.35e-85 |
|
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: 292.53 E-value: 9.35e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 105 LKERYAAWMIYTY---SGLfcVTVNPYKWLPVYNQEVVVAYR-------GKKRSEAPPHIFSISDNAYQYMLTDRENQSI 174
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 175 LITGESGAGKTVNTKRVIQYFASIAAggsakkegAEKKGT-LEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGA 253
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSS--------HSKKGTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 254 SGKLASADIETYLLEKSRVTfQLKA-ERDYHIFYQILSQRKPELLEMLLItNNPYDYAYI--SQGETTVAS--INDGE-- 326
Cdd:cd14879 160 RGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQHLGL-DDPSDYALLasYGCHPLPLGpgSDDAEgf 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 327 ELLATdeAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQkqreeqaEADGTEDG---------DKVAYLMGLNSADLIKG 397
Cdd:cd14879 238 QELKT--ALKTLGFKRKHVAQICQLLAAILHLGNLEFTY-------DHEGGEESavvkntdvlDIVAAFLGVSPEDLETS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 398 LCHPRVKVGNEWVTKGQNVQqvyyaiGA------LAKSVYEKMFLWMVVRINQSL-DTKQPRQYFIGVLDIAGFEIFD-- 468
Cdd:cd14879 309 LTYKTKLVRKELCTVFLDPE------GAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSst 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 469 -FNTFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEEC-MFPKASDS 545
Cdd:cd14879 383 gGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 546 TFKAKLyDNHLGKSNNFQKPRAIKGKPESH-FSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFqKSTVKLlsmlfanya 624
Cdd:cd14879 462 QMLEAL-RKRFGNHSSFIAVGNFATRSGSAsFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLL-RGATQL--------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 625 gtesdngkggkgggskkkgssfqtvsalhRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGI 704
Cdd:cd14879 531 -----------------------------NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELA 581
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 163644331 705 RICRKGFPNRILYGDFKQRYrilnpaaIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFF 767
Cdd:cd14879 582 ARLRVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-716 |
8.07e-75 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 264.46 E-value: 8.07e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNQEVVVAYRGKKRSEA-------PPHIFSISDNAYQYMLTDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 171 NQSILITGESGAGKTVNTKRVIQYFASIaaggsakkEGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIH 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI--------QTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 251 F---------GASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYDYAYISQGE----- 316
Cdd:cd14884 153 FeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEshqkr 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 317 -------TTVASINDGEELLATDEA-----FDVLGFTQEEK---NGIYKLIGAIMHFGNMKFKQkqreeqaeadgtedgd 381
Cdd:cd14884 233 svkgtlrLGSDSLDPSEEEKAKDEKnfvalLHGLHYIKYDErqiNEFFDIIAGILHLGNRAYKA---------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 382 kVAYLMGLNSADLIKGLCHPRVKVGNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRIN---------QSLDTKQPR 452
Cdd:cd14884 297 -AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekDESDNEDIY 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 453 QY---FIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEW--EFIDFGMDLQACIDLIEKPM 527
Cdd:cd14884 376 SIneaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICcsDVAPSYSDTLIFIAKIFRRL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 528 GIMSILEEECMfpKASDSTFKAKLYDNH----------LGKSNNFQKPRAIKGK--PESHFSLVHYAGTVDYNINNWLVK 595
Cdd:cd14884 456 DDITKLKNQGQ--KKTDDHFFRYLLNNErqqqlegkvsYGFVLNHDADGTAKKQniKKNIFFIRHYAGLVTYRINNWIDK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 596 NKDPLNETVVGLFQKSTVKLLSmlfANYAGTESDNgkggkgggskkkgssFQTVSALHRENLNKLMTNLRSTHPHFVRCI 675
Cdd:cd14884 534 NSDKIETSIETLISCSSNRFLR---EANNGGNKGN---------------FLSVSKKYIKELDNLFTQLQSTDMYYIRCF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 163644331 676 IPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRIL 716
Cdd:cd14884 596 LPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
100-736 |
5.95e-73 |
|
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: 257.49 E-value: 5.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYrgkkrseappHIFSISDNAYQYMLTDREN-QSILITG 178
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 179 ESGAGKTVNTKRVIQYFASiaaggsakkEGAEKKGTLEDQIIQAnpALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLA 258
Cdd:cd14874 72 ESGSGKSYNAFQVFKYLTS---------QPKSKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 259 SADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNpYDYAYISQGETTVASINDGEELLATDEAFDVL 338
Cdd:cd14874 141 LNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL-QKFFYINQGNSTENIQSDVNHFKHLEDALHVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 339 GFTQEEKNGIYKLIGAIMHFGNMKFKQKqREEQAEADGTEDGDK-----VAYLMGLNSADLIKGLChPRVKVGNEWvtkg 413
Cdd:cd14874 220 GFSDDHCISIYKIISTILHIGNIYFRTK-RNPNVEQDVVEIGNMsevkwVAFLLEVDFDQLVNFLL-PKSEDGTTI---- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 414 qNVQQVYYAIGALAKSVYEKMFLWMVVRInqSLDTKQPRQY-FIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHM 492
Cdd:cd14874 294 -DLNAALDNRDSFAMLIYEELFKWVLNRI--GLHLKCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 493 FVLEQEEYKKEGIEwefIDFGMdlQACID-------LIEKPMGIMSILEEECMFPKASDSTFKAKLYDNHLGKSNnFQKP 565
Cdd:cd14874 371 FHDQLVDYAKDGIS---VDYKV--PNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGKA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 566 RAikgKPESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANYAGTESDngkggkgggskkkgsS 645
Cdd:cd14874 445 RN---KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSD---------------M 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 646 FQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYR 725
Cdd:cd14874 507 IVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYR 586
|
650
....*....|.
gi 163644331 726 ILNPAAIPEGQ 736
Cdd:cd14874 587 CLLPGDIAMCQ 597
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-748 |
4.90e-71 |
|
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: 251.96 E-value: 4.90e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPvyNQEVVVAYRGKKRSeapPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 180 SGAGKTVNTKRVIQYFASIAAGGS---AKKEGAekkgtledqiiQANPALEAFGNAKTIRNDNSSRFGKFIRIHFgASGK 256
Cdd:cd14881 77 SGSGKTYASMLLLRQLFDVAGGGPetdAFKHLA-----------AAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDGA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 257 LASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITN-NPYDYAYISQGETTVASINDGEELLATDEAF 335
Cdd:cd14881 145 LYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGySPANLRYLSHGDTRQNEAEDAARFQAWKACL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 336 DVLG--FTQeekngIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDgDKVAYLMGLNSADLIKGL---CHprvkvgnewV 410
Cdd:cd14881 225 GILGipFLD-----VVRVLAAVLLLGNVQFIDGGGLEVDVKGETEL-KSVAALLGVSGAALFRGLttrTH---------N 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 411 TKGQNVQQV------YYAIGALAKSVYEKMFLWMVVRINQ-----SLDTKQPRQYFIGVLDIAGFEIFDFNTFEQLCINF 479
Cdd:cd14881 290 ARGQLVKSVcdanmsNMTRDALAKALYCRTVATIVRRANSlkrlgSTLGTHATDGFIGILDMFGFEDPKPSQLEHLCINL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 480 TNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-IDFgMDLQACIDLIEK-PMGIMSILEEECMfPKASDSTFKAKLYDNHlg 557
Cdd:cd14881 370 CAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQH-- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 558 KSNN-FQKPRAIKGkpeSHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVkllSMLFANYAgteSDngkggkg 636
Cdd:cd14881 446 RQNPrLFEAKPQDD---RMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNC---NFGFATHT---QD------- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 637 ggskkkgssFQTvsalhreNLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRIL 716
Cdd:cd14881 510 ---------FHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMR 573
|
650 660 670
....*....|....*....|....*....|..
gi 163644331 717 YGDFKQRYRILNPAAiPEGQFIDSRKGAEKLL 748
Cdd:cd14881 574 FKAFNARYRLLAPFR-LLRRVEEKALEDCALI 604
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
105-720 |
1.48e-65 |
|
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: 236.91 E-value: 1.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 105 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNQEVVVAYrgKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAG 183
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 184 KTVNTKRVIQYFASIaaggsakkeGAEKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLASADIE 263
Cdd:cd14905 85 KSENTKIIIQYLLTT---------DLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 264 TYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLItNNPYDYAYISQGET-TVASINDGEELLATDEAFDVLGFTQ 342
Cdd:cd14905 156 SYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQL-GDINSYHYLNQGGSiSVESIDDNRVFDRLKMSFVFFDFPS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 343 EEKNGIYKLIGAIMHFGNMKFKQKQREeqaeadgTEDGDKVaylmglnsadLIKGLCH----PRVKVGNEWVT-KGQNVQ 417
Cdd:cd14905 235 EKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDRT----------LIESLSHnitfDSTKLENILISdRSMPVN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 418 QVYYAIGALAKSVYEKMFLWMVVRINQSLdtkQPRQY--FIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVL 495
Cdd:cd14905 298 EAVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 496 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKpmgIMSILEEECMFPKASDSTFKAKLydnhlgksNNFQKPRAIKGKPESH 575
Cdd:cd14905 375 EQREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKKPNK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 576 FSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLL----SMLFANYAGTESDNGKGGKGGGSKKKGSSFQTVSA 651
Cdd:cd14905 444 FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLfsrdGVFNINATVAELNQMFDAKNTAKKSPLSIVKVLLS 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 652 LHRENLNKL--------------------------MTNLRSTHP---------HFVRCIIPNETKTPGAMENPLVMHQLR 696
Cdd:cd14905 524 CGSNNPNNVnnpnnnsgggggggnsgggsgsggstYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIK 603
|
650 660
....*....|....*....|....*...
gi 163644331 697 CNGVLEGIRICRKGFP----NRILYGDF 720
Cdd:cd14905 604 SLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
101-727 |
6.76e-64 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 231.17 E-value: 6.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 101 VLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 181 GAGKTVNTKRVIQYFASIAAGgsakkegaeKKGTLEdQIIQANPALEAFGNAKTIRNDNSSRFGKFIRIHFGASGKLASA 260
Cdd:cd14882 83 YSGKTTNARLLIKHLCYLGDG---------NRGATG-RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 261 DIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPE--LLEMLLITNNPYDYAYISQG-------------ETTVASINDG 325
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQnrLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERYKEF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 326 EELLAtdeafdVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREeqAEADGTEDGDKVAYLMGLNSADLIKGLCHPRVKV 405
Cdd:cd14882 233 EEILK------DLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLIK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 406 GNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTkqPR-----QYFIGVLDIAGFEIFDFNTFEQLCINFT 480
Cdd:cd14882 305 GGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMVNTL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 481 NEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEecmfpkASDSTFKAKL-YDNHLGKS 559
Cdd:cd14882 383 NEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD------ASRSCQDQNYiMDRIKEKH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 560 NNFQKPRAikgkpESHFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKSTVKLLSMLFANyagtesdngkggkgggs 639
Cdd:cd14882 457 SQFVKKHS-----AHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN----------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 640 kKKGSSFQTVSALHR----ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRI 715
Cdd:cd14882 515 -SQVRNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRI 593
|
650
....*....|..
gi 163644331 716 LYGDFKQRYRIL 727
Cdd:cd14882 594 PFQEFLRRYQFL 605
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-767 |
1.51e-61 |
|
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: 226.39 E-value: 1.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 102 LFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKR----------SEAPPHIFSISDNAYQYMLTDREN 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 172 QSILITGESGAGKTVNTKRVIQYFASIAAGGSAKKEGAEKKGTLE---DQIIQANPALEAFGNAKTIRNDNSSRFGKFIR 248
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHpigQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 249 IHFGASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILS--QRKPELLEMLLITNNPYDYAYISQGETTVASIN-DG 325
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAgvQHDPTLRDSLEMNKCVNEFVMLKQADPLATNFAlDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 326 EELLATDEAFDVLGFTQEEKNGIYKLIGAIMHFGNMKFKQKQREEQAEADGTEDGDKVAYLMGLNSADLIKGLCH----- 400
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSDAQSCALKDPAQILLAAKlleve 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 401 PRV------------KVGNEWVT--KGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSL----DTKQPRQYFIG----- 457
Cdd:cd14893 324 PVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVINsqgvh 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 458 VLDIAGFEIFD--FNTFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWE-------FIDFGMDLQACIDLIE-KPM 527
Cdd:cd14893 404 VLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVEnrltvnsNVDITSEQEKCLQLFEdKPF 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 528 GIMSILEEECMFPKASDSTFKAKLYDNH-----LGKSNNFQKPRAIKGKPESHFSLV----HYAGTVDYNINNWLVKNKD 598
Cdd:cd14893 484 GIFDLLTENCKVRLPNDEDFVNKLFSGNeavggLSRPNMGADTTNEYLAPSKDWRLLfivqHHCGKVTYNGKGLSSKNML 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 599 PLNETVVGLFQKSTVKLLSMLFANYAGTESDNGKGGKGGGSKKKGSSFQTVSALHRENLN--------------KLMTNL 664
Cdd:cd14893 564 SISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadALLHAL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 665 RSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRilnpaaipegQFIDSRKGA 744
Cdd:cd14893 644 NHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK----------NVCGHRGTL 713
|
730 740
....*....|....*....|....*..
gi 163644331 745 EKLLGSLD----IDHNQYKFGHTKVFF 767
Cdd:cd14893 714 ESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-249 |
1.20e-60 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 205.66 E-value: 1.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 121 FCVTVNPYKWLPVYNQEVV-VAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASIA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 163644331 200 AGGSAKKEGA------EKKGTLEDQIIQANPALEAFGNAKTIRNDNSSRFGKFIRI 249
Cdd:cd01363 81 FNGINKGETEgwvyltEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-766 |
2.42e-43 |
|
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: 170.79 E-value: 2.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNQEVVVAYRGKKRSE-APPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 178 GESGAGKTVNTKRVIQYFASIAAGGSAKKEGAEK--------------KGTLEDQIIQANPALEAFGNAKTIRNDNSSRF 243
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDqeednihneentdyQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 244 GKFIRIHFgASGKLASADIETYLLEKSRVTFQLKAERDYHIFYQILSQRKPELLEMLLITNNPYdYAYISQGETTVASIN 323
Cdd:cd14938 161 SKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIEN-YSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 324 DGEELLATDEAFDVLGFTQEEKNGIYKLIGAIMHFGN-------------MKFKQKQRE----------EQAEADGTEDG 380
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 381 DKVAYL----MGLNSADLIKGLCHPRVkVGNEWVTKGQNVQQVYYAIGALAKSVYEKMFLWMVVRINQSLDTKQPRQYF- 455
Cdd:cd14938 319 VKNLLLacklLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININt 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 456 --IGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM--GIMS 531
Cdd:cd14938 398 nyINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 532 ILEEECMfPKASDSTFKAKLYDNHLGKSNNFQKPRAIKGKPEShFSLVHYAGTVDYNINNWLVKNKDPLNETVVGLFQKS 611
Cdd:cd14938 478 LLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 612 TVKLLSMLFANYAGTESDNGKGGKGGGSKKKGSSF---------QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKT 682
Cdd:cd14938 556 ENEYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLfkrrydtknQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKR 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 683 P-GAMENPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRILNPaaipegqfiDSRKGAEKLLGSLDIDHNQYKFG 761
Cdd:cd14938 636 ElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMIG 706
|
....*
gi 163644331 762 HTKVF 766
Cdd:cd14938 707 NNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
846-1745 |
3.73e-32 |
|
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: 137.50 E-value: 3.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 846 EAEKEMANMKDEFAKLKEAYAKSEARRKELE------EKMVSLLQEKNDLQLQVQAeqDNLCDAEERCDQLIKNKIQLEA 919
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKAELRELELALLV--LRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 920 KAKELTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTK--- 996
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESkld 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 997 ----EKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLtqeslmdLE 1072
Cdd:TIGR02168 334 elaeELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER-------LE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1073 NDKQQLEERLKKKDFEISQLNGKIEDeqticiqlqKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERL 1152
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEE---------AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1153 EEAGG---ATAAQIEMNKKREAEFQKLRRDLEEATLQheataatlRKKQADSVAELGEQIdnlqRVKQKLEKEKSE-LRL 1228
Cdd:TIGR02168 478 DAAERelaQLQARLDSLERLQENLEGFSEGVKALLKN--------QSGLSGILGVLSELI----SVDEGYEAAIEAaLGG 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1229 ELDDVVSNMEHVVK------TKANLEKMTRSLEDQMNEYktkyeegqrcindftmqksKLQSENGELSRQLEEKDSLVSQ 1302
Cdd:TIGR02168 546 RLQAVVVENLNAAKkaiaflKQNELGRVTFLPLDSIKGT-------------------EIQGNDREILKNIEGFLGVAKD 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1303 LTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARH------DTDLLReqyeeeqeAKAELQRGMSKANSEVAQWRTK 1376
Cdd:TIGR02168 607 LVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGyrivtlDGDLVR--------PGGVITGGSAKTNSSILERRRE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1377 YEtDAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLS 1456
Cdd:TIGR02168 679 IE-ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1457 EWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEqlgeggkSIHELEKMRKQLE 1536
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE-------EAANLRERLESLE 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1537 QEKSEIQSALEEAEASLEHEEGKILRAQLEFsqikadierklaekdEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRI 1616
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEI---------------EELEELIEELESELEALLNERASLEEALALLRSE 895
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1617 KKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLD---DSLR-----TNEDLKENTAIVERRNNLLQAELE 1688
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnlqERLSeeyslTLEEAEALENKIEDDEEEARRRLK 975
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 163644331 1689 ELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEE 1745
Cdd:TIGR02168 976 RLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
965-1873 |
9.07e-31 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 132.87 E-value: 9.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 965 KVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQT------------------LDDLQSEEDKVNTLTKAK 1026
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAerykelkaelrelelallVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1027 AKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQL 1106
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1107 QKKLKELQARieeleeeleaeraaRAKVEKQRADLARELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEEATLQ 1186
Cdd:TIGR02168 329 ESKLDELAEE--------------LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1187 HEATAATLRkkqadsvaELGEQIDNLQRVKQKLEKEKSELRLELDDVvsnmeHVVKTKANLEKMTRSLEDQMNEYKTKYE 1266
Cdd:TIGR02168 395 IASLNNEIE--------RLEARLERLEDRRERLQQEIEELLKKLEEA-----ELKELQAELEELEEELEELQEELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1267 EGQRCINDFTMQKSKLQSENGELSRQLEEKDSLvsqltrskmsytqqiEDLKRQLEEETKAKSALAHAVQSARHDTDLLR 1346
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARLDSL---------------ERLQENLEGFSEGVKALLKNQSGLSGILGVLS 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1347 EQYeeeqEAKAELQRGMSKANSEVAQW-RTKYETDAIQRTEELEEAKK--------------KLAQRLQETEEAVEAVNA 1411
Cdd:TIGR02168 527 ELI----SVDEGYEAAIEAALGGRLQAvVVENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILKNIEGFLG 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1412 KCSSLEKTKHRLQNEIEDL-----MVD-LERSNAAAAALDKKQRNF----DKVLSEWKQKFEESQAElessqkearclst 1481
Cdd:TIGR02168 603 VAKDLVKFDPKLRKALSYLlggvlVVDdLDNALELAKKLRPGYRIVtldgDLVRPGGVITGGSAKTN------------- 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1482 elfklknsyeealdhLETMKRENknlqeEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKIL 1561
Cdd:TIGR02168 670 ---------------SSILERRR-----EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS 729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1562 RAQLEFSQIKADIERkLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEA 1641
Cdd:TIGR02168 730 ALRKDLARLEAEVEQ-LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1642 QKQLKSVHAHMKDAQLQLddslrtnEDLKENTAIVERRNNLLQAELEELRAALEQtergrklAEQELLDTSERVQLLHSQ 1721
Cdd:TIGR02168 809 RAELTLLNEEAANLRERL-------ESLERRIAATERRLEDLEEQIEELSEDIES-------LAAEIEELEELIEELESE 874
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1722 NTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAItdaammaEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDE 1801
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELR-------RELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644331 1802 AEQIAMKGGKKQVQKLEARVRELESEVESEQKKSSE-------AVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKL 1873
Cdd:TIGR02168 948 EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
845-1610 |
7.51e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 129.79 E-value: 7.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 845 AEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAKEL 924
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 925 TERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQea 1004
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN-- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1005 hqqtlddlqseedkvNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRK-LEGDLKLTQESLMDLENDKQQLEERLK 1083
Cdd:TIGR02168 400 ---------------NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1084 KKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISER------LEEAGG 1157
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDegyeaaIEAALG 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1158 ATAAQIEMNKKREA--EFQKLRRDLEEATLQHEATAATLRKKQADSvAELGEQIDNLQRVKQKLEKEKSELRLELDDVVS 1235
Cdd:TIGR02168 545 GRLQAVVVENLNAAkkAIAFLKQNELGRVTFLPLDSIKGTEIQGND-REILKNIEGFLGVAKDLVKFDPKLRKALSYLLG 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1236 NMeHVVKTKANLEKMTRSLEDQMNEYKTkyeEGQRCINDFTMQKSKLQSENGELSRQ--LEEKDSLVSQLTRSKMSYTQQ 1313
Cdd:TIGR02168 624 GV-LVVDDLDNALELAKKLRPGYRIVTL---DGDLVRPGGVITGGSAKTNSSILERRreIEELEEKIEELEEKIAELEKA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1314 IEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQY---EEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEE 1390
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLarlEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1391 AKKK---LAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQA 1467
Cdd:TIGR02168 780 AEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1468 ELESSQKEARCLSTELFKLKNSYE-------EALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKS 1540
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERAsleealaLLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1541 EIQSAL--------EEAEASLEHEEGKILRAQLEFSQIKADIER-------------KLAEKDEEMEQSKRNLQRTIDTL 1599
Cdd:TIGR02168 940 NLQERLseeysltlEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaieeyeELKERYDFLTAQKEDLTEAKETL 1019
|
810
....*....|....
gi 163644331 1600 QSSLE---SETRSR 1610
Cdd:TIGR02168 1020 EEAIEeidREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1146-1938 |
2.97e-29 |
|
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: 127.87 E-value: 2.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1146 EEISERLEEAGGATaaqiemnkkreaefqKLRRDLEEATLQHEATAATLrKKQADSVAELGEQIDNLQRVKQKLEK---E 1222
Cdd:TIGR02168 155 EERRAIFEEAAGIS---------------KYKERRKETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERykeL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1223 KSELR-LELDDVVSNMEHVVKTKANLEKMTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKLQSENGELSRQLEEKDSLVS 1301
Cdd:TIGR02168 219 KAELReLELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1302 QLTRSKMSYTQQIEDLKRQLEEetkAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQrGMSKANSEVAQWRTKYETDA 1381
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEE---LEAQLEELESKLDELAEELAELEEKLEELKEELE-SLEAELEELEAELEELESRL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1382 IQRTEELEEAKKKLAQRLQETEEA---VEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRnfDKVLSEW 1458
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLnneIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL--EEELEEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1459 KQKFEESQAELESSQKEARCLSTELFKLKNSYEEA---LDHLETMKRENKNLQEEISDLT---EQLGEGGKSIHELEKMR 1532
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALLknqSGLSGILGVLSELISVD 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1533 KQLEQEKSEI-------------QSALEEAEASLEHEEGKilRAQLEFSQIKAdieRKLAEKDEEMEQSKRNLQRTIDTL 1599
Cdd:TIGR02168 533 EGYEAAIEAAlggrlqavvvenlNAAKKAIAFLKQNELGR--VTFLPLDSIKG---TEIQGNDREILKNIEGFLGVAKDL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1600 QSSlesetrsrneALRIKKKMEGDLNEMEI--QLSQANRQAAEAQKQLKSVhahMKDAQLQLDDSLRTNEDLKENTAIVE 1677
Cdd:TIGR02168 608 VKF----------DPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYRIV---TLDGDLVRPGGVITGGSAKTNSSILE 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1678 RRNnllqaELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKA 1757
Cdd:TIGR02168 675 RRR-----EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1758 KKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiamkggkkQVQKLEARVRELESEVESEQKKSSE 1837
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE--------ELKALREALDELRAELTLLNEEAAN 821
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1838 AVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKAYKRAAEEAEEQANTNLSKFRKIQHELDEAEERADIAES 1917
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
810 820
....*....|....*....|.
gi 163644331 1918 QVNKLRAKSRDVSSKKGHDQE 1938
Cdd:TIGR02168 902 ELRELESKRSELRRELEELRE 922
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
867-1592 |
1.35e-26 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 119.40 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 867 KSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAKELTERLED--EEEMNA------EL 938
Cdd:TIGR02169 220 KREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRvkekigEL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 939 TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEEDK 1018
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1019 VNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIED 1098
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1099 EQTICIQLQKKLKELQARIEEleeeleaeraarakVEKQRADLARELEEISER---LEEAGGATAAQIEMNKKREAEFQK 1175
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDR--------------VEKELSKLQRELAEAEAQaraSEERVRGGRAVEEVLKASIQGVHG 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1176 LRRDLEEATLQHEA---TAATLRKK----QADSVAElgEQIDNLQRVKQ------KLEKEKSELR----LELDDVVSNME 1238
Cdd:TIGR02169 526 TVAQLGSVGERYATaieVAAGNRLNnvvvEDDAVAK--EAIELLKRRKAgratflPLNKMRDERRdlsiLSEDGVIGFAV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1239 HVVKTKANLEK----------MTRSLE---DQMNEYKTKYEEG----------------QRCINDFTMQKSKLQSENGEL 1289
Cdd:TIGR02169 604 DLVEFDPKYEPafkyvfgdtlVVEDIEaarRLMGKYRMVTLEGelfeksgamtggsrapRGGILFSRSEPAELQRLRERL 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1290 SRQLEEKDSLVSQLTRSKM---SYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKA 1366
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1367 NSEVAQwrtkYETDAIQRTEELEEAKKKLAQrlqeteEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDK 1446
Cdd:TIGR02169 764 EARIEE----LEEDLHKLEEALNDLEARLSH------SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1447 KQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSyeealdhLETMKRENKNLQEEISDLTEQLGEGGKSIH 1526
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA-------LRDLESRLGDLKKERDELEAQLRELERKIE 906
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 163644331 1527 ELEKMRKQLEQEKSEIQSALEEAEASLEHEEgKILRAQLEFSQIKADIErKLAEKDEEMEQSKRNL 1592
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSLE-DVQAELQRVEEEIRAL 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
922-1795 |
2.41e-26 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 118.25 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 922 KELTERLEDEEEMNAELTAKKRKLEDECSELKKdIDDLELTLAKVE-----KEKHATENKVKNLTEEMAALDDIIAKLTK 996
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 997 EKKALQEAHQQTLDDLQSEEDKVNTLTKAKA-KLEQQVDDLEGSLEQekklrmdlerakrkLEGDLKLTQESLMDLENDK 1075
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIAS--------------LERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1076 QQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARieeleeeleaeraarakvekqRADLARELEEISERLEEA 1155
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE---------------------LEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1156 ggataaqIEMNKKREAEFQKLRRDLEEatLQHEATAATLRKKQADS-VAELGEQIDNLQRVKQKLEKEKSELRLELDDVV 1234
Cdd:TIGR02169 384 -------RDELKDYREKLEKLKREINE--LKRELDRLQEELQRLSEeLADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1235 SNMEHVVKTKANLEKMTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKLQSENGELSRQLEEKDS-------LVSQLTRSK 1307
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGSVG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1308 MSYTQQIEDLKRQ------LEEETKAKSA--LAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYET 1379
Cdd:TIGR02169 535 ERYATAIEVAAGNrlnnvvVEDDAVAKEAieLLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEP 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1380 D---AIQRT---EELEEAKK--------KLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALD 1445
Cdd:TIGR02169 615 AfkyVFGDTlvvEDIEAARRlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQ 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1446 KKQRNFDKVLSEWKQKFEESQAELESSQKEArclstelfklknsyEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSI 1525
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKEI--------------EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1526 HELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQikaDIERKLAEKDEEMEQSKRNLQRTIDTLQSSLES 1605
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLE---EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1606 ETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKsvhahmkdaqlQLDDSLrtnEDLKEntaivERRNnlLQA 1685
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR-----------DLESRL---GDLKK-----ERDE--LEA 896
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1686 ELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLET------DISQLQTEVEEAVQECRNAEEKAKK 1759
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelSLEDVQAELQRVEEEIRALEPVNML 976
|
890 900 910
....*....|....*....|....*....|....*.
gi 163644331 1760 AITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDL 1795
Cdd:TIGR02169 977 AIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1261-1925 |
4.51e-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: 4.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1261 YKTKYEEGQRCINDFTMQKSKLQSENGELSRQLEekdSLVSQLTRskmsyTQQIEDLKRQLEEetKAKSALAHAVQSARH 1340
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLK---SLERQAEK-----AERYKELKAELRE--LELALLVLRLEELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1341 DTDLLREQYEEEQEAKAELQRGMSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTK 1420
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKL---------------EELRLEVSELEEEIEELQKELYALANEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1421 HRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETM 1500
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1501 KRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIK-ADIERKLA 1579
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEElERLEEALE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1580 EKDEEMEQSKRNLQ-------------RTIDTLQSSLESETRSRNEALRIKKKMEGDLN--------------EMEIQL- 1631
Cdd:TIGR02168 465 ELREELEEAEQALDaaerelaqlqarlDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlselisvdegyeaAIEAALg 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1632 ----------SQANRQAAEAQKQLKSVHAHM------KDAQLQ------------------------------------- 1658
Cdd:TIGR02168 545 grlqavvvenLNAAKKAIAFLKQNELGRVTFlpldsiKGTEIQgndreilkniegflgvakdlvkfdpklrkalsyllgg 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1659 ------LDDSLRTNEDLKENTAIV------------------ERRNNLL--QAELEELRAALEQTERGRKLAEQELLDTS 1712
Cdd:TIGR02168 625 vlvvddLDNALELAKKLRPGYRIVtldgdlvrpggvitggsaKTNSSILerRREIEELEEKIEELEEKIAELEKALAELR 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1713 ERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEK---AKKAITDA----AMMAEELKKEQDTSAHLERMK 1785
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqLSKELTELeaeiEELEERLEEAEEELAEAEAEI 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1786 KNMEQTIKDLQHRLDEAEQiAMKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLAR 1865
Cdd:TIGR02168 785 EELEAQIEQLKEELKALRE-ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1866 LQDLVDKLQLKVKAYKRAAEEAEEQANTNLSKFRKIQHELDEAEERADIAESQVNKLRAK 1925
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1134-1911 |
9.50e-26 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 116.32 E-value: 9.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1134 VEKQRAdlARELEEISERLEEAggataaQIEMNKKREaEFQKLRRDLEEAtlqhEATAATLRKKQADSVAELGEQIDNLQ 1213
Cdd:TIGR02169 170 RKKEKA--LEELEEVEENIERL------DLIIDEKRQ-QLERLRREREKA----ERYQALLKEKREYEGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1214 RVKQKLEKEKSELRLELDDVVSNMEHVVKTKANLEKMTRSLEDQMNEY-KTKYEEGQRCINDFTMQKSKLQSENGELSRQ 1292
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1293 LEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRgmskansEVAQ 1372
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-------ELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1373 WRTKYEtDAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFD 1452
Cdd:TIGR02169 390 YREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1453 KVLSEWKQKFEESQAELESSQKEarclstelfklknsyeeaLDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELekmR 1532
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRE------------------LAEAEAQARASEERVRGGRAVEEVLKASIQGVHGT---V 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1533 KQLEQEKSEIQSALE-------------------EAEASLEHEEG---------KILRAQLEFSQIK----ADIERKLAE 1580
Cdd:TIGR02169 528 AQLGSVGERYATAIEvaagnrlnnvvveddavakEAIELLKRRKAgratflplnKMRDERRDLSILSedgvIGFAVDLVE 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1581 KDEEMEQSKRNLQRTIDTLQS--------------SLESE-----------TRSRNEALRIKKKMEGDLNEMEIQLSQAN 1635
Cdd:TIGR02169 608 FDPKYEPAFKYVFGDTLVVEDieaarrlmgkyrmvTLEGElfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLK 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1636 RQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQELLDTSERV 1715
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARI 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1716 QLLHSQNTSLLNQKKKLETDISQlqTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDL 1795
Cdd:TIGR02169 768 EELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1796 QHRLDE-AEQIAMKGGKK-----QVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDL 1869
Cdd:TIGR02169 846 KEQIKSiEKEIENLNGKKeeleeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 163644331 1870 VDKLQLKVKAYKRAAEEAEEQANTNLSkFRKIQHELDEAEER 1911
Cdd:TIGR02169 926 LEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
861-1603 |
8.61e-25 |
|
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: 113.35 E-value: 8.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 861 LKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCD-------QLIKNKIQLEAKAKELTERLEDEEE 933
Cdd:pfam01576 206 LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEeetaqknNALKKIRELEAQISELQEDLESERA 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 934 MNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEemaALDDIIAKLTKEKKALQEAHQQTLDDLQ 1013
Cdd:pfam01576 286 ARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKK---ALEEETRSHEAQLQEMRQKHTQALEELT 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1014 SEEDKVN----TLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEI 1089
Cdd:pfam01576 363 EQLEQAKrnkaNLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1090 SQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATAAQIEMNKKR 1169
Cdd:pfam01576 443 ESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1170 EAEFQKLRRDLEEATLQHEATAATLRKKQADSVAeLGEQIDNLQRVKQKLEKEKSELRLELDDVVSNMEHVVKTKANLEK 1249
Cdd:pfam01576 523 QAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEA-LTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEK 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1250 MTRSLEDQMNEYKT---KYEEGQ------------------RCINDFTMQKSKLQSENGELSRQLEE----KDSL---VS 1301
Cdd:pfam01576 602 KQKKFDQMLAEEKAisaRYAEERdraeaeareketralslaRALEEALEAKEELERTNKQLRAEMEDlvssKDDVgknVH 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1302 QLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKA-NSEVAQWRTKYETD 1380
Cdd:pfam01576 682 ELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQlVKQVRELEAELEDE 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1381 AIQRTEELEeAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAA-------AAALDKKQRNF-- 1451
Cdd:pfam01576 762 RKQRAQAVA-AKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASrdeilaqSKESEKKLKNLea 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1452 ------------DKVLSEWKQKFEESQAELESS-------QKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEIS 1512
Cdd:pfam01576 841 ellqlqedlaasERARRQAQQERDELADEIASGasgksalQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVE 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1513 DLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAE--------ASLEHEEGKILRAQLEFSQ--------------- 1569
Cdd:pfam01576 921 QLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEgtvkskfkSSIAALEAKIAQLEEQLEQesrerqaanklvrrt 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1570 --------IKADIERKLAE--KD----------------EEMEQ-------SKRNLQRTID--------------TLQSS 1602
Cdd:pfam01576 1001 ekklkevlLQVEDERRHADqyKDqaekgnsrmkqlkrqlEEAEEeasranaARRKLQRELDdatesnesmnrevsTLKSK 1080
|
.
gi 163644331 1603 L 1603
Cdd:pfam01576 1081 L 1081
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
916-1541 |
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 163644331 916 QLEAKAKELTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLT 995
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 996 KEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDK 1075
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1076 QQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARakvEKQRADLARELEEISERLEEA 1155
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE---AELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1156 GGATAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQADSVAELGEQIDNLQRVKQKLEK--EKSELRLELDDV 1233
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAalEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1234 VSNMEHVVK-----TKANLEKMTRSLEDQmneyktkyeegqrcindftMQKSKLQSENGELSRQLEEKDSLVSQLTRSKM 1308
Cdd:COG1196 553 VEDDEVAAAaieylKAAKAGRATFLPLDK-------------------IRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1309 SYTQQIEDLKRQLEEETKAKSALAHAVQsarhdtdLLREQYEEEQEAKAELQRGMSKANSEVAQwrtkyETDAIQRTEEL 1388
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVT-------LAGRLREVTLEGEGGSAGGSLTGGSRREL-----LAALLEAEAEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1389 EEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAE 1468
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1469 LESSQKEARclstelfKLKNSYEE-------ALDHLETMKRENKNLQEEISDLTEqlgeggkSIHELEKMRKQLEQEKSE 1541
Cdd:COG1196 762 LEELERELE-------RLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEE-------ARETLEEAIEEIDRETRE 827
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1288-1870 |
2.88e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.02 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1288 ELSRQLEEKDSLVSQLTRSKmsYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKAN 1367
Cdd:COG1196 217 ELKEELKELEAELLLLKLRE--LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1368 SEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKK 1447
Cdd:COG1196 295 AELAR--------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1448 QRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHE 1527
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1528 LEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIKADIERKLAEKDEEM---EQSKRNLQRTIDTLQSSLE 1604
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflEGVKAALLLAGLRGLAGAV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1605 SETRSRNEALRikKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQ 1684
Cdd:COG1196 527 AVLIGVEAAYE--AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1685 AELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAITDA 1764
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1765 AmmAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAMKGGKKQVQKLEARVRELESEVESEQ---------KKS 1835
Cdd:COG1196 685 A--ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEealeelpepPDL 762
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 163644331 1836 SEAVKGIRKYERRIKEL---------TYQTEEDRKN--LARLQDLV 1870
Cdd:COG1196 763 EELERELERLEREIEALgpvnllaieEYEELEERYDflSEQREDLE 808
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1312-1911 |
3.30e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.63 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1312 QQIEDLKRQ-----------LEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVaqwrtkyetd 1380
Cdd:COG1196 200 RQLEPLERQaekaeryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL---------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1381 aiqrtEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQ 1460
Cdd:COG1196 270 -----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1461 KFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQlgeggksIHELEKMRKQLEQEKS 1540
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-------LEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1541 EIQSALEEAEASLEHEEGKILRAQLEFSQIKADIERKLAEKDEEMEQSKRNLQRtidtlQSSLESETRSRNEALRIKKKM 1620
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE-----AALLEAALAELLEELAEAAAR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1621 EGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTERG 1700
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1701 RklAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQEcrnAEEKAKKAITDAAMMAEELKKEQDTSAH 1780
Cdd:COG1196 573 R--ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG---DTLLGRTLVAARLEAALRRAVTLAGRLR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1781 LERMKKNMEQTIKDLQHRLDEAEQIAMKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDR 1860
Cdd:COG1196 648 EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 163644331 1861 KNLARLQDLVDKLQLKVKAYKRAAEEAEEQANTNLSkfrKIQHELDEAEER 1911
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLE---ELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
841-1454 |
3.59e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.63 E-value: 3.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 841 LLKSAEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQdnlcdAEERcdQLIKNKIQLEAK 920
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-----AEEY--ELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 921 AKELTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKA 1000
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1001 LQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEE 1080
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1081 RLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLA-RELEEISERLEEAGGAT 1159
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvAVLIGVEAAYEAALEAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1160 AAQIEMNKKREAEFQ-KLRRDLEEATLQHEATAATLRKKQADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNME 1238
Cdd:COG1196 544 LAAALQNIVVEDDEVaAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1239 HVVKTKANLEKMTRSLEDQMNEYKTKYEEGQrcinDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLK 1318
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGE----GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1319 RQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLA-- 1396
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEal 779
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 163644331 1397 --------QRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLmvDLERSNAAAAALDKKQRNFDKV 1454
Cdd:COG1196 780 gpvnllaiEEYEELEERYDFLSEQREDLEEARETLEEAIEEI--DRETRERFLETFDAVNENFQEL 843
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
219-708 |
4.03e-21 |
|
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: 100.97 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 219 IIQANPALEAFGNAKTIRNDNSSRFGKF--IRIHFGASG---KLASADIETYLLEKSRVTFQL------KAERDYHIFYQ 287
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 288 ILSQRKPELLEMLLITNNPYD------YAYISQGETTVASINDGEELLATD--------EAFDVLGFTQEEKNGIYKLIG 353
Cdd:cd14894 329 MVAGVNAFPFMRLLAKELHLDgidcsaLTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 354 AIMHFGNMKFKQKQREEQAEADGT---EDGDKVAYLMGLNSADLIKGLCHPR---VKVGNEWVTKGQNVQQVYYAIGALA 427
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 428 KSVYEKMFLWMVVRINQ-----SLDTKQPRQY------------FIGVLDIAGFEIFDFNTFEQLCINFTNEKLQQFFNH 490
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEatkmsALSTDGNKHQmdsnasapeavsLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYAREEQ 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 491 HMFVLEQEEYKKEGIEWEfidfgmdlQACIDLIEKPMGIMSILEEECMFPKAS----------DSTFKAKLYDNHlgkSN 560
Cdd:cd14894 569 VIAVAYSSRPHLTARDSE--------KDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDRN---SS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 561 NFQKPRAIKGKPESH---------FSLVHYAGTVDYNINNWLVKNKDPL-NETVVGLFQKSTVKLLSMLFANYAGTESDN 630
Cdd:cd14894 638 RLPEPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLNESSQLGWSPN 717
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163644331 631 GKGGKGGGSKKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMENPLVMHQLRCNGVLEGIRICR 708
Cdd:cd14894 718 TNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1024-1749 |
5.34e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.31 E-value: 5.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1024 KAKAKLEQ------QVDDLEGSLE-QEKKLRMDLERAKR--KLEGDLKLTQESLM-----DLENDKQQLEERLKKKDFEI 1089
Cdd:COG1196 176 EAERKLEAteenleRLEDILGELErQLEPLERQAEKAERyrELKEELKELEAELLllklrELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1090 SQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATAAQIEMNKKR 1169
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1170 EAEFQKLRRDLEEATLQHEATAATLRKKQADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDVvsnmehvvKTKANLEK 1249
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA--------AQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1250 MTRSLEDQMNEYKTKYEEGQRcindftmQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKS 1329
Cdd:COG1196 408 AEEALLERLERLEEELEELEE-------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1330 ALAHAVQSARhdtdlLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEEakkklaqrlqetEEAVEAv 1409
Cdd:COG1196 481 ELLEELAEAA-----ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY------------EAALEA- 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1410 nakcsslektkhRLQNEIEDLMVDLERSNAAAAALDKKQRnfdkvlsEWKQKFEESQAELESSQKEARCLSTELFKLKNS 1489
Cdd:COG1196 543 ------------ALAAALQNIVVEDDEVAAAAIEYLKAAK-------AGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1490 YEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEfsq 1569
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE--- 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1570 iKADIERKLAEKDEEMEQSKRNLqrtidtlqsslESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQlksvh 1649
Cdd:COG1196 681 -LEELAERLAEEELELEEALLAE-----------EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE----- 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1650 ahmkdAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELraaleqterGR--KLAEQELLDTSERVQLLHSQNTSLLN 1727
Cdd:COG1196 744 -----EEELLEEEALEELPEPPDLEELERELERLEREIEAL---------GPvnLLAIEEYEELEERYDFLSEQREDLEE 809
|
730 740
....*....|....*....|..
gi 163644331 1728 QKKKLETDISQLQTEVEEAVQE 1749
Cdd:COG1196 810 ARETLEEAIEEIDRETRERFLE 831
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1276-1874 |
7.15e-20 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 97.17 E-value: 7.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1276 TMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDlKRQLEEETKAKSalahavqsarhdtdllrEQYEEEQEA 1355
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEE-KNALQEQLQAET-----------------ELCAEAEEM 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1356 KAELqrgmskansevaqwrtkyetdaIQRTEELEEAKKKLAQRLQETEEaveavnaKCSSLEKTKHRLQNEIEDLMVDLE 1435
Cdd:pfam01576 63 RARL----------------------AARKQELEEILHELESRLEEEEE-------RSQQLQNEKKKMQQHIQDLEEQLD 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1436 RSNAAAAAL-------DKKQRNFDK----------VLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLE 1498
Cdd:pfam01576 114 EEEAARQKLqlekvttEAKIKKLEEdillledqnsKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1499 T-MKRENKNLQE----------EISDLTEQLGEGGKSIHELekmRKQLEQEKSEIQSAL---EEAEASLEHEEGKILRAQ 1564
Cdd:pfam01576 194 ErLKKEEKGRQElekakrklegESTDLQEQIAELQAQIAEL---RAQLAKKEEELQAALarlEEETAQKNNALKKIRELE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1565 LEFSQIKADIE-----RKLAEK-----DEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQA 1634
Cdd:pfam01576 271 AQISELQEDLEseraaRNKAEKqrrdlGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEM 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1635 NRQAAEAQKQLksvhahmkdaQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQELldtser 1714
Cdd:pfam01576 351 RQKHTQALEEL----------TEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQL------ 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1715 vQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKN------- 1787
Cdd:pfam01576 415 -QELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNlstrlrq 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1788 MEQTIKDLQHRLDEAEQiAMKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQ 1867
Cdd:pfam01576 494 LEDERNSLQEQLEEEEE-AKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLE 572
|
....*..
gi 163644331 1868 DLVDKLQ 1874
Cdd:pfam01576 573 KTKNRLQ 579
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
970-1637 |
7.63e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.93 E-value: 7.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 970 KHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTL--DDLQSEED--KVNTLTKAKAKLEQQVDDLEGSLEQEKK 1045
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAEryRELKEELKelEAELLLLKLRELEAELEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1046 LRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELeeele 1125
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL----- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1126 aeraarakvEKQRADLARELEEISERLEEAggatAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQADSVAEL 1205
Cdd:COG1196 329 ---------EEELEELEEELEELEEELEEA----EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1206 GEQIDNLQRVKQKLEKEKSELrlelddvvsnmehvvktkANLEKMTRSLEDQMNEYKTKYEEGQRcindftmQKSKLQSE 1285
Cdd:COG1196 396 AELAAQLEELEEAEEALLERL------------------ERLEEELEELEEALAELEEEEEEEEE-------ALEEAAEE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1286 NGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQyeeeqeAKAELQRGMSK 1365
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA------LLLAGLRGLAG 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1366 ANSEVAQWRTKYETDAIQRteeleeakkkLAQRLQETEEAVEAVNAKCSSLEKtKHRLQNEIEDLMVDLERSNAAAAALD 1445
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAA----------LAAALQNIVVEDDEVAAAAIEYLK-AAKAGRATFLPLDKIRARAALAAALA 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1446 KKQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLEtmkrenknlqEEISDLTEQLGEGGKSI 1525
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRL----------REVTLEGEGGSAGGSLT 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1526 HELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLES 1605
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
650 660 670
....*....|....*....|....*....|..
gi 163644331 1606 ETRSRNEALRIKKKMEGDLNEMEIQLSQANRQ 1637
Cdd:COG1196 744 EEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
867-1555 |
9.00e-20 |
|
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: 96.24 E-value: 9.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 867 KSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLiKNKIQ-LEAKAKELTERLEDEEEMNAELTAKKRKL 945
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNS-NNKIKiLEQQIKDLNDKLKKNKDKINKLNSDLSKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 946 EDECSELKKDIDDLELTLAKVEKE-KHATENKVKNLTEemaalddiIAKLTKEKKALQEAHQQTLDDLQSEEDKVNTLTK 1024
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVELNKLEKQkKENKKNIDKFLTE--------IKKKEKELEKLNNKYNDLKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1025 AKAKLEQQVDDLEGSLEQEKKLRMDLErakrKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICI 1104
Cdd:TIGR04523 181 EKLNIQKNIDKIKNKLLKLELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1105 QLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEaggataaqiEMNKKREAEFQKLRRDLEEAT 1184
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ---------DWNKELKSELKNQEKKLEEIQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1185 LQheataatlRKKQADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNMEHVVKTKANLEKMTRSLEDQMNEYKTK 1264
Cdd:TIGR04523 328 NQ--------ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1265 YEEGQRCINDFTMQKSKLQSENGELSRQLEEkdslvsqltrskmsYTQQIEDLKRQLEEETKAKSALAHAVQSArhdtdl 1344
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIER--------------LKETIIKNNSEIKDLTNQDSVKELIIKNL------ 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1345 lrEQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQ 1424
Cdd:TIGR04523 460 --DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1425 NEIEDLMVDLERSNAaaaalDKKQRNFDKVLSEWKQKFEESQAELESsqkearclstelfkLKNSYEEALDHLETMKREN 1504
Cdd:TIGR04523 538 SKISDLEDELNKDDF-----ELKKENLEKEIDEKNKEIEELKQTQKS--------------LKKKQEEKQELIDQKEKEK 598
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 163644331 1505 KNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEH 1555
Cdd:TIGR04523 599 KDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1085-1840 |
1.06e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.13 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1085 KDFEISQLNGKIEDEQTIciQLQKKLKELQARIEELEEELEAERAARAKVEK-QRADLARELEEIsERLEEAGGATAAQI 1163
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATE--EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDaRKAEEARKAEDA-RKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1164 EMNKKREAEFQKLR--RDLEEATLQHEA-TAATLRKKQADSVAELGEQIDNLQRVKQKLEKEKSElRLELDDVVSNMEHV 1240
Cdd:PTZ00121 1154 VEIARKAEDARKAEeaRKAEDAKKAEAArKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1241 VKTKANLEKMTRSLEDQMNEYKTKYEEGQrcINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQ 1320
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEAR--MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1321 LEEETKAKSALAHAvQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEE---LEEAKKKLAQ 1397
Cdd:PTZ00121 1311 AEEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkADAAKKKAEE 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1398 RLQETEEAVEAVNAKCSSLE-KTKHRLQNEIEDLMVDLERSNAAAAAldKKQRNFDKVLSEWKQKFEESQAELESSQKEA 1476
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1477 RCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQlGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHE 1556
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1557 EGKILRAQLEfsqIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDlnemEIQLSQANR 1636
Cdd:PTZ00121 1547 KADELKKAEE---LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE----EAKKAEEAK 1619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1637 QAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDL-KENTAIVERRNNLLQAELEELRAA--LEQTERGRKLAEQELLDTSE 1713
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAE 1699
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1714 rvqllhsqntsllnQKKKLEtdisQLQTEVEEavqECRNAEEkAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIK 1793
Cdd:PTZ00121 1700 --------------EAKKAE----ELKKKEAE---EKKKAEE-LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 163644331 1794 DLQHRLDEAEQIAMKGGKKQVQKLEARVRELESEVESEQKKSSEAVK 1840
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1311-1933 |
1.14e-19 |
|
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: 96.40 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1311 TQQIEDLKRQLEEETKAKSALAHAvQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETdaiqRTEELEE 1390
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKA-ESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAA----RKQELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1391 AKKKLAQRLQETEEaveavnaKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAAL-------DKKQRNFDK---------- 1453
Cdd:pfam01576 76 ILHELESRLEEEEE-------RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLqlekvttEAKIKKLEEdillledqns 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1454 VLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLET-MKRENKNLQE----------EISDLTEQLGEGG 1522
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEErLKKEEKGRQElekakrklegESTDLQEQIAELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1523 KSIHELekmRKQLEQEKSEIQSAL---EEAEASLEHEEGKILRAQLEFSQIKADIE-----RKLAEK-----DEEMEQSK 1589
Cdd:pfam01576 229 AQIAEL---RAQLAKKEEELQAALarlEEETAQKNNALKKIRELEAQISELQEDLEseraaRNKAEKqrrdlGEELEALK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1590 RNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLksvhahmkdaQLQLDDSLRTNEDL 1669
Cdd:pfam01576 306 TELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL----------TEQLEQAKRNKANL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1670 KENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQELldtservQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQE 1749
Cdd:pfam01576 376 EKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQL-------QELQARLSESERQRAELAEKLSKLQSELESVSSL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1750 CRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKN-------MEQTIKDLQHRLDEAEQiAMKGGKKQVQKLEARVR 1822
Cdd:pfam01576 449 LNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNlstrlrqLEDERNSLQEQLEEEEE-AKRNVERQLSTLQAQLS 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1823 ELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEED-------RKNLARLQD--------------LVDKLQLKVKAYK 1881
Cdd:pfam01576 528 DMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKaaaydklEKTKNRLQQelddllvdldhqrqLVSNLEKKQKKFD 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 163644331 1882 RAAEEAEEQANTNL--------------SKFRKIQHELDEAEERADIAESQVNKLRAKSRDVSSKK 1933
Cdd:pfam01576 608 QMLAEEKAISARYAeerdraeaearekeTRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK 673
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1272-1925 |
1.24e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 96.29 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1272 INDFTMQKSKLQSENGELSRQLEEKDSLVS----QLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLRE 1347
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDekrqQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1348 QYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEI 1427
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1428 EDLMVDLERSNAAAAALDKKQRNFDK-------VLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETM 1500
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKrrdklteEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1501 KRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIKADIERklae 1580
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR---- 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1581 KDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEG------DLNEME------IQLSQANR----------QA 1638
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGvhgtvaQLGSVGeryataIEVAAGNRlnnvvveddaVA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1639 AEAQKQLKSVHA---------HMKDAQLQLDDSLRTNE-----DLKE--------------NTAIVER-----------R 1679
Cdd:TIGR02169 561 KEAIELLKRRKAgratflplnKMRDERRDLSILSEDGVigfavDLVEfdpkyepafkyvfgDTLVVEDieaarrlmgkyR 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1680 NNLLQAELEELRAALEQTERGRKLAE-------QELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRN 1752
Cdd:TIGR02169 641 MVTLEGELFEKSGAMTGGSRAPRGGIlfsrsepAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1753 AEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAE-------------------------QIAM 1807
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEedlhkleealndlearlshsripeiQAEL 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1808 KGGKKQVQKLEARVRELESEV-------ESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKAY 1880
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLnrltlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 163644331 1881 KRAAEEAEEQANTNLSKFRKIQHELDEAEERADIAESQVNKLRAK 1925
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
937-1598 |
2.74e-19 |
|
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: 94.70 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 937 ELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDiiaKLTKEKKALQEAHQqtldDLQSEE 1016
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLND---KLKKNKDKINKLNS----DLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1017 DKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKI 1096
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1097 EDEQTICIQLQKKLKELQARIeeleEELEAERAARAKVEKQRADLARELEEISERLEEaggataaqiemnkkREAEFQKL 1176
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKI----QKNKSLESQISELKKQNNQLKDNIEKKQQEINE--------------KTTEISNT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1177 RRDLEEATLQHEATAATLRKKQADsVAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNmeHVVKTKANLEKMTRSLED 1256
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKE-LEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1257 QMNEYKTKYEEGQRCINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQleeetkaKSALAHAVQ 1336
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ-------INDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1337 SARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSL 1416
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK-DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1417 EKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKnsYEEALDH 1496
Cdd:TIGR04523 481 KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD--FELKKEN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1497 LETMKRENknlQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIKAdIER 1576
Cdd:TIGR04523 559 LEKEIDEK---NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS-IIK 634
|
650 660
....*....|....*....|..
gi 163644331 1577 KLAEKDEEMEQSKRNLQRTIDT 1598
Cdd:TIGR04523 635 NIKSKKNKLKQEVKQIKETIKE 656
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
990-1803 |
3.67e-19 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 94.80 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 990 IIAKLTKE--KKALQEAHQQtLDDLQSEEDKVNTL-TKAKAKLEQQVDDLEGSLEQ---EKKLRMDLERAKRKLEGDLK- 1062
Cdd:pfam15921 67 IIAYPGKEhiERVLEEYSHQ-VKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLRn 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1063 LTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKEL-QARIEELEEELEAERAARAKVEKQRADL 1141
Cdd:pfam15921 146 QLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFeEASGKKIYEHDSMSTMHFRSLGSAISKI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1142 ARELE-EIS----------ERLEeaggatAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQADSVAELGEQID 1210
Cdd:pfam15921 226 LRELDtEISylkgrifpveDQLE------ALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1211 NLQRVKQKLEKEKSELRLELDDVVSNmehVVKTKANLEKMTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKLQSENGELS 1290
Cdd:pfam15921 300 QLEIIQEQARNQNSMYMRQLSDLEST---VSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1291 RQLEEkdsLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAHavqsarhdtdlLREQYEEEQeakAELQR--GMSKANS 1368
Cdd:pfam15921 377 DQLQK---LLADLHKREKELSLEKEQNKRLWDRDTGNSITIDH-----------LRRELDDRN---MEVQRleALLKAMK 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1369 EVAQWRTKYETDAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKq 1448
Cdd:pfam15921 440 SECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE- 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1449 rnFDKVLSEWKQKFEESQaELESSQKEARCLSTELFKLKNSYEEALDHLETmkrenknLQEEISDLTEQLGEGGKSIHEL 1528
Cdd:pfam15921 519 --ITKLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEI-------LRQQIENMTQLVGQHGRTAGAM 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1529 EKMRKQLEQEKSEIQSALEEAEASLEHEEGKI--LRAQ---LEFSQIK---ADIERKLAEKDeeMEQSKRNLQRTIDTLQ 1600
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIreLEARvsdLELEKVKlvnAGSERLRAVKD--IKQERDQLLNEVKTSR 666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1601 SSLESETRsrnEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRN 1680
Cdd:pfam15921 667 NELNSLSE---DYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQI 743
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1681 NLLQAELEELRAALEQTERGRKLAEQELLDTSERVqllhsqnTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKA 1760
Cdd:pfam15921 744 DALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL-------STVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA 816
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 163644331 1761 ITDAAMMAEELKKEQDTSAHLErmkknmeqtikdLQHRLDEAE 1803
Cdd:pfam15921 817 SLQFAECQDIIQRQEQESVRLK------------LQHTLDVKE 847
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
837-1623 |
1.01e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.67 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 837 KIKPLLKSAEAEK-EMANMKDEFAKLKEAYAKSEARRKElEEKMVSLLQEKNDLQLQVQAEQDN---LCDAEERCDQLIK 912
Cdd:PTZ00121 1189 KAEELRKAEDARKaEAARKAEEERKAEEARKAEDAKKAE-AVKKAEEAKKDAEEAKKAEEERNNeeiRKFEEARMAHFAR 1267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 913 NKIQLEAKAKELTERLEDEEEMNAELTAKKRKLEDECSELKKdiddleltlaKVEKEKHATENKVKnlTEEMAALDDIIA 992
Cdd:PTZ00121 1268 RQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK----------KAEEAKKADEAKKK--AEEAKKKADAAK 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 993 KLTKEKKALQEAhqqtlddlqseedkvntltkAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLE 1072
Cdd:PTZ00121 1336 KKAEEAKKAAEA--------------------AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1073 NDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAeraarakveKQRADLARELEEISERL 1152
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA---------KKKAEEAKKAEEAKKKA 1466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1153 EEAGGATAAQIEMNKKREAEfqKLRRDLEEAtlqheataatlrKKQADSVAELGEQIDNLQRVKQKLEKEKS-ELRLELD 1231
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKAD--EAKKKAEEA------------KKKADEAKKAAEAKKKADEAKKAEEAKKAdEAKKAEE 1532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1232 DVVSNMEHVVKTKANLEKMTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKlqsenGELSRQLEEKdSLVSQLTRSKMSYT 1311
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK-----AEEAKKAEEA-RIEEVMKLYEEEKK 1606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1312 QQIEDLKRqlEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAiQRTEEL--- 1388
Cdd:PTZ00121 1607 MKAEEAKK--AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkka 1683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1389 -EEAKKKLAQRLQETEEA--VEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAAlDKKQRNFDKVLSEWKQKFEES 1465
Cdd:PTZ00121 1684 eEDEKKAAEALKKEAEEAkkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE-DKKKAEEAKKDEEEKKKIAHL 1762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1466 QAELESSQKEARCLSTELFKlknsyEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKqlEQEKSEIQ-- 1543
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK--EMEDSAIKev 1835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1544 -----SALEEAEASLEHEEGK-ILRAQLEFSQIKADIERKLAEKD-EEMEQSKRNLQRTIDTLQSSLESETRSRNEALRI 1616
Cdd:PTZ00121 1836 adsknMQLEEADAFEKHKFNKnNENGEDGNKEADFNKEKDLKEDDeEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDII 1915
|
....*..
gi 163644331 1617 KKKMEGD 1623
Cdd:PTZ00121 1916 DDKLDKD 1922
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1416-1928 |
7.39e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 7.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1416 LEKTKHRLqNEIEDLMVDLER--------SNAA--AAALDKKQRNFDKVLS-----EWKQKFEESQAELESSQKEARCLS 1480
Cdd:COG1196 181 LEATEENL-ERLEDILGELERqleplerqAEKAerYRELKEELKELEAELLllklrELEAELEELEAELEELEAELEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1481 TELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKI 1560
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1561 LRAQLEFSQIKADIERKLAEKDEEmEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAE 1640
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEA-EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1641 AQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHS 1720
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1721 QNTS------------LLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAI-----TDAAMMAEELKKEQD---TSAH 1780
Cdd:COG1196 499 AEADyegflegvkaalLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIvveddEVAAAAIEYLKAAKAgraTFLP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1781 LERMKKNmEQTIKDLQHRLDEAEQIAMKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTY------ 1854
Cdd:COG1196 579 LDKIRAR-AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLegeggs 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1855 --------QTEEDRKNLARLQDLVDKLQLKVKAYKRAAEEAEEQANTNLSKFRKIQHELDEAEERADIAESQVNKLRAKS 1926
Cdd:COG1196 658 aggsltggSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
..
gi 163644331 1927 RD 1928
Cdd:COG1196 738 LE 739
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
832-1513 |
8.01e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.97 E-value: 8.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 832 MKLFFKIKPLLKSAEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDlQLQVQAEQdnlcdAEERCDQLi 911
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEE-----AKKKADAA- 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 912 KNKIQLEAKAKELTERLEDEEEMNAELTAKKRKL-EDECSELKKDIDDLEltlAKVEKEKHATENKVKnlTEEMAALDDI 990
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKEEAKKKADAAK---KKAEEKKKADEAKKK--AEEDKKKADE 1409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 991 IAKLTKEKKALQEAHQqtlddlQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGD-LKLTQESLM 1069
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKK------KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAEEAK 1483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1070 DLENDKQQLEERLKKKDfEISqlngKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEIS 1149
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKAD-EAK----KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1150 ERLEEaggataAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQADSVAELGEQIDNLQRVKQKLEKEKSElrle 1229
Cdd:PTZ00121 1559 KAEEK------KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA---- 1628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1230 lDDVVSNMEHVVKTKANLEKMTRSLEDQMNEYKTKYEEGQRcindftmqKSKLQSENGELSRQLEEKDSLVSQLTRSKMS 1309
Cdd:PTZ00121 1629 -EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK--------KAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1310 YTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQyEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEEL- 1388
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKe 1778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1389 ----EEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSewKQKFEE 1464
Cdd:PTZ00121 1779 avieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFE--KHKFNK 1856
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 163644331 1465 SQAELESSQKEARcLSTELFKLKNSYEEALDHLETMKRENKNLQEEISD 1513
Cdd:PTZ00121 1857 NNENGEDGNKEAD-FNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1202-1913 |
1.01e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.59 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1202 VAELGEQIDNLQRVKQK----LEKEK-SELRLELDDVVSNMEHVVKTKANLE--KMTRSLEDQM-NEYKTKYEEGQRCIN 1273
Cdd:PTZ00121 1029 IEELTEYGNNDDVLKEKdiidEDIDGnHEGKAEAKAHVGQDEGLKPSYKDFDfdAKEDNRADEAtEEAFGKAEEAKKTET 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1274 DFTMQKSKLQS--ENGELSRQLEE--KDSLVSQLTRSKMSYTQQIEDLKRQLEEETKA----KSALAHAVQSARHDTDLL 1345
Cdd:PTZ00121 1109 GKAEEARKAEEakKKAEDARKAEEarKAEDARKAEEARKAEDAKRVEIARKAEDARKAeearKAEDAKKAEAARKAEEVR 1188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1346 R----EQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEEL----EEAKKKLAQRLQET----EEAVEAVNAKC 1413
Cdd:PTZ00121 1189 KaeelRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAkkdaEEAKKAEEERNNEEirkfEEARMAHFARR 1268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1414 SSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARclstelfKLKNSYEEA 1493
Cdd:PTZ00121 1269 QAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKAD-------AAKKKAEEA 1341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1494 LDHLETMKRENKNLQEEISdlteqlgeggKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEgkiLRAQLEFSQIKAD 1573
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAE----------AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE---AKKKAEEDKKKAD 1408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1574 IERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRiKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHaHMK 1653
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK-KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK-KAD 1486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1654 DAQLQLDDSLRTNEDLKENTAIVERRNNLLQAE----LEELRAALE--QTERGRKLAEQELLDTSERVQ-LLHSQNTSLL 1726
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeakkADEAKKAEEakKADEAKKAEEKKKADELKKAEeLKKAEEKKKA 1566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1727 NQKKKLETDISQLQTEVEEAVQ-ECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQI 1805
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1806 -AMKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKnlarlqdlVDKLQLKVKAYKRAA 1884
Cdd:PTZ00121 1647 kKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK--------AEELKKKEAEEKKKA 1718
|
730 740
....*....|....*....|....*....
gi 163644331 1885 EEAEEQANTNLSKFRKIQHELDEAEERAD 1913
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1141-1872 |
1.36e-17 |
|
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: 89.79 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1141 LARELEEISERLEEAGGATAAQIEMNKKREAEFQK----LRRDLEEATLQHEATAaTLRKKQADSVAELGEQidnLQRVK 1216
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidLQTKLQEMQMERDAMA-DIRRRESQSQEDLRNQ---LQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1217 QKLEKEKSELRLELDDVVSNMEHvvktkanLEKMTRSLEDQMNEYKT---KYEE--GQRCINDFTMQKSKLQSENGELSR 1291
Cdd:pfam15921 152 HELEAAKCLKEDMLEDSNTQIEQ-------LRKMMLSHEGVLQEIRSilvDFEEasGKKIYEHDSMSTMHFRSLGSAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1292 QLEEKDSLVSQLTRSKMSYTQQIEDLKRQ-------------------LEEETKAKSALAHAVQSARHDTDLLREQYEEE 1352
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKSEsqnkielllqqhqdrieqlISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1353 QEA----KAELQRGMSKANSEVAQWRTkyetdaiqrteELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHR------ 1422
Cdd:pfam15921 305 QEQarnqNSMYMRQLSDLESTVSQLRS-----------ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQfsqesg 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1423 -LQNEIEDLMVDL-ERSNAAAAALDKKQRNFDKVLSEwKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALD-HLET 1499
Cdd:pfam15921 374 nLDDQLQKLLADLhKREKELSLEKEQNKRLWDRDTGN-SITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMErQMAA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1500 MKRENKNLqEEISDLTEQLgEGGKSIheLEKMRKQLEQEKSEIQSA---LEEAEASLEHEEGKILRAQLEFSQIKADIER 1576
Cdd:pfam15921 453 IQGKNESL-EKVSSLTAQL-ESTKEM--LRKVVEELTAKKMTLESSertVSDLTASLQEKERAIEATNAEITKLRSRVDL 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1577 KLAEKdeemeQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQ 1656
Cdd:pfam15921 529 KLQEL-----QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1657 LQLDDsLRTNEDlKENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQElldtSERVQLLHSQNTSLlNQKKKLETDI 1736
Cdd:pfam15921 604 LELQE-FKILKD-KKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIK----QERDQLLNEVKTSR-NELNSLSEDY 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1737 SQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEE----LKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAE------QIA 1806
Cdd:pfam15921 677 EVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQtrntLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQskiqflEEA 756
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 163644331 1807 MKGGKKQVQKLEARVRELESE---VESEQKKSSEAVKGIRKYERRIKELTYQTEE--DRKNL--ARLQDLVDK 1872
Cdd:pfam15921 757 MTNANKEKHFLKEEKNKLSQElstVATEKNKMAGELEVLRSQERRLKEKVANMEValDKASLqfAECQDIIQR 829
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
974-1648 |
2.20e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 88.54 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 974 ENKVKNLTEEMAALDDIIAKLTKEKKALQeahqqtlDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERA 1053
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLD-------KNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1054 KRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAK 1133
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1134 VEKQRADLARELEEISERLeeaggataAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQADSVAELGEQIDNLQ 1213
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLL--------SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1214 RVKQKLEKEKSELRLELDDVVSNmehvvktkanlEKMTRSLEDQMNEYKTKYEEgqrcindftMQKSKLQSENGELSRQL 1293
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKELEQN-----------NKKIKELEKQLNQLKSEISD---------LNNQKEQDWNKELKSEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1294 EEKDslvsqltrskmsytQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQW 1373
Cdd:TIGR04523 317 KNQE--------------KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1374 RtkyetdaiQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDK 1453
Cdd:TIGR04523 383 K--------QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1454 VLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRK 1533
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1534 QLEQEKSEIQSALEEAEASLEHE--EGKILRAQLEFSQIKADIERKLAEKDE------EMEQSKRNLQRTIDTLQSSLES 1605
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEkqelidQKEKEKKDLIKEIEEKEKKISS 614
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 163644331 1606 ETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSV 1648
Cdd:TIGR04523 615 LEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEI 657
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
902-1604 |
4.57e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 88.05 E-value: 4.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 902 DAEERCDQLIKNKIQLEA------KAKELTERLEDEEEMNAELTAKKRKLEdecselKKDIDDLELTLAKVEKEKHATEN 975
Cdd:COG4913 222 DTFEAADALVEHFDDLERahealeDAREQIELLEPIRELAERYAAARERLA------ELEYLRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 976 KVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEEdkvntlTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKR 1055
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1056 KLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTiciQLQKKLKELQARIEEleeeleaeraarakVE 1135
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR---DLRRELRELEAEIAS--------------LE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1136 KQRADLARELEEISERLEEAGGATAAQ-------IEMnKKREAEFQK--------LRRDL--EEatlQHEATAAT----- 1193
Cdd:COG4913 433 RRKSNIPARLLALRDALAEALGLDEAElpfvgelIEV-RPEEERWRGaiervlggFALTLlvPP---EHYAAALRwvnrl 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1194 -LRKK-QADSVAELGEQIDNLQRVKQ----KLEKEKSELRLELDDVVSNMEHVVK--TKANLEKMTRSL--EDQMneyKT 1263
Cdd:COG4913 509 hLRGRlVYERVRTGLPDPERPRLDPDslagKLDFKPHPFRAWLEAELGRRFDYVCvdSPEELRRHPRAItrAGQV---KG 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1264 KYEEGQRCINDFTMQKSKLQSENGelsRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTD 1343
Cdd:COG4913 586 NGTRHEKDDRRRIRSRYVLGFDNR---AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1344 L--LREQYEEEQEAKAELQRGmskaNSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKH 1421
Cdd:COG4913 663 VasAEREIAELEAELERLDAS----SDDL---------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1422 RLQNEIEDLMVDLER-----SNAAAAALDKK--QRNFDKVLSEWKQKFEESQAELESSQKEARclsTELFKLKNSYeeal 1494
Cdd:COG4913 724 QAEEELDELQDRLEAaedlaRLELRALLEERfaAALGDAVERELRENLEERIDALRARLNRAE---EELERAMRAF---- 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1495 dhletmkrenknlQEEISDLTEQLGEGGKSIHELEKMRKQLEQEkseiqsALEEAEAsleheegKILRAQLEFSqikadi 1574
Cdd:COG4913 797 -------------NREWPAETADLDADLESLPEYLALLDRLEED------GLPEYEE-------RFKELLNENS------ 844
|
730 740 750
....*....|....*....|....*....|
gi 163644331 1575 ERKLAEKDEEMEQSKRNLQRTIDTLQSSLE 1604
Cdd:COG4913 845 IEFVADLLSKLRRAIREIKERIDPLNDSLK 874
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
859-1229 |
4.75e-17 |
|
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: 87.82 E-value: 4.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 859 AKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAKELTERLEDEEEMNAEL 938
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 939 TAKKRKLEDECSELKKDIDDLELTLAKVEK-----EKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQ 1013
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1014 SEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLN 1093
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1094 GKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRaDLARELEEISERLEEAGGATAAQI---EMNKKRE 1170
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE-DVQAELQRVEEEIRALEPVNMLAIqeyEEVLKRL 988
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1171 AEFQKLRRDLEEATLQHEATAATLRKKQADSVAELGEQI-DNLQRVKQKLEKEKSELRLE 1229
Cdd:TIGR02169 989 DELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAInENFNEIFAELSGGTGELILE 1048
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
877-1579 |
8.42e-17 |
|
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: 86.95 E-value: 8.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 877 EKMVSLLQEKNDLQLQVQAEQDnlcDAEERCDQLIKNKIQLEAKAKELTERLEDEEEMNAELTAK------KRKLEDECS 950
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTL---CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKreaqeeQLKKQQLLK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 951 ELKKDIDDLELTLAKVEKEKHATENKVKnlteemaalddiIAKLTKEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLE 1030
Cdd:TIGR00618 264 QLRARIEELRAQEAVLEETQERINRARK------------AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1031 QQVDDlEGSLEQEKKLRMDLERakrklegdlkltQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKL 1110
Cdd:TIGR00618 332 AHVKQ-QSSIEEQRRLLQTLHS------------QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1111 KELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEEATlQHEAT 1190
Cdd:TIGR00618 399 CKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKERE-QQLQT 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1191 AATLRKKQADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDV------VSNMEHVVKTKANLEKMTRSLE-------DQ 1257
Cdd:TIGR00618 478 KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgplTRRMQRGEQTYAQLETSEEDVYhqltserKQ 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1258 MNEYKTKYEEGQR-------CINDFTMQKSKLQSENGEL----SRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETK 1326
Cdd:TIGR00618 558 RASLKEQMQEIQQsfsiltqCDNRSKEDIPNLQNITVRLqdltEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQC 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1327 AKSALAHAVQSARHDTDLLREQYEE--------EQEAKAELQRGMSKANSEVAQWRTKYETDAIQRT--EELEEAKKKLA 1396
Cdd:TIGR00618 638 SQELALKLTALHALQLTLTQERVREhalsirvlPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTllRELETHIEEYD 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1397 QRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDlmvdlERSNAAAAALDKKQRNFDKVLSEWK--QKFEESQAELESSQK 1474
Cdd:TIGR00618 718 REFNEIENASSSLGSDLAAREDALNQSLKELMH-----QARTVLKARTEAHFNNNEEVTAALQtgAELSHLAAEIQFFNR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1475 EARCLSTELFKLKNSYEEALDHLETMKR-ENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEaEASL 1553
Cdd:TIGR00618 793 LREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQE-QAKI 871
|
730 740
....*....|....*....|....*.
gi 163644331 1554 EHEEGKILRAQLEFSQIKADIERKLA 1579
Cdd:TIGR00618 872 IQLSDKLNGINQIKIQFDGDALIKFL 897
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
32-76 |
1.43e-16 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 74.77 E-value: 1.43e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 163644331 32 DMKKECFVPDPDEEYVKASIVSREGDKVTVQTEKRKTVTVKEADI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1313-1826 |
2.12e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 85.48 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1313 QIEDLKRQLEE-ETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAElQRGmsKANSEVAQWRTKYEtdaiqRTEELEEA 1391
Cdd:PRK02224 188 SLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARE-TRD--EADEVLEEHEERRE-----ELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1392 KKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEE------- 1464
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEcrvaaqa 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1465 --SQAE--------LESSQKEARclsTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQ 1534
Cdd:PRK02224 340 hnEEAEslredaddLEERAEELR---EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1535 LEQEKSEIQSALEEAEASLEHEEGKILRAQ--------------LEFSQIKADIERKlAEKDEEMEQSKRNLQRTIDTLQ 1600
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpVEGSPHVETIEED-RERVEELEAELEDLEEEVEEVE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1601 SSLES-----ETRSRNEALRIKKKMEGDL--------NEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRT-- 1665
Cdd:PRK02224 496 ERLERaedlvEAEDRIERLEERREDLEELiaerretiEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEva 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1666 --NEDLKENTAIVERRNNL--LQAELEELRAALEqtERGRKLAEQELLDTSERVQLlhsqntsllnqkKKLETDISQLQT 1741
Cdd:PRK02224 576 elNSKLAELKERIESLERIrtLLAAIADAEDEIE--RLREKREALAELNDERRERL------------AEKRERKRELEA 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1742 EVEEA-VQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiamkggkkQVQKLEA- 1819
Cdd:PRK02224 642 EFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALEN--------RVEALEAl 713
|
....*....
gi 163644331 1820 --RVRELES 1826
Cdd:PRK02224 714 ydEAEELES 722
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
988-1860 |
2.27e-16 |
|
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: 85.87 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 988 DDIIAKLTKE--KKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERakrKLEGDLKLTQ 1065
Cdd:TIGR00606 224 DQITSKEAQLesSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELEL---KMEKVFQGTD 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1066 ESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTiciQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLAREL 1145
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERR---LLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1146 E-EISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQADSVAELGEQIDNlqrVKQKLEKEKS 1224
Cdd:TIGR00606 378 ElDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIEL---KKEILEKKQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1225 ELRL---ELDDVVSNMEHVVKTKANLEKMTRSL----EDQMNEYKTKYEEG-QRCINDFTMQKSKLQSENGELSRQLEEK 1296
Cdd:TIGR00606 455 ELKFvikELQQLEGSSDRILELDQELRKAERELskaeKNSLTETLKKEVKSlQNEKADLDRKLRKLDQEMEQLNHHTTTR 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1297 DSLVSqLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQWRtk 1376
Cdd:TIGR00606 535 TQMEM-LTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN-- 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1377 yetdaiqrteelEEAKKKLAQRLQETEEAVEAVNakCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKK--------- 1447
Cdd:TIGR00606 612 ------------NELESKEEQLSSYEDKLFDVCG--SQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFitqltdenq 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1448 ------QRNFdKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEG 1521
Cdd:TIGR00606 678 sccpvcQRVF-QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1522 GKSIHELEKMRKQLEQEKSEIQSALEEAEAsLEHEEGKILRAQLEFSQIKADIERKLAEKD--------EEMEQSKRNLQ 1593
Cdd:TIGR00606 757 NRDIQRLKNDIEEQETLLGTIMPEEESAKV-CLTDVTIMERFQMELKDVERKIAQQAAKLQgsdldrtvQQVNQEKQEKQ 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1594 RTIDTLQSSLESETRSRNEALRIKKKMEGDLNEM---EIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDslRTNEDLK 1670
Cdd:TIGR00606 836 HELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELkseKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKD--AKEQDSP 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1671 ENTAiverrnnlLQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLN--------QKKKLETDISQLQTE 1742
Cdd:TIGR00606 914 LETF--------LEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENkiqdgkddYLKQKETELNTVNAQ 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1743 VEEAVQECRNAEE--KAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAMkggKKQVQKLEAR 1820
Cdd:TIGR00606 986 LEECEKHQEKINEdmRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQM---KQEHQKLEEN 1062
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 163644331 1821 VRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDR 1860
Cdd:TIGR00606 1063 IDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1383-1933 |
3.08e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 85.12 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1383 QRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKhrlqNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKF 1462
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1463 EEsqaeLESSQKEarclSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMR---KQLEQEK 1539
Cdd:PRK03918 276 EE----LEEKVKE----LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1540 SEIQSALEEAEASLE-HEEGKILRAQLEfsQIKADIE----RKLAEKDEEMEQSKRNLQRTIDTLQ---SSLESETRSRN 1611
Cdd:PRK03918 348 KELEKRLEELEERHElYEEAKAKKEELE--RLKKRLTgltpEKLEKELEELEKAKEEIEEEISKITariGELKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1612 EALRIKKKMEGDLNEMEIQLSQANRQaaeaqKQLKSVHAHMKDAQlqlddslrtnEDLKENTAIVERrnnlLQAELEELR 1691
Cdd:PRK03918 426 KAIEELKKAKGKCPVCGRELTEEHRK-----ELLEEYTAELKRIE----------KELKEIEEKERK----LRKELRELE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1692 AALEQTERGRKLAEqelldtservqllhsqntsLLNQKKKLETDISQLQTE-VEEAVQECRNAEEKAKKAITDAAMMAEE 1770
Cdd:PRK03918 487 KVLKKESELIKLKE-------------------LAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1771 LKKEQDtsahLERMKKNMEQTIKDLQHRLDEAEQIAMKGGKKQVQKLEARVRELEsEVESEQKKSSEAVKGIRKYERRIK 1850
Cdd:PRK03918 548 LEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKELEREEKELK 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1851 ELTYQTEEDRKNLARLQDLVDKLQLKVKAYKRAAEEAEEQANTNL-----SKFRKIQHELDEAEERADIAESQVNKLRAK 1925
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEylelsRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
....*...
gi 163644331 1926 SRDVSSKK 1933
Cdd:PRK03918 703 LEEREKAK 710
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
847-1387 |
3.21e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 85.12 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 847 AEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAKELTE 926
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 927 ---RLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKnLTEEMAALDDIIAKLTKEKKALQE 1003
Cdd:PRK03918 243 lekELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1004 ---AHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGS---LEQEKKLRMDLERAKRKLEG-DLKLTQESLMDLENDKQ 1076
Cdd:PRK03918 322 einGIEERIKELEEKEERLEELKKKLKELEKRLEELEERhelYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1077 QLEERLKKKDFEISQLNGKIEDEQTICIQLQK--------------------------KLKELQARIEELEEELEAERAA 1130
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelleeytaELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1131 RAKVEKQRA---------DLARELEEISERLEEAGgataaqIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQA-- 1199
Cdd:PRK03918 482 LRELEKVLKkeseliklkELAEQLKELEEKLKKYN------LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElk 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1200 DSVAELGEQIDNLQRVKQKLEKEKSELRL----ELDDVVSNME-------HVVKTKANLEKMTRSLEDQMNEYKTKYEEG 1268
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEELGFesveELEERLKELEpfyneylELKDAEKELEREEKELKKLEEELDKAFEEL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1269 QRCINDFTMQKSKLQS---------------ENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALaH 1333
Cdd:PRK03918 636 AETEKRLEELRKELEElekkyseeeyeelreEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL-E 714
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 163644331 1334 AVQSARHDTDLLREQY-----EEEQEAKAELQRGMSKANSEVAQwrTKYETDAIQRTEE 1387
Cdd:PRK03918 715 KLEKALERVEELREKVkkykaLLKERALSKVGEIASEIFEELTE--GKYSGVRVKAEEN 771
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
927-1536 |
5.68e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 84.35 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 927 RLEDEEEMNAELTAKKRKLEDECSELKKDI---DDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQE 1003
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIkrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1004 ahqqtlddlqseedkvntltkakakleqqvddLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLK 1083
Cdd:PRK03918 236 --------------------------------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1084 kkdfEISQLNGKiEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAggataaqi 1163
Cdd:PRK03918 284 ----ELKELKEK-AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL-------- 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1164 emnKKREAEFQKLRRDLEEAtLQHEATAATLRKKQAD-SVAELGEQIDNLQRVKQKLEKE-------KSELRLELDDVVS 1235
Cdd:PRK03918 351 ---EKRLEELEERHELYEEA-KAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEiskitarIGELKKEIKELKK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1236 NMEHVVKTKANLEKMTRSLEDQ-----MNEYKTKYEEGQRCINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKmsy 1310
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE--- 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1311 tqQIEDLKRQLE----EETKAKSALAHAVQSA----RHDTDLLREQYEEEQE---AKAELQRGMSKANSEVAQWRTKYET 1379
Cdd:PRK03918 504 --QLKELEEKLKkynlEELEKKAEEYEKLKEKliklKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEE 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1380 DAIQRTEELEEakkklaqRLQETEEAVEAVNaKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWK 1459
Cdd:PRK03918 582 LGFESVEELEE-------RLKELEPFYNEYL-ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163644331 1460 QKFeeSQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEIsdltEQLGEGGKSIHELEKMRKQLE 1536
Cdd:PRK03918 654 KKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL----EEREKAKKELEKLEKALERVE 724
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
989-1928 |
1.10e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 83.56 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 989 DIIAKLTKEKKALQEAHQ------QTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLK 1062
Cdd:TIGR00606 176 DEIFSATRYIKALETLRQvrqtqgQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1063 LTQE---SLMDLENDKQQLEERLKKKDFEISQLNGKIEDE-QTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQR 1138
Cdd:TIGR00606 256 EIEHnlsKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKER 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1139 ADLARELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEEATLQHEA-------TAATLRKKQADSVAELGEQIDN 1211
Cdd:TIGR00606 336 RLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPfserqikNFHTLVIERQEDEAKTAAQLCA 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1212 LQRVKQKLEKEkselrlELDDVVSNMEHVVKTkanLEKMTRSLEDQMNEYKTKYEEGQRC---INDFTMQKSKLQSENGE 1288
Cdd:TIGR00606 416 DLQSKERLKQE------QADEIRDEKKGLGRT---IELKKEILEKKQEELKFVIKELQQLegsSDRILELDQELRKAERE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1289 LSrqLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANS 1368
Cdd:TIGR00606 487 LS--KAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTS 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1369 EVAQWRTKyetdaiqrtEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQ 1448
Cdd:TIGR00606 565 LLGYFPNK---------KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQ 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1449 rNFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHEL 1528
Cdd:TIGR00606 636 -DEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1529 EKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIKADIERklaEKDEEMEQSKRnlqrtIDTLQSSLESETR 1608
Cdd:TIGR00606 715 ESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQR---LKNDIEEQETL-----LGTIMPEEESAKV 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1609 SRNEALRIKK-KMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAEL 1687
Cdd:TIGR00606 787 CLTDVTIMERfQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1688 EEL---RAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQecrNAEEKAKKAITDA 1764
Cdd:TIGR00606 867 NELkseKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS---SKETSNKKAQDKV 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1765 AMMAEELKK--------EQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiamkggkkQVQKLEARVRELESEVESEQKKSS 1836
Cdd:TIGR00606 944 NDIKEKVKNihgymkdiENKIQDGKDDYLKQKETELNTVNAQLEECEK--------HQEKINEDMRLMRQDIDTQKIQER 1015
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1837 --EAVKGIRKYERRIKELtyqtEEDRKNLARLQDLVDKLQLKVKAYKRAAEEAEEQANTNLSKFRKIQHELDEAEERADI 1914
Cdd:TIGR00606 1016 wlQDNLTLRKRENELKEV----EEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
970
....*....|....
gi 163644331 1915 AESQVNKLRAKSRD 1928
Cdd:TIGR00606 1092 REPQFRDAEEKYRE 1105
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1068-1628 |
1.51e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.80 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1068 LMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLaRELEE 1147
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV-KELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1148 ISERLEEAggataaqiemnKKREAEFQKLRRDLEEATLQHEATAATLRKKqadsVAELGEQIDNLQRVKQKlEKEKSELR 1227
Cdd:PRK03918 236 LKEEIEEL-----------EKELESLEGSKRKLEEKIRELEERIEELKKE----IEELEEKVKELKELKEK-AEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1228 LELDDVVSNMEHVVKTKANLEKMTRSLEDQMNEYKTKYEEgqrcINDFTMQKSKLQSENGELsrqleEKDSLVSQLTRSK 1307
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER----LEELKKKLKELEKRLEEL-----EERHELYEEAKAK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1308 MSytqQIEDLKRQLEEETKAKsalahavqsarhdtdlLREQYEEEQEAKAELQRGMSKANSEVAQWRTKyETDAIQRTEE 1387
Cdd:PRK03918 371 KE---ELERLKKRLTGLTPEK----------------LEKELEELEKAKEEIEEEISKITARIGELKKE-IKELKKAIEE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1388 LEEAKKK--LAQRL---QETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDK--KQRNFDKVLSEWKQ 1460
Cdd:PRK03918 431 LKKAKGKcpVCGRElteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1461 KFEESQAE-LESSQKEARCLSTELFKLK----------NSYEEALDHLETMKRENKNLQEEISDLTEQLGEGG-KSIHEL 1528
Cdd:PRK03918 511 KLKKYNLEeLEKKAEEYEKLKEKLIKLKgeikslkkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEEL 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1529 EKMRKQLEQ------EKSEIQSALEEAEASLEHEEGKILRAQLEFSQIKADIERKLA-----------EKDEEMEQSKRN 1591
Cdd:PRK03918 591 EERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKeleelekkyseEEYEELREEYLE 670
|
570 580 590
....*....|....*....|....*....|....*..
gi 163644331 1592 LQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEME 1628
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
884-1772 |
1.86e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 82.79 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 884 QEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAK----------ELTERLEDEEEMNA---ELTAKKRKLEDECS 950
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREivksyeneldPLKNRLKEIEHNLSkimKLDNEIKALKSRKK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 951 ELKKDIDDLELTLAKV-----EKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQ--------QTLDDLQSEED 1017
Cdd:TIGR00606 280 QMEKDNSELELKMEKVfqgtdEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQektellveQGRLQLQADRH 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1018 KVNTLTKAKAKLEQQ----VDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLN 1093
Cdd:TIGR00606 360 QEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLG 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1094 GKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADL--ARELEEISERLEEAGGATAAQIEMNKKREA 1171
Cdd:TIGR00606 440 RTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELskAEKNSLTETLKKEVKSLQNEKADLDRKLRK 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1172 EFQKLRRDLEEATLQHEATAATLRKKQADS---------VAELGEQIDNLQRVKQ------KLEKEKSELRLELDDVVSN 1236
Cdd:TIGR00606 520 LDQEMEQLNHHTTTRTQMEMLTKDKMDKDEqirkiksrhSDELTSLLGYFPNKKQledwlhSKSKEINQTRDRLAKLNKE 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1237 MEHVVKTKANLEKMTRSLEDQMNEYKTKYEEGQRCindftmqkSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIED 1316
Cdd:TIGR00606 600 LASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS--------QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQ 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1317 LKRQ-------LEEETKAKSALAHAVQSARHDTDLLREQYEE------EQEAKAELQRGMSKANSEVAQWRTKYETDAIQ 1383
Cdd:TIGR00606 672 LTDEnqsccpvCQRVFQTEAELQEFISDLQSKLRLAPDKLKSteselkKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRN 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1384 RTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTK------HRLQNEIEDLMVDLERSNAAAAALDkkqrnFDKVLSE 1457
Cdd:TIGR00606 752 KLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLtdvtimERFQMELKDVERKIAQQAAKLQGSD-----LDRTVQQ 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1458 WKQKFEESQAELESSQKEARclstELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEggksihelekMRKQLEQ 1537
Cdd:TIGR00606 827 VNQEKQEKQHELDTVVSKIE----LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ----------FEEQLVE 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1538 EKSEIQSALEEAEASLEHEegkilraqLEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALR-I 1616
Cdd:TIGR00606 893 LSTEVQSLIREIKDAKEQD--------SPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENkI 964
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1617 KKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAElEELRAALEQ 1696
Cdd:TIGR00606 965 QDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVE-EELKQHLKE 1043
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163644331 1697 TERGRKLA-EQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEavQECRNAEEKAKKAITDAAMMAEELK 1772
Cdd:TIGR00606 1044 MGQMQVLQmKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE--PQFRDAEEKYREMMIVMRTTELVNK 1118
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1445-1926 |
2.47e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.01 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1445 DKKQRNFDKVLSEWKQKFEESQAELE--SSQKE-ARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEG 1521
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIEryEEQREqARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1522 GKSIHELEKMRKQLEQEKSEIQsaleeAEASLEHEEGKILRAQLEfsqikaDIERKLAEKDEEMEQSKRNLQRTIDTLQS 1601
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLL-----AEAGLDDADAEAVEARRE------ELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1602 SLES--ETRSRNEALRIK-KKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVER 1678
Cdd:PRK02224 347 LREDadDLEERAEELREEaAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1679 RNNLLQAELEELRAALEQTER----------GRKLAEQELLDTSERVQllhsqntsllNQKKKLETDISQLQTEVEEAvq 1748
Cdd:PRK02224 427 REAELEATLRTARERVEEAEAlleagkcpecGQPVEGSPHVETIEEDR----------ERVEELEAELEDLEEEVEEV-- 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1749 ecrnaEEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiamkggkkQVQKLEARVRELESEV 1828
Cdd:PRK02224 495 -----EERLERA--------EDLVEAEDRIERLEERREDLEELIAERRETIEEKRE--------RAEELRERAAELEAEA 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1829 ESEQKKSSEAVKGIRKYERRIKELTYQTEE---DRKNLARLQDLVDKLQLKVKAYKRAAEEAEEQANTN------LSKFR 1899
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAElkeRIESLERIRTLLAAIADAEDEIERLREKREALAELNderrerLAEKR 633
|
490 500
....*....|....*....|....*..
gi 163644331 1900 KIQHELDEAEERADIAESQVNKLRAKS 1926
Cdd:PRK02224 634 ERKRELEAEFDEARIEEAREDKERAEE 660
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
845-1457 |
2.97e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.04 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 845 AEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAKEL 924
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 925 TERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVK-NLTEEMAALDDI------IAKLTKE 997
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRgGRAVEEVLKASIqgvhgtVAQLGSV 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 998 K----KALQEAHQQTLDDLQSEEDKVNT------------------LTKAKAK--------LEQQVDDLEGSLEQEKKLR 1047
Cdd:TIGR02169 534 GeryaTAIEVAAGNRLNNVVVEDDAVAKeaiellkrrkagratflpLNKMRDErrdlsilsEDGVIGFAVDLVEFDPKYE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1048 -------------MDLERAKR--------KLEGDL--------------KLTQESLMDLENDKQQLEERLKKKDFEISQL 1092
Cdd:TIGR02169 614 pafkyvfgdtlvvEDIEAARRlmgkyrmvTLEGELfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSL 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1093 NGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAggataaqiemnkkrEAE 1172
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV--------------KSE 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1173 FQKLRRDLEEatlqHEATAATLRKKQADSVAELG-EQIDNLQRVKQKLEKEKSELRLELDDVVSNMEHVVKTKANLEKMT 1251
Cdd:TIGR02169 760 LKELEARIEE----LEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1252 RSLEDQMNEYKTKYEEGQRCINDftmqkskLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSAL 1331
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIEN-------LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1332 AHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQETEEAVEAVNA 1411
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE--ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLK 986
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 163644331 1412 KCSSLEKTKHRLQNEIEDL-----MVDLERSNAAAAALDKKQRNFDKVLSE 1457
Cdd:TIGR02169 987 RLDELKEKRAKLEEERKAIlerieEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1416-1928 |
4.52e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 81.32 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1416 LEKTKHRLQNEIEDLMVDLERSNAaaaaLDKKQRNF-DKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEAL 1494
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNE----LHEKQKFYlRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1495 DHLETMKrenkNLQEEIsdlteqLGEGGKSIHELEKMRKQLEQEKSEIQSAL---EEAEASLEHEEGKIlrAQLEFSQIK 1571
Cdd:pfam15921 152 HELEAAK----CLKEDM------LEDSNTQIEQLRKMMLSHEGVLQEIRSILvdfEEASGKKIYEHDSM--STMHFRSLG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1572 ADIERKLAEKDEEMEQSKRNLQRTIDTLQSsLESETRSRNEAL--RIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVH 1649
Cdd:pfam15921 220 SAISKILRELDTEISYLKGRIFPVEDQLEA-LKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1650 AHMKDAQlqlddslrtnEDLKENTAIVERRNNLLQAELEELRAALEQTERgrkLAEQELLDTSERVQLLHSQntsllnqk 1729
Cdd:pfam15921 299 SQLEIIQ----------EQARNQNSMYMRQLSDLESTVSQLRSELREAKR---MYEDKIEELEKQLVLANSE-------- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1730 kkletdISQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiamkg 1809
Cdd:pfam15921 358 ------LTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM----- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1810 gkkQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLAR------------------LQDLVD 1871
Cdd:pfam15921 427 ---EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKvveeltakkmtlessertVSDLTA 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 163644331 1872 KLQLKVKAYKRAAEEAEEQANTNLSKFRKIQHELDEAEERADI-AESQVNKLRAKSRD 1928
Cdd:pfam15921 504 SLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVqTECEALKLQMAEKD 561
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1072-1802 |
5.71e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 80.83 E-value: 5.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1072 ENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISER 1151
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1152 LEeaggataAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQADsVAELGEQIDNLQRVKQKLEKEKSELRLELD 1231
Cdd:TIGR04523 112 IK-------NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1232 DVVSNMEHVVKTKANLEKMTRSLEDQMNEYKTkyeegqrcindFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYT 1311
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKS-----------LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1312 QQIEDLKrqlEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELqrgmSKANSEVAQ-WRTKYETDAIQRTEELEE 1390
Cdd:TIGR04523 253 TQLNQLK---DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI----SDLNNQKEQdWNKELKSELKNQEKKLEE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1391 AKKKLAQrlqeTEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELE 1470
Cdd:TIGR04523 326 IQNQISQ----NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1471 SSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAE 1550
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1551 ASLEHEEGKILRAQLEFSQIKADIeRKLAEKDEEMEQSKRNLQRTIDTLQS---SLESETRSRNEALrIKKKMEGDLNEM 1627
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEK-KELEEKVKDLTKKISSLKEKIEKLESekkEKESKISDLEDEL-NKDDFELKKENL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1628 EIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQE 1707
Cdd:TIGR04523 560 EKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1708 LLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKA----KKAIT------DAAMMAEELKKEQDT 1777
Cdd:TIGR04523 640 KNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELslhyKKYITrmirikDLPKLEEKYKEIEKE 719
|
730 740
....*....|....*....|....*
gi 163644331 1778 SAHLERMKKNMEQTIKDLQHRLDEA 1802
Cdd:TIGR04523 720 LKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
843-1154 |
7.84e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.88 E-value: 7.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 843 KSAEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAK 922
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 923 ELTERLEDEEEMNA-----ELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKE 997
Cdd:TIGR02169 776 KLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 998 KKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQ 1077
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163644331 1078 LeERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEE 1154
Cdd:TIGR02169 936 I-EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
872-1430 |
9.60e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.08 E-value: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 872 RKELEEKmvsllqEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAKELTERLEDEEEMNAELTakkrkledecsE 951
Cdd:PRK02224 193 KAQIEEK------EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE-----------T 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 952 LKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEkKALQEAHQQTLDDLQSEedkvntltkakakLEQ 1031
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE-AGLDDADAEAVEARREE-------------LED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1032 QVDDLEGSLEQEkklRMDLERAKRKLEGdlkltqeslmdLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLK 1111
Cdd:PRK02224 322 RDEELRDRLEEC---RVAAQAHNEEAES-----------LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1112 ELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEaggataaqiemnkkREAEFQKLRRDLEEA-TLQHEAT 1190
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE--------------LEATLRTARERVEEAeALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1191 AATLRKKQADSvaELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNMEHVVKTKAnLEKMTRSLEDQMNEYKTKYEEGQR 1270
Cdd:PRK02224 454 CPECGQPVEGS--PHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE-AEDRIERLEERREDLEELIAERRE 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1271 CINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAH------AVQSARHDTDL 1344
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaAIADAEDEIER 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1345 LREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQ 1424
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERKRELEAEFDEARI---EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVE 687
|
....*.
gi 163644331 1425 NEIEDL 1430
Cdd:PRK02224 688 NELEEL 693
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1254-1907 |
2.22e-14 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 79.39 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1254 LEDQMNEYKTKYEEGQRCIND----FTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLE----EET 1325
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNEsnelHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQntvhELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1326 KAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMskANSEVAQWRTKYETDAIQrTEELEEAKKKLAQRLQETEEA 1405
Cdd:pfam15921 156 AAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL--VDFEEASGKKIYEHDSMS-TMHFRSLGSAISKILRELDTE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1406 VEAVNAKC----SSLEKTKHRLQNEIEDLMVD-LERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLS 1480
Cdd:pfam15921 233 ISYLKGRIfpveDQLEALKSESQNKIELLLQQhQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1481 TELFKLKNSYEEALDHLETMKRENKNLQEE-ISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALE---------EAE 1550
Cdd:pfam15921 313 SMYMRQLSDLESTVSQLRSELREAKRMYEDkIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQklladlhkrEKE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1551 ASLEHEEGKILRAQLEFSQIKAD-IERKLAEKDEEMEQskrnLQRTIDTLQSSLESETRSRNEALRIKkkmegdlNEMEI 1629
Cdd:pfam15921 393 LSLEKEQNKRLWDRDTGNSITIDhLRRELDDRNMEVQR----LEALLKAMKSECQGQMERQMAAIQGK-------NESLE 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1630 QLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEQtergrKLAE-QEL 1708
Cdd:pfam15921 462 KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDL-----KLQElQHL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1709 LDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECrnaeekAKKAITDAAMMAEelkkeqdtsahlermKKNM 1788
Cdd:pfam15921 537 KNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLV------GQHGRTAGAMQVE---------------KAQL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1789 EQTIKDLQHRLDEAEQIAMKGGKKqVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQD 1868
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAK-IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
650 660 670
....*....|....*....|....*....|....*....
gi 163644331 1869 LVDKLQlkvKAYKRAAEEAEEQANTNLSKFRKIQHELDE 1907
Cdd:pfam15921 675 DYEVLK---RNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1610-1925 |
2.34e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.21 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1610 RNEALRIKKKMEGDLN-------EMEIQLSQANRQAAEAQKqLKSVHAHMKDAQLQLddSLRTNEDLKENTAIVERRNNL 1682
Cdd:COG1196 174 KEEAERKLEATEENLErledilgELERQLEPLERQAEKAER-YRELKEELKELEAEL--LLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1683 LQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAIT 1762
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1763 DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiAMKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGI 1842
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1843 RKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKAYKRAAEEAEEQANTNLSKFRKIQHELDEAEERADIAESQVNKL 1922
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
...
gi 163644331 1923 RAK 1925
Cdd:COG1196 490 AAR 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
843-1097 |
8.83e-14 |
|
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: 77.40 E-value: 8.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 843 KSAEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAK 922
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 923 ELTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQ 1002
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1003 EAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEK----KLRMDLERAKRKLEGDLKLTQESLMDLENDKQQL 1078
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElrleGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDD 966
|
250
....*....|....*....
gi 163644331 1079 EERLKKkdfEISQLNGKIE 1097
Cdd:TIGR02168 967 EEEARR---RLKRLENKIK 982
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
848-1589 |
1.34e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 76.62 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 848 EKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQdnlCDAEERCDQLIKNKIQLEAKAKE---- 923
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQ---EHIRARDSLIQSLATRLELDGFErgpf 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 924 -----------LTERLEDEEEMNAELTA--------KKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEM 984
Cdd:TIGR00606 388 serqiknfhtlVIERQEDEAKTAAQLCAdlqskerlKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 985 AALDDIIAK----------------------LTKEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQ 1042
Cdd:TIGR00606 468 GSSDRILELdqelrkaerelskaeknsltetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDK 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1043 EKKLRMDLERAKRKLEGDL------KLTQESLMDLENDKQQLEERLKKKDFEIS-------QLNGKIEDEQTICIQLQKK 1109
Cdd:TIGR00606 548 DEQIRKIKSRHSDELTSLLgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELAsleqnknHINNELESKEEQLSSYEDK 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1110 LKELqARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATAAQIEMNK---KREAEFQKLRRDLEEATL- 1185
Cdd:TIGR00606 628 LFDV-CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQrvfQTEAELQEFISDLQSKLRl 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1186 ---QHEATAATLRKKQADSVAELGeQIDNLQRVKQKLEKEKSELRLELDDVVSNMEhvvKTKANLEKMTRSLEDQMNEYK 1262
Cdd:TIGR00606 707 apdKLKSTESELKKKEKRRDEMLG-LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ---RLKNDIEEQETLLGTIMPEEE 782
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1263 TkyeeGQRCINDFTMQKsKLQSENGELSRQLEEkdsLVSQLtrskmsytqQIEDLKRQLEEETKAKSALAHAVQSARHDT 1342
Cdd:TIGR00606 783 S----AKVCLTDVTIME-RFQMELKDVERKIAQ---QAAKL---------QGSDLDRTVQQVNQEKQEKQHELDTVVSKI 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1343 DLLREQYEEEQEAKAELQRGMSKANSEVAQWRTkyetdAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHR 1422
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGT-----NLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEK 920
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1423 LQNEIEDLMVDLERSNAAAA-ALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARclsTELFKLKNSYEEALDHLETMK 1501
Cdd:TIGR00606 921 DQQEKEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKE---TELNTVNAQLEECEKHQEKIN 997
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1502 RENKNLQEEISDLTEQ---------LGEGGKSIHELEKMRKQLEQEKSEIQ--------SALEEAEASLEHEEGKILRAQ 1564
Cdd:TIGR00606 998 EDMRLMRQDIDTQKIQerwlqdnltLRKRENELKEVEEELKQHLKEMGQMQvlqmkqehQKLEENIDLIKRNHVLALGRQ 1077
|
810 820
....*....|....*....|....*
gi 163644331 1565 LEFSQIKADIERKLAEKDEEMEQSK 1589
Cdd:TIGR00606 1078 KGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
918-1823 |
1.63e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 76.55 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 918 EAKAKELTERLEDEEEMNAEL-TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHatenkvknlteemaaLDDIIAKLTK 996
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL---------------NEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 997 EKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQ 1076
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1077 QLEERLKKkdfeisqlngkiedEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAg 1156
Cdd:pfam02463 325 KAEKELKK--------------EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1157 gatAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDvvsn 1236
Cdd:pfam02463 390 ---AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK---- 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1237 MEHVVKTKANLEKMTRSLEDQMneYKTKYEEGQRCINDFTMQKSKLQSENGELSRQLEEKDSLVsqltrskmsyTQQIED 1316
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQE--QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI----------ISAHGR 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1317 LKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELeeakKKLA 1396
Cdd:pfam02463 531 LGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPI----LNLA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1397 QRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNfdkvLSEWKQKFEESQAELESSQKEA 1476
Cdd:pfam02463 607 QLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAE----KSEVKASLSELTKELLEIQELQ 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1477 RCLSTELFKLKNSYeealdHLETMKRENKNLQEEISDLTEQLgeggksIHELEKMRKQLEQEKSEIQSALEEAEASLEHE 1556
Cdd:pfam02463 683 EKAESELAKEEILR-----RQLEIKKKEQREKEELKKLKLEA------EELLADRVQEAQDKINEELKLLKQKIDEEEEE 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1557 EGKILRAQLEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRiKKKMEGDLNEMEIQLSQANR 1636
Cdd:pfam02463 752 EEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL-KEEAELLEEEQLLIEQEEKI 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1637 QAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQELLDTSERVQ 1716
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLN 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1717 LLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAItdaamMAEELKKEQDTSAHLERMKKN----MEQTI 1792
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK-----EEEEERNKRLLLAKEELGKVNlmaiEEFEE 985
|
890 900 910
....*....|....*....|....*....|.
gi 163644331 1793 KDLQHRLDEAEQIAMKGGKKQVQKLEARVRE 1823
Cdd:pfam02463 986 KEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
842-1407 |
2.17e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 75.93 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 842 LKSAEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDnlcdaeercdqliKNKIQLEAKA 921
Cdd:pfam15921 250 LKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE-------------QARNQNSMYM 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 922 KELTERLEDEEEMNAELTAKKRKLEDECSELKKD--IDDLELTLAKVEKEKHATENkvKNLTEEmaaLDDIIAKLTKEKK 999
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQ---LQKLLADLHKREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1000 ALQEAHQQT--------------------LDDLQSEEDKVNTLTKA-----KAKLEQQVDDLEG---SLEQEKKLRMDLE 1051
Cdd:pfam15921 392 ELSLEKEQNkrlwdrdtgnsitidhlrreLDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGkneSLEKVSSLTAQLE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1052 RAK---RKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTiciQLQKKLKELQaRIEELEEELEAER 1128
Cdd:pfam15921 472 STKemlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRS---RVDLKLQELQ-HLKNEGDHLRNVQ 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1129 AARAKVEKQRADLARELEEISERLEEAG------GATAAQIEMNKKR-EAEFQKLRRDLEEATLqheataatLRKKQADS 1201
Cdd:pfam15921 548 TECEALKLQMAEKDKVIEILRQQIENMTqlvgqhGRTAGAMQVEKAQlEKEINDRRLELQEFKI--------LKDKKDAK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1202 VAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNMEHV---VKTKAN-LEKMTRSLEDQMNEYKTKYEEGQRCINDFTM 1277
Cdd:pfam15921 620 IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLlneVKTSRNeLNSLSEDYEVLKRNFRNKSEEMETTTNKLKM 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1278 QKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKA 1357
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELS 779
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 163644331 1358 ELQRGMSKANSEVAQWRTKyETDAIQRTEELEEAKKKLAQRLQETEEAVE 1407
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQ-ERRLKEKVANMEVALDKASLQFAECQDIIQ 828
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1482-1938 |
2.91e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 75.60 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1482 ELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKIL 1561
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1562 RAQLEFSQIKADIErKLAEKDEEMEQSKRNLQR---TIDTLQSSLESET----RSRNEALRIKKKMEGDLNEMEIQLSQA 1634
Cdd:pfam01576 93 QLQNEKKKMQQHIQ-DLEEQLDEEEAARQKLQLekvTTEAKIKKLEEDIllleDQNSKLSKERKLLEERISEFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1635 NRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQELLDTSER 1714
Cdd:pfam01576 172 EEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1715 VQLLHSQNTSLLNQKKKLETDISQLQTEVEEAvqecRNAEEKAKKAITDAAMMAEELKKE----QDTSAHLERMKKNMEQ 1790
Cdd:pfam01576 252 LEEETAQKNNALKKIRELEAQISELQEDLESE----RAARNKAEKQRRDLGEELEALKTEledtLDTTAAQQELRSKREQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1791 TIKDLQHRLDEAEQIAMKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQ----------TEEDR 1860
Cdd:pfam01576 328 EVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAElrtlqqakqdSEHKR 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163644331 1861 KnlaRLQDLVDKLQLKVKAYKRAAEEAEEqantnlsKFRKIQHELDEAEERADIAESQVNKLrakSRDVSSKKGHDQE 1938
Cdd:pfam01576 408 K---KLEGQLQELQARLSESERQRAELAE-------KLSKLQSELESVSSLLNEAEGKNIKL---SKDVSSLESQLQD 472
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
849-1394 |
4.84e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 74.67 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 849 KEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEkndlqlqVQAEQDNLCDAEERCDQLIKNKIQLEAKAKELTERL 928
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE-------IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 929 EDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKekhaTENKVKNLTEEMAALDDIIAKLTKEkkaLQEAHQQT 1008
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQQEINEKTTE---ISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1009 LDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDL-KLTQESLMDLENDKQQLEERLKKKDF 1087
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKLEEIQNQISQNNK 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1088 EISQLNGKIE-------DEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEiserleeaggata 1160
Cdd:TIGR04523 336 IISQLNEQISqlkkeltNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN------------- 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1161 aQIEMNKKREAEFQKLRRDLEEATLQHEATAATlRKKQADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNMEhv 1240
Cdd:TIGR04523 403 -QEKLNQQKDEQIKKLQQEKELLEKEIERLKET-IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN-- 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1241 vKTKANLEKMTRSLEDQMNEyktkyeegqrcINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQ 1320
Cdd:TIGR04523 479 -KIKQNLEQKQKELKSKEKE-----------LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644331 1321 LEE--ETKAKSALAHAVQSARHDTDLLREQYEE---EQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEEAKKK 1394
Cdd:TIGR04523 547 LNKddFELKKENLEKEIDEKNKEIEELKQTQKSlkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1095-1929 |
8.70e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 73.85 E-value: 8.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1095 KIEDEQTICIQLQKKLKELQARI-----EELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATAAQIEM--NK 1167
Cdd:pfam02463 157 EIEEEAAGSRLKRKKKEALKKLIeetenLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLklNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1168 KREAEFQKLRRDLEEATLQHEATAATLRKKQADSVAELGE---QIDNLQRVKQKLEKEKSELRLELDDVVSNMEHVVKTK 1244
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEeekEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1245 ANLEKMTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEE 1324
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1325 tkaksaLAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQETEE 1404
Cdd:pfam02463 397 ------LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1405 AVEAVNAKCsSLEKTKHRLQNEIEDLMVDLERSNAA---AAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLST 1481
Cdd:pfam02463 471 EDLLKETQL-VKLQEQLELLLSRQKLEERSQKESKArsgLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1482 -ELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEkmrkqLEQEKSEIQSALEEAEASLEHEEGKI 1560
Cdd:pfam02463 550 iVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE-----IDPILNLAQLDKATLEADEDDKRAKV 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1561 LRAQLEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAE 1640
Cdd:pfam02463 625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1641 AQKQLKSVHAHMKDAQLQLDDSLRTNEDlKENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHS 1720
Cdd:pfam02463 705 EQREKEELKKLKLEAEELLADRVQEAQD-KINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKT 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1721 QntsLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLD 1800
Cdd:pfam02463 784 E---KLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1801 EAEQIAMKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKAY 1880
Cdd:pfam02463 861 EEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL 940
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 163644331 1881 KRAAEEAEEQANTNLSKFRkiqHELDEAEERADIAESQVNKLRAKSRDV 1929
Cdd:pfam02463 941 LLEEADEKEKEENNKEEEE---ERNKRLLLAKEELGKVNLMAIEEFEEK 986
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1028-1671 |
9.65e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.80 E-value: 9.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1028 KLEQQVDDLEGSLEQEKKLRMDLERAKRKLE--GDLKLTQESLMDLENDKQQLEERLKKKDFEISQLngKIEDEQTICIQ 1105
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1106 LQKKLKELQARIEEleeeleaeraarakVEKQRADLARELEEISERLEEAGGATAAQIEMN--------KKREAEFQKLR 1177
Cdd:COG4913 300 LRAELARLEAELER--------------LEARLDALREELDELEAQIRGNGGDRLEQLEREierlerelEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1178 RDLEEATLQHEATAATLRKKQADSVA----------ELGEQIDNLQRVKQKLEKEKSELRLELDDV---VSNM-EHVVKT 1243
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAAllealeeeleALEEALAEAEAALRDLRRELRELEAEIASLerrKSNIpARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1244 KANLEKMTRSLEDQMN------EYKTKYEEGQRCIND------FTMqksklqsengeL--SRQLEEKDSLVSQL-TRSKM 1308
Cdd:COG4913 446 RDALAEALGLDEAELPfvgeliEVRPEEERWRGAIERvlggfaLTL-----------LvpPEHYAAALRWVNRLhLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1309 SYtQQIEDLKRQLEEETKAKSALAHAVQSARHD-TDLLREQYEEEQ-----EAKAELQR--------GMSKANSEVAQ-- 1372
Cdd:COG4913 515 VY-ERVRTGLPDPERPRLDPDSLAGKLDFKPHPfRAWLEAELGRRFdyvcvDSPEELRRhpraitraGQVKGNGTRHEkd 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1373 ----WRTKYET--DAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQN--EIEDLMVDLERSNAAAAAL 1444
Cdd:COG4913 594 drrrIRSRYVLgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAEL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1445 DKKQRNFDK---VLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDhletmkrenknLQEEISDLTEQLGEG 1521
Cdd:COG4913 674 EAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE-----------ELDELQDRLEAAEDL 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1522 GKSIH--ELEKMRKQLEQEKSEiQSALEEAEASLEHEEGKILRAQlefsqikADIERKLAEKDEEMEQSKRNLQRTIDTL 1599
Cdd:COG4913 743 ARLELraLLEERFAAALGDAVE-RELRENLEERIDALRARLNRAE-------EELERAMRAFNREWPAETADLDADLESL 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1600 QSSLESETRSRNEAL-RIKKKMEGDLNEMEIQ-----LSQANRQAAEAQKQLKSVHAHMKDAQ------LQLDDSLRTNE 1667
Cdd:COG4913 815 PEYLALLDRLEEDGLpEYEERFKELLNENSIEfvadlLSKLRRAIREIKERIDPLNDSLKRIPfgpgryLRLEARPRPDP 894
|
....
gi 163644331 1668 DLKE 1671
Cdd:COG4913 895 EVRE 898
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
832-1583 |
1.06e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 73.85 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 832 MKLFFKIKPLLKSAEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLqvqaeqdnlcdaEERCDQLI 911
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLL------------AKEEEELK 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 912 KNKIQLEAKAKELTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLEltlAKVEKEKHATENKVKNLTEEMAALDDII 991
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE---IKREAEEEEEEELEKLQEKLEQLEEELL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 992 AKLTKEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDL 1071
Cdd:pfam02463 377 AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1072 ---ENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARE-LEE 1147
Cdd:pfam02463 457 elkLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGdLGV 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1148 ISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQADSVAELGEQIDNLQRVKQKLEKEKSELR 1227
Cdd:pfam02463 537 AVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1228 LELDDVVSNMEHVVKTK------ANLEKMTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKLQSENGELSRQLEEKDSLVS 1301
Cdd:pfam02463 617 EDDKRAKVVEGILKDTEltklkeSAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILR 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1302 QLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQ--SARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQ------- 1372
Cdd:pfam02463 697 RQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQdkINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELslkekel 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1373 --WRTKYETDAIQRTE-------ELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLER------- 1436
Cdd:pfam02463 777 aeEREKTEKLKVEEEKeeklkaqEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEklaeeel 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1437 ---SNAAAAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISD 1513
Cdd:pfam02463 857 erlEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEE 936
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1514 LTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIKADIERKLAEKDE 1583
Cdd:pfam02463 937 PEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKK 1006
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1312-1804 |
1.63e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1312 QQIEDLKRQLEEETKAKSALAHAVQSARHDTDL--LREQYEEEQEAKAELQRGMSKANSEVAQwrTKYETdAIQRTEELE 1389
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELLEPIreLAERYAAARERLAELEYLRAALRLWFAQ--RRLEL-LEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1390 EAKKKLAQRLQETEEAVEAVNAKCSSLE--------KTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDkvlsewkQK 1461
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALG-------LP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1462 FEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSI-HELEKMRKQLEQEKS 1540
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIpARLLALRDALAEALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1541 EIQSAL----EEAEASLEHE--EGKI-----------------------------LRAQLEFSQIKADIERK-------- 1577
Cdd:COG4913 455 LDEAELpfvgELIEVRPEEErwRGAIervlggfaltllvppehyaaalrwvnrlhLRGRLVYERVRTGLPDPerprldpd 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1578 -LAEK---------------------------DEEMEQSKRNLQRT-------------------------------IDT 1598
Cdd:COG4913 535 sLAGKldfkphpfrawleaelgrrfdyvcvdsPEELRRHPRAITRAgqvkgngtrhekddrrrirsryvlgfdnrakLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1599 LQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANR--QAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKEntaiv 1676
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDASSDDLAA----- 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1677 errnnlLQAELEELRAALEQTERgrklaeqelldtservqllhsqntsllnQKKKLETDISQLQTEVEEAVQECRNA--- 1753
Cdd:COG4913 690 ------LEEQLEELEAELEELEE----------------------------ELDELKGEIGRLEKELEQAEEELDELqdr 735
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 163644331 1754 -EEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQ 1804
Cdd:COG4913 736 lEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1293-1921 |
1.82e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1293 LEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKsALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQ 1372
Cdd:PTZ00121 1026 IEKIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKAE-AKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAK 1104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1373 wrtKYETDAIQRTEELEEAKKKL--------AQRLQETEEAVEAVNAKCSSLEKTKHRLQN----EIEDLMVDLERSNAA 1440
Cdd:PTZ00121 1105 ---KTETGKAEEARKAEEAKKKAedarkaeeARKAEDARKAEEARKAEDAKRVEIARKAEDarkaEEARKAEDAKKAEAA 1181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1441 AAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTE--LFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQL 1518
Cdd:PTZ00121 1182 RKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAkkAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1519 GEG---GKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIKADIERKLAEKDEEMEQSKRNLQRT 1595
Cdd:PTZ00121 1262 MAHfarRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA 1341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1596 IDTLQSSLESETRSRNEALRIKKKMEGDlnemEIQLSQANRQAAEAQKQLKSVHaHMKDAQLQLDDSLRTNEDLKENTAi 1675
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAA----EKKKEEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAA- 1415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1676 VERRNNLLQAELEELRAALEQTERGR-KLAEQELLDTSERVQllHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAE 1754
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKADEAKKKAEeAKKADEAKKKAEEAK--KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1755 EKAKKAitDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAMKGGKKQVQKLEaRVRELESEVESEQKK 1834
Cdd:PTZ00121 1494 EAKKKA--DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAK 1570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1835 SSEAVKGIrkyERRIKELTYQTEEDRknlarlQDLVDKLQLKVKAYKRAAEEAEEQANTNLSKFRKIQHELDEAEERADI 1914
Cdd:PTZ00121 1571 KAEEDKNM---ALRKAEEAKKAEEAR------IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
....*..
gi 163644331 1915 AESQVNK 1921
Cdd:PTZ00121 1642 EAEEKKK 1648
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1200-1873 |
2.32e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.64 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1200 DSVAELGEQIDNLQRVKQKLEKEKSELRL--ELDDVVSNMEHVVKTKANLEKMTRSLEDQMNEykTKYEEGQRCINDFTM 1277
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1278 QKSKLQSENGELSRQLEEKDSLVSQLTRSKM-SYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAK 1356
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRgNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1357 AELQRGMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQE-----------TEEAVEAVNAKCSSLEKTKHRL-- 1423
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiaslerrksniPARLLALRDALAEALGLDEAELpf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1424 --------------QNEIE--------DLMVDLERSNAAAAALDK---KQR-NFDKVlsewkqkfEESQAELESSQKEAR 1477
Cdd:COG4913 463 vgelievrpeeerwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1478 CLSTEL-FK-------LKNSYEEALDH-----LETMKRENKNlqeeisdLTEQ-LGEGGKSIHEL--------------- 1528
Cdd:COG4913 535 SLAGKLdFKphpfrawLEAELGRRFDYvcvdsPEELRRHPRA-------ITRAgQVKGNGTRHEKddrrrirsryvlgfd 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1529 -EKMRKQLEQEKSEIQSALEEAEASLEheegkILRAQLEFSQIKADIERKLAEKDEEmEQSKRNLQRTIDTLQSSLESET 1607
Cdd:COG4913 608 nRAKLAALEAELAELEEELAEAEERLE-----ALEAELDALQERREALQRLAEYSWD-EIDVASAEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1608 RSRNEALRIKKKmegdLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEdlkentAIVERRNNLLQAEL 1687
Cdd:COG4913 682 ASSDDLAALEEQ----LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE------AAEDLARLELRALL 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1688 EELRAALEQTERGRKLAEQelldtservqllhsqntsLLNQKKKLETDISQLQTEVEEAVQE-CRNAEEKAKKAITDAAM 1766
Cdd:COG4913 752 EERFAAALGDAVERELREN------------------LEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLES 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1767 MAEELK-----KEQDTSAHLERMK----KNMEQTIKDLQHRLDEAEQIAmkggKKQVQKLEARVRELE------SEVESE 1831
Cdd:COG4913 814 LPEYLAlldrlEEDGLPEYEERFKellnENSIEFVADLLSKLRRAIREI----KERIDPLNDSLKRIPfgpgryLRLEAR 889
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 163644331 1832 QKKSSEavkgIRKYERRIKELT----YQTEEDR-KNLARLQDLVDKL 1873
Cdd:COG4913 890 PRPDPE----VREFRQELRAVTsgasLFDEELSeARFAALKRLIERL 932
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1417-1926 |
2.66e-12 |
|
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: 71.98 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1417 EKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKLK---NSYEEA 1493
Cdd:TIGR04523 137 KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKkkiQKNKSL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1494 LDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIKAD 1573
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1574 IE----RKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVH 1649
Cdd:TIGR04523 297 ISdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1650 AHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQK 1729
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1730 KKLETDISQLQTEVEEAVQECRNAEEKAKKaitdaamMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiAMKG 1809
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKQNLEQ-------KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE-KIEK 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1810 GKKQVQKLEARVRELESEVES--EQKKSSEAVKGIRKYERRIKELtyqtEEDRKNLARLQdlvDKLQLKVKAYKRAAEEA 1887
Cdd:TIGR04523 529 LESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEEL----KQTQKSLKKKQ---EEKQELIDQKEKEKKDL 601
|
490 500 510
....*....|....*....|....*....|....*....
gi 163644331 1888 EEQANTNLSKFRKIQHELDEAEERADIAESQVNKLRAKS 1926
Cdd:TIGR04523 602 IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
869-1302 |
5.67e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 869 EARRKELEEKMVSLLQEKNDLQLQVQA-------EQDNLCDAEERCDQLIKNKIQLEAKAKELTERLEDEEEMNAELTAK 941
Cdd:PRK02224 313 EARREELEDRDEELRDRLEECRVAAQAhneeaesLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 942 KRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAkltkEKKALQEA--------------HQQ 1007
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE----EAEALLEAgkcpecgqpvegspHVE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1008 TLDDlqsEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRmDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDF 1087
Cdd:PRK02224 469 TIEE---DRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1088 EISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLArELEEISERLEEAGGATAAQIEMNK 1167
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIERLREKREALAELND 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1168 KREAEFQKLR---RDLEEATLQHEATAATLRKKQADSVaelgeqidnLQRVKQKLEkEKSELRLELDDVVSNMEHVVKTK 1244
Cdd:PRK02224 624 ERRERLAEKRerkRELEAEFDEARIEEAREDKERAEEY---------LEQVEEKLD-ELREERDDLQAEIGAVENELEEL 693
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 163644331 1245 ANLEKMTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKLQSEN-GELSRQLEEKDSLVSQ 1302
Cdd:PRK02224 694 EELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNvETLERMLNETFDLVYQ 752
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
842-1232 |
7.06e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 7.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 842 LKSAEAE-KEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQD--NLCDAEERCDQLIKNKIQLE 918
Cdd:COG4717 73 LKELEEElKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 919 AKAKELTERLEDEEEMNAELTAKKRKLEDEC-----------SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAL 987
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLeqlslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 988 DDIIAKLTKEKKALQE-----------AHQQTLDDLQSEEDKV---------------NTLTKAKAKLEQQVDDLEGSLE 1041
Cdd:COG4717 233 ENELEAAALEERLKEArlllliaaallALLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1042 QEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNgkiedeqtiCIQLQKKLKELQARIEELE 1121
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ---------LEELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1122 EELEAERAARAKvekQRADLARELEEISERLEEAGGATAAQIEMNKKR--EAEFQKLRRDLEEATLQHEAtaatLRKKQA 1199
Cdd:COG4717 384 EEELRAALEQAE---EYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEE----LREELA 456
|
410 420 430
....*....|....*....|....*....|....*
gi 163644331 1200 DSVAELG--EQIDNLQRVKQKLEKEKSELRLELDD 1232
Cdd:COG4717 457 ELEAELEqlEEDGELAELLQELEELKAELRELAEE 491
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1041-1762 |
1.05e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 70.38 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1041 EQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKkdfeisqlngkIEDEQTICIQLQKKLKELQARIEEL 1120
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKH-----------LREALQQTQQSHAYLTQKREAQEEQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1121 EEELEAERAARAKVEKQRADLAReLEEISERLEEAggATAAQIEMNKKREAEFQKlRRDLEEATLQHEATAATLRKKQAD 1200
Cdd:TIGR00618 256 LKKQQLLKQLRARIEELRAQEAV-LEETQERINRA--RKAAPLAAHIKAVTQIEQ-QAQRIHTELQSKMRSRAKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1201 SVAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNMEHVVKTKANLEKMtRSLEDQMNEYKTKyeegqrcINDFTMQKS 1280
Cdd:TIGR00618 332 AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI-HTLQQQKTTLTQK-------LQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1281 KLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQ----LEEETKAKSALAHAVQSARHdtdlLREQYEEEQEAK 1356
Cdd:TIGR00618 404 ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCaaaiTCTAQCEKLEKIHLQESAQS----LKEREQQLQTKE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1357 AELQRgmskansevaqwRTKYETDAIQRTEELEEAKKKLAQRLQETEEAV------EAVNAKCSSLEKTKHRLQNEIEDL 1430
Cdd:TIGR00618 480 QIHLQ------------ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnpGPLTRRMQRGEQTYAQLETSEEDV 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1431 MVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELfklknsyeEALDHLETMKRENknLQEE 1510
Cdd:TIGR00618 548 YHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT--------EKLSEAEDMLACE--QHAL 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1511 ISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIKADIERKLAEKDEEMEQSKR 1590
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1591 NLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLK 1670
Cdd:TIGR00618 698 MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTG 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1671 ENTAIVERRNNLLQAELEELRAALEQTE----RGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEA 1746
Cdd:TIGR00618 778 AELSHLAAEIQFFNRLREEDTHLLKTLEaeigQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEEC 857
|
730
....*....|....*.
gi 163644331 1747 VQECRNAEEKAKKAIT 1762
Cdd:TIGR00618 858 SKQLAQLTQEQAKIIQ 873
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1197-1911 |
1.11e-11 |
|
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: 70.25 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1197 KQADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNMEHVVKTKANLEKMTRSLEDQMNEYKTkyeegqRCINDFT 1276
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRD------ELNGELS 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1277 MQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLReqyeeeQEAK 1356
Cdd:pfam12128 312 AADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRR------SKIK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1357 AELQRGMSKANSEVAQwrtKYETDAIQRTEElEEAKKKLAQRLQETEEAVEAvnakcsSLEKTKHRLQNEIEDLMVdleR 1436
Cdd:pfam12128 386 EQNNRDIAGIKDKLAK---IREARDRQLAVA-EDDLQALESELREQLEAGKL------EFNEEEYRLKSRLGELKL---R 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1437 SNAAAAALDKK--QRNFDKVLsewkqkfEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDL 1514
Cdd:pfam12128 453 LNQATATPELLlqLENFDERI-------ERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDEL 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1515 TEQLGEGGKSIHELekMRKQLEQEKSEIQSALEEA---EASLEHE-EGKILRAQLEFSQIKADIERKLAEKDEEMEQSkr 1590
Cdd:pfam12128 526 ELQLFPQAGTLLHF--LRKEAPDWEQSIGKVISPEllhRTDLDPEvWDGSVGGELNLYGVKLDLKRIDVPEWAASEEE-- 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1591 nLQRTIDTLQSSLESEtRSRNEALrikkkmegdlnemEIQLSQANRQAAEAQKQLKSVHAHMKDAQL---QLDDSLRtNE 1667
Cdd:pfam12128 602 -LRERLDKAEEALQSA-REKQAAA-------------EEQLVQANGELEKASREETFARTALKNARLdlrRLFDEKQ-SE 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1668 DLKENTAIvERRNNLLQAELEELRAALEQTERGRKLAEQELLDTServqllhSQNTSLLNQKKK-LETDISQLQTEVEEA 1746
Cdd:pfam12128 666 KDKKNKAL-AERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQK-------REARTEKQAYWQvVEGALDAQLALLKAA 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1747 VQecrnAEEKAKKAITDA--AMMAEELKK---EQDTSAHLERMKKNMEQTIKDLQHRLDEA---EQIAMKGGKKQVQKLE 1818
Cdd:pfam12128 738 IA----ARRSGAKAELKAleTWYKRDLASlgvDPDVIAKLKREIRTLERKIERIAVRRQEVlryFDWYQETWLQRRPRLA 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1819 ARVRELESEVESEQ----KKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKL-QLKVKAYKRAAEEAEEQANT 1893
Cdd:pfam12128 814 TQLSNIERAISELQqqlaRLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLaTLKEDANSEQAQGSIGERLA 893
|
730
....*....|....*...
gi 163644331 1894 NLSKFRKIQHELDEAEER 1911
Cdd:pfam12128 894 QLEDLKLKRDYLSESVKK 911
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1213-1876 |
2.33e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 68.89 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1213 QRVKQKLEKEKSELR---LELDDVVSNMEHVVKTKANLEKMTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKLqseNGEL 1289
Cdd:TIGR04523 36 KQLEKKLKTIKNELKnkeKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKI---NSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1290 SRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAhavqSARHDTDLLREQYEEEQEAKAELQRGMSKANSE 1369
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELE----KLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1370 VAQWRTKYetdaiQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQR 1449
Cdd:TIGR04523 189 IDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1450 NFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEalDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELE 1529
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ--DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1530 KMRKQLEQEKSEIQSALEEAEASLEHEEGKIlraqlefsqikadieRKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRS 1609
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEI---------------EKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1610 RNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEE 1689
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1690 LRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVeeavqecRNAEEKAKKaitdaamMAE 1769
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI-------SDLEDELNK-------DDF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1770 ELKKEQdtsahLERMKKNMEQTIKDLQHRLDEaeqiamkggkkqvqkLEARVRELESEVESEQKKSSEAVKGIRKYERRI 1849
Cdd:TIGR04523 553 ELKKEN-----LEKEIDEKNKEIEELKQTQKS---------------LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612
|
650 660
....*....|....*....|....*..
gi 163644331 1850 KELTYQTEEDRKNLARLQDLVDKLQLK 1876
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSIIKNIKSK 639
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1172-1798 |
2.55e-11 |
|
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: 69.08 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1172 EFQKLRRDLEEATLQHEATAATLRKKQaDSVAELGEQIDNlQRVKQKLEKEKSELRLELDDVVSNMEHvvktkanlekMT 1251
Cdd:pfam10174 131 ELFLLRKTLEEMELRIETQKQTLGARD-ESIKKLLEMLQS-KGLPKKSGEEDWERTRRIAEAEMQLGH----------LE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1252 RSLEDQMNEYKTKYEEGQRcindftmqKSKLQSENGE---LSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAK 1328
Cdd:pfam10174 199 VLLDQKEKENIHLREELHR--------RNQLQPDPAKtkaLQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1329 SALAHAVQSARHDTDLLREQYEEeqeakaeLQRGMSKANSEVAQWRTKYETDAIQRTEELeeakkklaqrlQETEEAVEA 1408
Cdd:pfam10174 271 EEEIKQMEVYKSHSKFMKNKIDQ-------LKQELSKKESELLALQTKLETLTNQNSDCK-----------QHIEVLKES 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1409 VNAKcsslEKTKHRLQNEIEDLMVDLERSnaaAAALDKKQRnfdkvlsewkqkfeesqaELESSQKEARCLSTELFKLKn 1488
Cdd:pfam10174 333 LTAK----EQRAAILQTEVDALRLRLEEK---ESFLNKKTK------------------QLQDLTEEKSTLAGEIRDLK- 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1489 syeealDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEfs 1568
Cdd:pfam10174 387 ------DMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQ-- 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1569 qiKADIERKLAEKDEEMEQSKRNLQRTIDTLQ--------SSLESETRSRNEALRIKKKmEGDLNEMEIQLSQANRQAAE 1640
Cdd:pfam10174 459 --REREDRERLEELESLKKENKDLKEKVSALQpeltekesSLIDLKEHASSLASSGLKK-DSKLKSLEIAVEQKKEECSK 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1641 AQKQLKSVHahmkdaqlQLDDSLRTNEDLKENTAIVERR-------NNLLQAELEELRAALEQTERGRKLAEQELLDTSE 1713
Cdd:pfam10174 536 LENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEvarykeeSGKAQAEVERLLGILREVENEKNDKDKKIAELES 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1714 RVQLLH-SQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQdtsahLERMKKNMEQTI 1792
Cdd:pfam10174 608 LTLRQMkEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQE-----LDATKARLSSTQ 682
|
....*.
gi 163644331 1793 KDLQHR 1798
Cdd:pfam10174 683 QSLAEK 688
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1133-1838 |
5.66e-11 |
|
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: 67.82 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1133 KVEKQRADLARELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEEAtLQHEATAATLRKKQADSVAELGEQIDNL 1212
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEE-IQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1213 QRVKQKLEKEKSELRLELDDVVSNMEHVVKTKANLEKMTRSLEDQMN-EYKTKYEEGQRCINDFTMQKSKLQSENGELSR 1291
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1292 QLEEKDSLVSQLTrskmSYTQQIEDLKRQLEEETKAKSA-LAHAVQSARHDTdllreqyEEEQEAKAELQRGMS--KANS 1368
Cdd:pfam05483 248 QITEKENKMKDLT----FLLEESRDKANQLEEKTKLQDEnLKELIEKKDHLT-------KELEDIKMSLQRSMStqKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1369 EVAQWRTKyetDAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEK----TKHRLQN---EIEDLMVDLERSNAAA 1441
Cdd:pfam05483 317 EDLQIATK---TICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEllrtEQQRLEKnedQLKIITMELQKKSSEL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1442 AALDKKQRNFDKVLSEWKQKFEESQAELESsQKEARCLSTELfklKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEG 1521
Cdd:pfam05483 394 EEMTKFKNNKEVELEELKKILAEDEKLLDE-KKQFEKIAEEL---KGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1522 GKsihELEKMRKQLEQEKSEiqsaleeaEASLEHEEGKILRAQLEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQS 1601
Cdd:pfam05483 470 LK---EVEDLKTELEKEKLK--------NIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1602 SLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNN 1681
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENK 618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1682 LLQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKK----KLETDISQLQTEVEEAVQECRNAEEKA 1757
Cdd:pfam05483 619 ALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKiseeKLLEEVEKAKAIADEAVKLQKEIDKRC 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1758 KKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAMKGGKKQVQKLEarvRELESEVESEQKKSSE 1837
Cdd:pfam05483 699 QHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLK---KQLEIEKEEKEKLKME 775
|
.
gi 163644331 1838 A 1838
Cdd:pfam05483 776 A 776
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1247-1716 |
5.68e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1247 LEKMTRSLEDQMNEYKTKYEEgqrcINDFTMQKSKLQSENGELSRQLEEKDSLVSQLtrskmSYTQQIEDLKRQLEEETK 1326
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEE----LEELEEELEELEAELEELREELEKLEKLLQLL-----PLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1327 AKSALAHAVQSARHdtdlLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQETEEAV 1406
Cdd:COG4717 147 RLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1407 EAVNAKCSSLEKTK--HRLQNEIEDLMVDLeRSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELEssqkearCLSTELF 1484
Cdd:COG4717 223 EELEEELEQLENELeaAALEERLKEARLLL-LIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLA-------LLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1485 KLKNSYEEALDHLETMKRENKNLQEEISDLTEQLG-EGGKSIHELEKMRKQLEQEKsEIQSALEEAEASLEHEEGKILRA 1563
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQ-ELLREAEELEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1564 QLeFSQIKADIERKLAEKDEEMEQsKRNLQRTIDTLQSSLESETRSRNEALRikkkmEGDLNEMEIQLSQANRQAAEAQK 1643
Cdd:COG4717 374 AL-LAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEELEELEE 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 163644331 1644 QLKSVHAHMKDAQLQLddslrtnEDLKENTAIVErrnnlLQAELEELRAALEQTERGR---KLAEQELLDTSERVQ 1716
Cdd:COG4717 447 ELEELREELAELEAEL-------EQLEEDGELAE-----LLQELEELKAELRELAEEWaalKLALELLEEAREEYR 510
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
911-1353 |
6.85e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 911 IKNKIQLEAKAKELTErLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKhatenKVKNLTEEMAALDDI 990
Cdd:COG4717 67 ELNLKELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 991 IAKLTKEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDL----EGSLEQEKKLRMDLERAKRKLEGDLKLTQE 1066
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1067 SLMDLENDKQQLEERLKKKDFE--ISQLNGKIEDEQTIC-------------------------------IQLQKKLKEL 1113
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEerLKEARLLLLIAAALLallglggsllsliltiagvlflvlgllallfLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1114 QARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEEATLQheataAT 1193
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA-----AL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1194 LRKKQADSVAELGEQIDNLQRvKQKLEKEKSELRLELDDVVSNMEHVVK--TKANLEKMTRSLEDQMNEYKTKYEEgqrc 1271
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEalDEEELEEELEELEEELEELEEELEE---- 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1272 indftmqkskLQSENGELSRQLE--EKDSLVSQLtrskmsyTQQIEDLKRQLEEETKAKSALAHAVQSARHdtdlLREQY 1349
Cdd:COG4717 451 ----------LREELAELEAELEqlEEDGELAEL-------LQELEELKAELRELAEEWAALKLALELLEE----AREEY 509
|
....
gi 163644331 1350 EEEQ 1353
Cdd:COG4717 510 REER 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1145-1610 |
7.99e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 7.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1145 LEEISERLEEAGGATAAQIEMNKKreaEFQKLRRDLEEATLQHEATAATLRKKQadsvaELGEQIDNLQRVKQKLEKEKS 1224
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLK---ELKELEEELKEAEEKEEEYAELQEELE-----ELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1225 ELRLELDDvvsnmEHVVKTKANLEKMTRSLEDQMNEYKTKYEEgqrcINDFTMQKSKLQSENGELSRQLEEKDSLVSQLT 1304
Cdd:COG4717 120 KLEKLLQL-----LPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1305 RSKMSYT-QQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKaELQRGMSKANSEVAQWRTKYETDAIQ 1383
Cdd:COG4717 191 EEELQDLaEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLLIAAALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1384 RTEE------------LEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNF 1451
Cdd:COG4717 270 SLILtiagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1452 DKVLSEWKQkfEESQAELESSQKEARCLsteLFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKM 1531
Cdd:COG4717 350 QELLREAEE--LEEELQLEELEQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1532 --RKQLEQEKSEIQSALEEAEASLE--HEEGKILRAQLE-------FSQIKADIERKLAEKDEEMEQSKRN--LQRTIDT 1598
Cdd:COG4717 425 ldEEELEEELEELEEELEELEEELEelREELAELEAELEqleedgeLAELLQELEELKAELRELAEEWAALklALELLEE 504
|
490
....*....|..
gi 163644331 1599 LQSSLESETRSR 1610
Cdd:COG4717 505 AREEYREERLPP 516
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
929-1855 |
9.48e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.45 E-value: 9.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 929 EDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEE--------MAALDDIIAKLTKEKKA 1000
Cdd:pfam15921 253 ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQarnqnsmyMRQLSDLESTVSQLRSE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1001 LQEAHQQTlddlqseEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEE 1080
Cdd:pfam15921 333 LREAKRMY-------EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWD 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1081 RLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATA 1160
Cdd:pfam15921 406 RDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELT 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1161 AQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQA------DSVAELGEQIDNLQRVKQKLEKEKSELRlELDDVV 1234
Cdd:pfam15921 486 AKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSrvdlklQELQHLKNEGDHLRNVQTECEALKLQMA-EKDKVI 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1235 SNMEHVVKTKANLEKMTRSLEDQMNEYKTKYEEGqrcINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQI 1314
Cdd:pfam15921 565 EILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKE---INDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAG 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1315 EDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEeeqeakaELQRGMSkansevaqwrtkyetdaiQRTEELEEAKKK 1394
Cdd:pfam15921 642 SERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYE-------VLKRNFR------------------NKSEEMETTTNK 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1395 LAQRLQETEeaveavnakcSSLEKTKHRLQNeiedlmvdLERSNAAAAaldkkqrnfdKVLSEWKQKFEESQAELESSQK 1474
Cdd:pfam15921 697 LKMQLKSAQ----------SELEQTRNTLKS--------MEGSDGHAM----------KVAMGMQKQITAKRGQIDALQS 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1475 EARCLstelfklknsyEEALDHletMKRENKNLQEEISDLTEQLG----EGGKSIHELEKMRKQLEQEKSEIQSaleeAE 1550
Cdd:pfam15921 749 KIQFL-----------EEAMTN---ANKEKHFLKEEKNKLSQELStvatEKNKMAGELEVLRSQERRLKEKVAN----ME 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1551 ASLEheegkilRAQLEFSQIKADIERklaekdEEMEQSKRNLQRTIDTlqSSLESETRSRNEALRIKKkmegdLNEMEIQ 1630
Cdd:pfam15921 811 VALD-------KASLQFAECQDIIQR------QEQESVRLKLQHTLDV--KELQGPGYTSNSSMKPRL-----LQPASFT 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1631 LSQANRQAAEAQKQLKSVHAhMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALeQTERGRKLAEQELLD 1710
Cdd:pfam15921 871 RTHSNVPSSQSTASFLSHHS-RKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGRAP-SLGALDDRVRDCIIE 948
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1711 TSERVQLLHSQNTSLLNQKKKLETDISQlqteveEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ 1790
Cdd:pfam15921 949 SSLRSDICHSSSNSLQTEGSKSSETCSR------EPVLLHAGELEDPSSCFTFPSTASPSVKNSASRSFHSSPKKSPVHS 1022
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1791 TIKDL---------QHR----------LDEAEQIAMKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKE 1851
Cdd:pfam15921 1023 LLTSSaegsigsssQYRsaktihspdsVKDSQSLPIETTGKTCRKLQNRLESLQTLVEDLQLKNQAMSSMIRNQEKRIQK 1102
|
....
gi 163644331 1852 LTYQ 1855
Cdd:pfam15921 1103 VKDQ 1106
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
856-1506 |
1.22e-10 |
|
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: 66.99 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 856 DEFAKLKEAYAKSEARRKELEE---------KMVSLLQEKNDL------QLQVQAEQDNLCDAEERCDQLIKNKIQLEAK 920
Cdd:TIGR00606 471 DRILELDQELRKAERELSKAEKnsltetlkkEVKSLQNEKADLdrklrkLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 921 AKELTERLEDEEEMNAELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAK 993
Cdd:TIGR00606 551 IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 994 LTKekkalQEAHQQTLDDLQSEEDKVNT----LTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLM 1069
Cdd:TIGR00606 631 VCG-----SQDEESDLERLKEEIEKSSKqramLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLR 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1070 DLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEIS 1149
Cdd:TIGR00606 706 LAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK 785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1150 ERLEEAGGATAAQIEMnKKREAEFQKLRRDLEEATLqhEATAATLRKKQADSVAEL---GEQIDNLQRVKQKLEKEKSEL 1226
Cdd:TIGR00606 786 VCLTDVTIMERFQMEL-KDVERKIAQQAAKLQGSDL--DRTVQQVNQEKQEKQHELdtvVSKIELNRKLIQDQQEQIQHL 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1227 RLELDDVVSNMEHVVKTKANLEKMTRSLEdqmneykTKYEEGQRCINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRS 1306
Cdd:TIGR00606 863 KSKTNELKSEKLQIGTNLQRRQQFEEQLV-------ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETS 935
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1307 KMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAK-AELQRGMSKANSEVAQWRTKYETDAIQ-- 1383
Cdd:TIGR00606 936 NKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQlEECEKHQEKINEDMRLMRQDIDTQKIQer 1015
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1384 ----------RTEELEEAKKKLAQRLQETEEaveavnAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDK 1453
Cdd:TIGR00606 1016 wlqdnltlrkRENELKEVEEELKQHLKEMGQ------MQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKK 1089
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 163644331 1454 VLSEWK-QKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKN 1506
Cdd:TIGR00606 1090 ELREPQfRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEIN 1143
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
869-1211 |
1.34e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 869 EARRKELEEKMVSLLQEKNDLQLQVQAEQDnLCDAEERCDQLIKNKI---QLEAKAKELTERLEDEEEMNAELtakkRKL 945
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQE-RREALQRLAEYSWDEIdvaSAEREIAELEAELERLDASSDDL----AAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 946 EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHqqtLDDLQSEEDKVNTLTKA 1025
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LEERFAAALGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1026 KAKLEQQVDDLEGSLEQ-EKKLRMDLERAKRKLEGDLKLTQESLMDLEnDKQQLEERLkkkdfeisqlngkiedEQTICI 1104
Cdd:COG4913 768 RENLEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLP-EYLALLDRL----------------EEDGLP 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1105 QLQKKLKELQARieeleeeleaerAARAKVEKQRADLARELEEISERLEEA---------GGATAAQIEMNKKREAEFQK 1175
Cdd:COG4913 831 EYEERFKELLNE------------NSIEFVADLLSKLRRAIREIKERIDPLndslkripfGPGRYLRLEARPRPDPEVRE 898
|
330 340 350
....*....|....*....|....*....|....*.
gi 163644331 1176 LRRDLEEATLQHEATAATLRKKQADSVAELGEQIDN 1211
Cdd:COG4913 899 FRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
919-1117 |
1.38e-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: 65.56 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 919 AKAKELTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEK 998
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 999 KALQEAHQQTLDDLQSEE-----------DKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQES 1067
Cdd:COG4942 100 EAQKEELAELLRALYRLGrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 163644331 1068 LMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARI 1117
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
869-1235 |
1.55e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.20 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 869 EARRKELEEKMVSLLQEK-----NDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAKELTERLEDEEEMNAELTAKKR 943
Cdd:TIGR04523 287 EKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 944 KLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEEDKVNTLT 1023
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1024 KAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMD-------LENDKQQLEERLKKKDFEISQLNGKI 1096
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSkekelkkLNEEKKELEEKVKDLTKKISSLKEKI 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1097 EDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQradlarelEEISERLEEAGGATAAQIEMN---KKREAEF 1173
Cdd:TIGR04523 527 EKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKN--------KEIEELKQTQKSLKKKQEEKQeliDQKEKEK 598
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 163644331 1174 QKLRRDLEEatlqHEATAATLRKKQADSVAE---LGEQIDNLQRVKQKLEKEKSELRLELDDVVS 1235
Cdd:TIGR04523 599 KDLIKEIEE----KEKKISSLEKELEKAKKEnekLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1317-1699 |
1.79e-10 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 65.69 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1317 LKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEA----KAELQRGMSKANSEVAQWRTKYEtDAIQRTEELEEAK 1392
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQwerqRRELESRVAELKEELRQSREKHE-ELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1393 KKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERsnaaaaaLDKKQRNFDKVLSEWKQKFEESQAELESS 1472
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER-------MKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1473 QKEARCLSTELFKLKNSYEEALDHLETmkrenknLQEEISDLTEQLGEGGKSIHELEKMRKQL----------EQEKSEI 1542
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLTTAHRKEAENEALLEELrslqerlnasERKVEGL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1543 QSALEEAEASLEHEEGKILRAQLEFSQIKAdierKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRsrnealRIKKkmeg 1622
Cdd:pfam07888 257 GEELSSMAAQRDRTQAELHQARLQAAQLTL----QLADASLALREGRARWAQERETLQQSAEADKD------RIEK---- 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644331 1623 dLNEmEIQLSQANRQAAEAQKQ-LKSVHAHMKDAQL-QLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTER 1699
Cdd:pfam07888 323 -LSA-ELQRLEERLQEERMEREkLEVELGREKDCNRvQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
843-1427 |
2.41e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 843 KSAEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDnlcdaeercdqliknkiQLEAKAK 922
Cdd:PRK02224 231 QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE-----------------RLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 923 ELTERLEDEEEMNAELTAkkrkLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQ 1002
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEA----VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1003 EAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERL 1082
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1083 KK-KDFEISQlngKIEDEQTICiqlqkKLKELQARIeeleeeleaeraarAKVEKQRADLARELEEISERLEEAGGATAA 1161
Cdd:PRK02224 450 EAgKCPECGQ---PVEGSPHVE-----TIEEDRERV--------------EELEAELEDLEEEVEEVEERLERAEDLVEA 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1162 QIEMNKKREAefqklRRDLEEATLQHEATAAtlrkKQADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNMEHVV 1241
Cdd:PRK02224 508 EDRIERLEER-----REDLEELIAERRETIE----EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1242 KTKANLEKMTRSLEDqMNEYKTKYEEGQRCINDFTMQKSKLQSENGELSRQLEEKdslvsqltrskmsytqqiEDLKRQL 1321
Cdd:PRK02224 579 SKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK------------------RERKREL 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1322 EEE------TKAKSALAHAVQSARHDTDLLREQYEEeqeaKAELQRGMSKANSEVaqwrtkyetdaiqrtEELEEAKKKL 1395
Cdd:PRK02224 640 EAEfdeariEEAREDKERAEEYLEQVEEKLDELREE----RDDLQAEIGAVENEL---------------EELEELRERR 700
|
570 580 590
....*....|....*....|....*....|..
gi 163644331 1396 AQrLQETEEAVEAVNAKCSSLEKTKHRLQNEI 1427
Cdd:PRK02224 701 EA-LENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
916-1251 |
2.58e-10 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 65.30 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 916 QLEAKAKELTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLT 995
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 996 KEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDK 1075
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1076 QQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLAR------------ 1143
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrtqael 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1144 -----ELEEISERLEEA------GGATAAQ--------IEMNKKR----EAEFQKLRRDLEEATLQHEATAATLRKKQAD 1200
Cdd:pfam07888 275 hqarlQAAQLTLQLADAslalreGRARWAQeretlqqsAEADKDRieklSAELQRLEERLQEERMEREKLEVELGREKDC 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 163644331 1201 SVAELGEQIDNLQRVKQKL---EKEKSELRLELDDVvsnMEHVVKTKANLEKMT 1251
Cdd:pfam07888 355 NRVQLSESRRELQELKASLrvaQKEKEQLQAEKQEL---LEYIRQLEQRLETVA 405
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1383-1829 |
2.65e-10 |
|
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: 65.10 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1383 QRTEELE-------EAKKKLAQ---RLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFD 1452
Cdd:pfam05622 14 QRCHELDqqvsllqEEKNSLQQenkKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1453 KVLSEWKQKFEEsqaeLESSQKEARCLSTELFKLKNS-------------YEEALDHLETMKRENKNLQEEISDLTEQLG 1519
Cdd:pfam05622 94 KEVLELQHRNEE----LTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNAEYMQRTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1520 EGGKSIHELEKMRKQLEQEKSEIQsaleEAEASLEHEEGKILRAQLEFSQIKADIERKLAEKDEEMEQsKRNLQRTIDTL 1599
Cdd:pfam05622 170 QLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIE-RDTLRETNEEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1600 Q-SSLESETRSRNEALRIKKKMEGD----------LNEMEIQLSQANRQAAEAQKQlkSVHAHMKDAQLQLDDSLRTNED 1668
Cdd:pfam05622 245 RcAQLQQAELSQADALLSPSSDPGDnlaaeimpaeIREKLIRLQHENKMLRLGQEG--SYRERLTELQQLLEDANRRKNE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1669 LKENTAIVERRNNLLQAELEELRAALEQtergrklaeqelldtservQLLHSQNTSLLnqKKKLETDISQLQTEVEEAVQ 1748
Cdd:pfam05622 323 LETQNRLANQRILELQQQVEELQKALQE-------------------QGSKAEDSSLL--KQKLEEHLEKLHEAQSELQK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1749 ECRNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQ---TIKDLQHRLDEAEQIAMKGGKKQVQKLEAR 1820
Cdd:pfam05622 382 KKEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksVIKTLDPKQNPASPPEIQALKNQLLEKDKK 461
|
....*....
gi 163644331 1821 VRELESEVE 1829
Cdd:pfam05622 462 IEHLERDFE 470
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1384-1925 |
5.32e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.66 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1384 RTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLmvdlersNAAAAALDKKQRNFDKVLSEWKQKFE 1463
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKIL-------EQQIKDLNDKLKKNKDKINKLNSDLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1464 ESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQ 1543
Cdd:TIGR04523 107 KINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1544 SALEEAEAsleheegKILRAQLEFSQIKADIER--KLAEKDEEMEQSKRNLQRTIDTLQSSLESET-----------RSR 1610
Cdd:TIGR04523 187 KNIDKIKN-------KLLKLELLLSNLKKKIQKnkSLESQISELKKQNNQLKDNIEKKQQEINEKTteisntqtqlnQLK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1611 NEALRIKKKM-----------------EGDLNEMEIQLSQANRQAA-----EAQKQLKSVHAHMKDAQLQLDDSLRTNED 1668
Cdd:TIGR04523 260 DEQNKIKKQLsekqkeleqnnkkikelEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1669 LKENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQ 1748
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1749 ECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLD-------------EAEQIAMKGGKKQVQ 1815
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqnlEQKQKELKSKEKELK 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1816 KLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQL-KVKAYKRAAEEAEEQANTN 1894
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLeKEIDEKNKEIEELKQTQKS 579
|
570 580 590
....*....|....*....|....*....|.
gi 163644331 1895 LSKfrkiqhELDEAEERADIAESQVNKLRAK 1925
Cdd:TIGR04523 580 LKK------KQEEKQELIDQKEKEKKDLIKE 604
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
860-1428 |
6.26e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.36 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 860 KLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAK----ELTERLEDEEEMN 935
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKlqdeNLKELIEKKDHLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 936 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSE 1015
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1016 EDKVNTLTkakAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLM------DLENDKQQLEERLKKKDFEI 1089
Cdd:pfam05483 376 EDQLKIIT---MELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfekiaeELKGKEQELIFLLQAREKEI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1090 SQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEaggaTAAQIEMNKKR 1169
Cdd:pfam05483 453 HDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKK----HQEDIINCKKQ 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1170 EAEFQKLRRDLEEATLQheataatLRkkqadsvaelgeqiDNLQRVKQKLEKEKSELRLELDDVVSNMEHVVKTKANLEK 1249
Cdd:pfam05483 529 EERMLKQIENLEEKEMN-------LR--------------DELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1250 MTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKLQSENGELSRQLE----EKDSLVSQLTRSKMSYTQQIEDLKRQLEEET 1325
Cdd:pfam05483 588 QMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNayeiKVNKLELELASAKQKFEEIIDNYQKEIEDKK 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1326 KAKSALAHAVQSARHDTDllrEQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEEAKkklaQRLQETEEA 1405
Cdd:pfam05483 668 ISEEKLLEEVEKAKAIAD---EAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYK----NKEQEQSSA 740
|
570 580
....*....|....*....|...
gi 163644331 1406 VEAVNAKCSSLEKTKHRLQNEIE 1428
Cdd:pfam05483 741 KAALEIELSNIKAELLSLKKQLE 763
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
804-1876 |
7.20e-10 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 64.69 E-value: 7.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 804 QKIVERRDALLVIQWNVRAFM------GVKN-----WPWMKLFFKIKPLL-----KSAEAEKEMANMKDEFAKLKEAYAK 867
Cdd:TIGR01612 518 DEVPSKNIIGFDIDQNIKAKLykeieaGLKEsyelaKNWKKLIHEIKKELeeeneDSIHLEKEIKDLFDKYLEIDDEIIY 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 868 SEARRKELEEKMVSLlQEKND-----LQLQVQAEQDNlcdaeERCDQLIKnkiqleAKAKELTERLEDEEEMNAELTAKK 942
Cdd:TIGR01612 598 INKLKLELKEKIKNI-SDKNEyikkaIDLKKIIENNN-----AYIDELAK------ISPYQVPEHLKNKDKIYSTIKSEL 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 943 RKLEDEcselkkDIDDLELTLAKVEKEkhateNKVKNlTEEMAALDDIIAKLTKEKKALQEAHQQTLddlqseEDKVNTL 1022
Cdd:TIGR01612 666 SKIYED------DIDALYNELSSIVKE-----NAIDN-TEDKAKLDDLKSKIDKEYDKIQNMETATV------ELHLSNI 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1023 TKAKAKLEQQVddlegsLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTI 1102
Cdd:TIGR01612 728 ENKKNELLDII------VEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINI 801
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1103 ciqlqKKLKELQArieeleeeleaeraarakveKQRADLARE-LEEISERLEEaggaTAAQIEMNKKREAEFqklrrdle 1181
Cdd:TIGR01612 802 -----DNIKDEDA--------------------KQNYDKSKEyIKTISIKEDE----IFKIINEMKFMKDDF-------- 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1182 eatLQHEATAATLRKKQADSVAELGEQIDNLqrvkqkLEKEKSELRlelDDVVSNMEHVVK-TKANLEKMTRSLEDQMNE 1260
Cdd:TIGR01612 845 ---LNKVDKFINFENNCKEKIDSEHEQFAEL------TNKIKAEIS---DDKLNDYEKKFNdSKSLINEINKSIEEEYQN 912
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1261 YKT--KYEEGQRCINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIE----DLKRQLEEETKAKSALAHA 1334
Cdd:TIGR01612 913 INTlkKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDntliDKINELDKAFKDASLNDYE 992
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1335 VQS--------------ARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQ 1400
Cdd:TIGR01612 993 AKNnelikyfndlkanlGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLN 1072
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1401 EteEAVEAVNAKCSSLEKTKHRLQ----------------NEIEDLMVDLErsnaaaaALDKKQRNFDKVLSEWKQKFEE 1464
Cdd:TIGR01612 1073 K--EILEEAEINITNFNEIKEKLKhynfddfgkeenikyaDEINKIKDDIK-------NLDQKIDHHIKALEEIKKKSEN 1143
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1465 SQAELESSQKEARCLSTELFKLKN--SYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMR---------- 1532
Cdd:TIGR01612 1144 YIDEIKAQINDLEDVADKAISNDDpeEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKginlsygknl 1223
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1533 -----KQLEQEKSEIQSALEEAEASLEHEEGkiLRAQLEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESET 1607
Cdd:TIGR01612 1224 gklflEKIDEEKKKSEHMIKAMEAYIEDLDE--IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENIS 1301
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1608 RSRNEALRIKKKM--EGDLNEMEIQLsqaNRQAAEAQKQLKSVHAHMKDAQ-----LQLDDSLRTNEDLKENTAIVERRN 1680
Cdd:TIGR01612 1302 DIREKSLKIIEDFseESDINDIKKEL---QKNLLDAQKHNSDINLYLNEIAniyniLKLNKIKKIIDEVKEYTKEIEENN 1378
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1681 NLLQAEL----------------EELRAALEQTERGRKLAE--QELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTE 1742
Cdd:TIGR01612 1379 KNIKDELdkseklikkikddinlEECKSKIESTLDDKDIDEciKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKN 1458
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1743 VEEAVQECRN-AEEKAKKAITDAAMMAEELKKEQDTS-----------AHLERMKKNMEQTIKDLQHRLDEAEQIAMKGG 1810
Cdd:TIGR01612 1459 IEMADNKSQHiLKIKKDNATNDHDFNINELKEHIDKSkgckdeadknaKAIEKNKELFEQYKKDVTELLNKYSALAIKNK 1538
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1811 ----KKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLK 1876
Cdd:TIGR01612 1539 faktKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENK 1608
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
854-1295 |
8.69e-10 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 64.07 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 854 MKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCdqlikNKIQLEAKAkeLTERLEDEEE 933
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRA-----AILQTEVDA--LRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 934 MNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQ------ 1007
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtalt 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1008 TLDDLQSEEDKV-NTLTKAKAKLEQQVDDlegSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKD 1086
Cdd:pfam10174 440 TLEEALSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKD 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1087 FEISQLNGKIEDEQTICIQLQKKLKELQarieeleeeleaeraarakvekQRADLARELEEISERLEEAGGATAAQIEMN 1166
Cdd:pfam10174 517 SKLKSLEIAVEQKKEECSKLENQLKKAH----------------------NAEEAVRTNPEINDRIRLLEQEVARYKEES 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1167 KKREAEFQKLR---RDLEEATLQHEATAATLRKKQADSVAELGEQIDNLQRVKQKLEKEKSEL----RLELDDVVSNMEH 1239
Cdd:pfam10174 575 GKAQAEVERLLgilREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLleeaRRREDNLADNSQQ 654
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 163644331 1240 VvktkaNLEKMTRSLE---DQMNEYKTKYEEGQRCIndfTMQKSKLQSENGELSRQLEE 1295
Cdd:pfam10174 655 L-----QLEELMGALEktrQELDATKARLSSTQQSL---AEKDGHLTNLRAERRKQLEE 705
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1294-1777 |
1.02e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1294 EEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALahavQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQW 1373
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1374 RTKYETDAIQRT-EELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMV----DLERSNAAAAALDKKQ 1448
Cdd:COG4717 129 PLYQELEALEAElAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLateeELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1449 RNFDKVLSEWKQKFEESQAELESSQKEArclstELFKLKNSYEE---------ALDHLETMKRENKNLQEEISDLTeQLG 1519
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEarlllliaaALLALLGLGGSLLSLILTIAGVL-FLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1520 EGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQikaDIERKLAEKDEEMEQSKRNLQRTIDTL 1599
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPP---DLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1600 QSSLESEtrsrnealRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRtnedlkentaivERR 1679
Cdd:COG4717 360 EEELQLE--------ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLG------------ELE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1680 NNLLQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNqkkklETDISQLQTEVEEAVQECRNAEEKAKK 1759
Cdd:COG4717 420 ELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEWAA 494
|
490
....*....|....*...
gi 163644331 1760 AITDAAMMAEELKKEQDT 1777
Cdd:COG4717 495 LKLALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1012-1227 |
1.15e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1012 LQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQ 1091
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1092 LNGKIEDEQTiciQLQKKLKELQARIEELE----------EELEAERAARAKVEKQRADLARELEEISERLEEAGGATAA 1161
Cdd:COG4942 95 LRAELEAQKE---ELAELLRALYRLGRQPPlalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644331 1162 QIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKK---QADSVAELGEQIDNLQRVKQKLEKEKSELR 1227
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKElaeLAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1425-1920 |
1.22e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1425 NEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEW-KQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRE 1503
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAERYAAARERLaELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1504 NKNLQEEISDLTEQL-GEGGKSIHELEKMRKQLEQEKSEI-------QSALEEAEASLEHEEGKILRAQLEFSQIKADIE 1575
Cdd:COG4913 318 LDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERerrrarlEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1576 RKLAEKDE---EMEQSKRNLQRTIDTLQSSLES-ETRSRN---EALRIKKKMEGDLNEMEIQLsqanRQAAEAQkQLKSV 1648
Cdd:COG4913 398 EELEALEEalaEAEAALRDLRRELRELEAEIASlERRKSNipaRLLALRDALAEALGLDEAEL----PFVGELI-EVRPE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1649 HAHMKDAqlqlddslrtnedlkentaiVER-----RNNLL--QAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQ 1721
Cdd:COG4913 473 EERWRGA--------------------IERvlggfALTLLvpPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1722 NTSLLNqkkKLETDISQLQTEVEEAVQE------CRNAEE--KAKKAITDAAMM-----AEELKKEQDTSAHL------E 1782
Cdd:COG4913 533 PDSLAG---KLDFKPHPFRAWLEAELGRrfdyvcVDSPEElrRHPRAITRAGQVkgngtRHEKDDRRRIRSRYvlgfdnR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1783 RMKKNMEQTIKDLQHRLDEAEQiAMKGGKKQVQKLEARVRELE--SEVESEQKKSSEAVKGIRKYERRIKELtyqtEEDR 1860
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEE-RLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERL----DASS 684
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1861 KNLARLQDLVDKLQLKVKAYKRAAEEAEEQAntnlskfRKIQHELDEAEERADIAESQVN 1920
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEI-------GRLEKELEQAEEELDELQDRLE 737
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
977-1426 |
1.29e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 977 VKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRK 1056
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1057 LE--GDLKLTQESLMDLENDKQQLEERLKkkdfEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEEL-EAERAARAK 1133
Cdd:COG4717 128 LPlyQELEALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1134 VEKQRADLARELEEISERLEEAGGATaAQIEMNKKREAEFQKLRR------------------DLEEATLQHEATAATL- 1194
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEEL-EQLENELEAAALEERLKEarlllliaaallallglgGSLLSLILTIAGVLFLv 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1195 ----------RKKQADSVAELGEQIDNLQRVK----QKLEKEKSELRLELDDVVSNMEHVVKTKANLEKMTRSLEDQMNE 1260
Cdd:COG4717 283 lgllallfllLAREKASLGKEAEELQALPALEeleeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1261 YKTKYEEGQRcindftmqKSKLQSENGELSRQLEEKDSLVSQLTRskmsYTQQIEDLKRQLEEETKAKSALAhavqsARH 1340
Cdd:COG4717 363 LQLEELEQEI--------AALLAEAGVEDEEELRAALEQAEEYQE----LKEELEELEEQLEELLGELEELL-----EAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1341 DTDLLREQYEEEQEAKAELQRGMSKANSEVAqwRTKYETDAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKC---SSLE 1417
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELA--ELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKlalELLE 503
|
....*....
gi 163644331 1418 KTKHRLQNE 1426
Cdd:COG4717 504 EAREEYREE 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1490-1917 |
2.28e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1490 YEEALDHLETMKRENKNLqEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEasLEHEEGKILRAQLEFSQ 1569
Cdd:COG4913 237 LERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1570 IKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQA----NRQAAEAQKQL 1645
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeefAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1646 KSVHAHMKDAQLQLDDSLRTNEDLKENTAIV-------ERRNNLLQAELEELRAALEQtERGRKLAE----QELLDTS-- 1712
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELeaeiaslERRKSNIPARLLALRDALAE-ALGLDEAElpfvGELIEVRpe 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1713 --------ERVqlLHSQNTSLL-------------NQKK-----------------------------KLETDISQLQTE 1742
Cdd:COG4913 473 eerwrgaiERV--LGGFALTLLvppehyaaalrwvNRLHlrgrlvyervrtglpdperprldpdslagKLDFKPHPFRAW 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1743 VEEAVQE------CRNAEE--KAKKAITDAAMM-----AEELKKEQDTSAHL------ERMKKNMEQTIKDLQHRLDEAE 1803
Cdd:COG4913 551 LEAELGRrfdyvcVDSPEElrRHPRAITRAGQVkgngtRHEKDDRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1804 QiAMKGGKKQVQKLEARVRELE--SEVESEQKKSSEAVKGIRKYERRIKELtyqtEEDRKNLARLQDLVDKLQLKVKAYK 1881
Cdd:COG4913 631 E-RLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAELEELE 705
|
490 500 510
....*....|....*....|....*....|....*.
gi 163644331 1882 RAAEEAEEQANTNLSKFRKIQHELDEAEERADIAES 1917
Cdd:COG4913 706 EELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
846-1285 |
3.51e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.96 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 846 EAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLcdaeERCDQLIKNkiqLEAKAKELT 925
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL----EQNNKKIKE---LEKQLNQLK 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 926 ERLEDeeemnaeltAKKRKLEDECSELKKDIDdleltlaKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAH 1005
Cdd:TIGR04523 295 SEISD---------LNNQKEQDWNKELKSELK-------NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEN 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1006 QQTLDDLQSEEDKVNTLTKAKA-------KLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQL 1078
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQsykqeikNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1079 EERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGA 1158
Cdd:TIGR04523 439 NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1159 TAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQ-ADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNM 1237
Cdd:TIGR04523 519 ISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEK 598
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 163644331 1238 EHVVKTKANLEKMTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKLQSE 1285
Cdd:TIGR04523 599 KDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1587-1869 |
6.41e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.19 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1587 QSKRNLQRTIDTLQ--SSLESETRSRNEAL-----RIKKKMEGDLNEMEIQLSQANRQaaEAQKQLKSVhahmkdAQLQL 1659
Cdd:COG3206 91 KSRPVLERVVDKLNldEDPLGEEASREAAIerlrkNLTVEPVKGSNVIEISYTSPDPE--LAAAVANAL------AEAYL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1660 DDSLRTNedlkenTAIVERRNNLLQAELEELRAALEQTERgrKLA----EQELLDTSERVQLLHSQNTSLLNQKKKLETD 1735
Cdd:COG3206 163 EQNLELR------REEARKALEFLEEQLPELRKELEEAEA--ALEefrqKNGLVDLSEEAKLLLQQLSELESQLAEARAE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1736 ISQLQTEVEeAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNMEQTIKDLQHRLDEAEQI 1805
Cdd:COG3206 235 LAEAEARLA-ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQR 313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163644331 1806 AMKGGKKQVQKLEARVRELESEVESEQKKsseaVKGIRKYERRIKELTYQTEEDRKN----LARLQDL 1869
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVARELyeslLQRLEEA 377
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1381-1608 |
6.91e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1381 AIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQ 1460
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1461 KFEESQAELE----SSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLE 1536
Cdd:COG4942 98 ELEAQKEELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 163644331 1537 QEKSEiqsaLEEAEASLEHEEGKILRAQLEFSQIKADIERKLAekdeEMEQSKRNLQRTIDTLQSSLESETR 1608
Cdd:COG4942 178 ALLAE----LEEERAALEALKAERQKLLARLEKELAELAAELA----ELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
849-1147 |
7.79e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.89 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 849 KEMANMKDEFA--KLKEAYAKSEARRKELEEKmvSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAKELTE 926
Cdd:pfam05483 471 KEVEDLKTELEkeKLKNIELTAHCDKLLLENK--ELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRD 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 927 RLEDEEEmnaELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQ 1006
Cdd:pfam05483 549 ELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1007 QTLDDLQSEEDKVNT----LTKAKAKLEQQVDDLEGSLE----QEKKLRMDLERAKRKLEGDLKLTQ-----------ES 1067
Cdd:pfam05483 626 AENKQLNAYEIKVNKleleLASAKQKFEEIIDNYQKEIEdkkiSEEKLLEEVEKAKAIADEAVKLQKeidkrcqhkiaEM 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1068 LMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEE 1147
Cdd:pfam05483 706 VALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
885-1533 |
1.04e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 60.69 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 885 EKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAKELTERLEDEEEMNAELtakkRKLEDECSELKKDIDDLELTLA 964
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKL----KSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 965 KVEKEKHATENKVKNLTEEMAALDdiiakltkekkalqeahqQTLDDLQSEEDKVNTLTKAKAKLEqqvDDLEGSLEQEK 1044
Cdd:PRK01156 215 ITLKEIERLSIEYNNAMDDYNNLK------------------SALNELSSLEDMKNRYESEIKTAE---SDLSMELEKNN 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1045 KLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKkdfeISQLNGKIEDEQTIciqlQKKLKELQArieeleeel 1124
Cdd:PRK01156 274 YYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQI----LSNIDAEINKYHAI----IKKLSVLQK--------- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1125 eaERAARAKVEKQRADLARELEEISERLEEAGGATAAQIEMNKKREAEFQKLRR---DLEEATLQHEATAATLRKKQads 1201
Cdd:PRK01156 337 --DYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERmsaFISEILKIQEIDPDAIKKEL--- 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1202 vAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNMEH--------VVKTKANLEKMTRSLEDqMNEYKTKYEEGqrcIN 1273
Cdd:PRK01156 412 -NEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMlngqsvcpVCGTTLGEEKSNHIINH-YNEKKSRLEEK---IR 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1274 DFTMQKSKLqseNGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQ 1353
Cdd:PRK01156 487 EIEIEVKDI---DEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDL 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1354 EAKAElqrGMSKANSEvaqwRTKYETDAIQ-RTEELEEAKKKLAQRLQETEEAVEAVNakcSSLEKTKHRLQNEIEDL-- 1430
Cdd:PRK01156 564 DSKRT---SWLNALAV----ISLIDIETNRsRSNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLnn 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1431 -MVDLERSNAAAAALDKKQRNFDKVLSEwKQKFEESQAELESSQKEarcLSTELFKLKNSYEEALDHLETMKRENKNLQE 1509
Cdd:PRK01156 634 kYNEIQENKILIEKLRGKIDNYKKQIAE-IDSIIPDLKEITSRIND---IEDNLKKSRKALDDAKANRARLESTIEILRT 709
|
650 660
....*....|....*....|....
gi 163644331 1510 EISDLTEQLGEGGKSIHELEKMRK 1533
Cdd:PRK01156 710 RINELSDRINDINETLESMKKIKK 733
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1481-1911 |
1.17e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1481 TELFKLKNSYEEALDHLETMKRENKNLQEEIS---DLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEE 1557
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKrteNIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1558 ---GKILRAQLEFSQIKADIeRKLAEKDEEMEQSKRNLQRTIDTLQS------SLESETRSRNEALRIKKKMEGDLNEME 1628
Cdd:PRK03918 235 elkEEIEELEKELESLEGSK-RKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1629 IQLSQANRQAAEAQKQLKsvhahmkdaqlQLDDSLRTNEDLKENTAIVERRNNLLQA---ELEELRAALEQTERGRK-LA 1704
Cdd:PRK03918 314 KRLSRLEEEINGIEERIK-----------ELEEKEERLEELKKKLKELEKRLEELEErheLYEEAKAKKEELERLKKrLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1705 EQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAvqecRNAEEKAKKAITDAAMMAEELKKEqdtsaHLERM 1784
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL----KKAIEELKKAKGKCPVCGRELTEE-----HRKEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1785 KKNMEQTIKDLQHRLDEAEqiamkggkKQVQKLEARVRELESEVESEQK--KSSEAVKGIRKYERRIKELTYQT-EEDRK 1861
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIE--------EKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEElEKKAE 525
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 163644331 1862 NLARLQDLVDKLQLKVKAYKRAAEEAEEQANtnlsKFRKIQHELDEAEER 1911
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEE 571
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1155-1415 |
1.28e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1155 AGGATAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATlRKKQADSVAELGEQIDNLQRVKQKLEKEKSELRLELddvv 1234
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAEL---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1235 snmehvvktkANLEKMTRSLEDQMNEYKTKYEEGQRcindfTMQKSKLQSENGELSRQleekdSLVSQLTRSKMSYTQQI 1314
Cdd:COG4942 86 ----------AELEKEIAELRAELEAQKEELAELLR-----ALYRLGRQPPLALLLSP-----EDFLDAVRRLQYLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1315 EDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAiQRTEELEEAKKK 1394
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEE 224
|
250 260
....*....|....*....|.
gi 163644331 1395 LAQRLQETEEAVEAVNAKCSS 1415
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPA 245
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
957-1306 |
1.39e-08 |
|
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: 60.24 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 957 DDLELTLAKVEKEKHATENKVKNLTEEMA----ALDDIIAKLTKEKKALQEAH---QQTLDDLQSEEDKVN-TLTKAKAK 1028
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVqangELEKASREETFARTALKNARldlRRLFDEKQSEKDKKNkALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1029 LEQQVDDLEGsleQEKKLRMDLERAKRKLEGDLKltqESLMDLENDKQQLEErlkKKDFEISQLNGKIEDEQTiciQLQK 1108
Cdd:pfam12128 680 ANERLNSLEA---QLKQLDKKHQAWLEEQKEQKR---EARTEKQAYWQVVEG---ALDAQLALLKAAIAARRS---GAKA 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1109 KLKELQARIEELEEELEAERAARAKVEKQRADLARELEEIserleeaggataaqiemnKKREAEFQKLRRDLEEATLQHE 1188
Cdd:pfam12128 748 ELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERI------------------AVRRQEVLRYFDWYQETWLQRR 809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1189 ----ATAATLRKKQADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNMEhvvKTKANLEKMTRSLEDQ-MNEYKT 1263
Cdd:pfam12128 810 prlaTQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLR---GLRCEMSKLATLKEDAnSEQAQG 886
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 163644331 1264 KYEEGQRCINDFtmqKSKLQSENGELSRQLEEKDSLVSQLTRS 1306
Cdd:pfam12128 887 SIGERLAQLEDL---KLKRDYLSESVKKYVEHFKNVIADHSGS 926
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
925-1162 |
1.46e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 925 TERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEa 1004
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1005 hqqtldDLQSEEDKVNTLTKAKAKLEQQvDDLEGSLEQEKKLrmDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKK 1084
Cdd:COG4942 98 ------ELEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFL--DAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163644331 1085 KDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATAAQ 1162
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1076-1539 |
1.47e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1076 QQLEERLKKKDFEISQLNGKIEDEQticiQLQKKLKELQARIEELEEELEAERAARAKVE--KQRADLARELEEISERLE 1153
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1154 EAggatAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDV 1233
Cdd:COG4717 150 EL----EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1234 vsnmehvvktKANLEKMTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKLQSENGELSRQLEEKDSLVSQL--------TR 1305
Cdd:COG4717 226 ----------EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLlallflllAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1306 SKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQwrtkyetdaIQRT 1385
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE---------LQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1386 EELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNfdKVLSEWKQKFEES 1465
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEEL 444
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163644331 1466 QAELESSQKEARCLSTELFKLKNS--YEEALDHLETMKRENKNLQEEIS--DLTEQLgeggksiheLEKMRKQLEQEK 1539
Cdd:COG4717 445 EEELEELREELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAalKLALEL---------LEEAREEYREER 513
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1483-1882 |
1.59e-08 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 59.48 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1483 LFKLKNSYEEaLDHLETMKRE--NKNLQEEISDLtEQLGEGGKSIHELEKMRKQ----LEQEKSEIQSALEEAEASLEhe 1556
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1557 EGKILRAQlefsqikadieRKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKK----------------- 1619
Cdd:pfam06160 78 KYRFKKAK-----------KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKyrelrktllanrfsygp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1620 ----MEGDLNEMEIQLSQ-----ANRQAAEAQKQLKSVHAHMKDAQlqlddslrtnEDLKENTAIVERRNNLLQAELEEL 1690
Cdd:pfam06160 147 aideLEKQLAEIEEEFSQfeeltESGDYLEAREVLEKLEEETDALE----------ELMEDIPPLYEELKTELPDQLEEL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1691 RAALEQ-TERGRKLAEQELLDTSERVQLLHSQNTSLLNQK--KKLETDISQLQTEVEEaVQECRNAEEKAKKaitdaamm 1767
Cdd:pfam06160 217 KEGYREmEEEGYALEHLNVDKEIQQLEEQLEENLALLENLelDEAEEALEEIEERIDQ-LYDLLEKEVDAKK-------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1768 aeELKKEQDT-SAHLERMKKNMEQTIKDLQH-----RLDEAEQIAMKGGKKQVQKLEARVRELESEVESEQKKSSEAVKG 1841
Cdd:pfam06160 288 --YVEKNLPEiEDYLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEE 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 163644331 1842 IRKYERRIKELTYQTEEDRKNLARL-------QDLVDKLQLKVKAYKR 1882
Cdd:pfam06160 366 LEEILEQLEEIEEEQEEFKESLQSLrkdeleaREKLDEFKLELREIKR 413
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1135-1870 |
1.60e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1135 EKQRA-DLARELEEISERLEEAGGA-TAAQIEMNKKREAE--FQKLRR---DLEEATLQHEAtaatlrkkQADSVAELGE 1207
Cdd:PRK04863 305 EQYRLvEMARELAELNEAESDLEQDyQAASDHLNLVQTALrqQEKIERyqaDLEELEERLEE--------QNEVVEEADE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1208 QIDNLQRVKQKLEKEKSELRLELDDVVSNMEhvvktkanlEKMTRSLedQMNEYKTKYEEGQRCINDFTMQKSKLQSENG 1287
Cdd:PRK04863 377 QQEENEARAEAAEEEVDELKSQLADYQQALD---------VQQTRAI--QYQQAVQALERAKQLCGLPDLTADNAEDWLE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1288 ELSRQLEEKDSLVSQLTRsKMSYTQQIedlKRQLEEETKAKSALAHAV------QSARhdtDLLREQyeEEQEAKAELQR 1361
Cdd:PRK04863 446 EFQAKEQEATEELLSLEQ-KLSVAQAA---HSQFEQAYQLVRKIAGEVsrseawDVAR---ELLRRL--REQRHLAEQLQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1362 GMSKANSEVAQwRTKYETDAIQRteeLEEAKKKLAQRLQ----------ETEEAVEAVNAKCSSLEKTKHRLQNEIEDLM 1431
Cdd:PRK04863 517 QLRMRLSELEQ-RLRQQQRAERL---LAEFCKRLGKNLDdedeleqlqeELEARLESLSESVSEARERRMALRQQLEQLQ 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1432 VDLERSNAAAAALdkkqRNFDKVLSewkQKFEESQAELESSQKEARCLSTELFKLKnSYEEALDHLETMKREnknLQEEI 1511
Cdd:PRK04863 593 ARIQRLAARAPAW----LAAQDALA---RLREQSGEEFEDSQDVTEYMQQLLERER-ELTVERDELAARKQA---LDEEI 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1512 SDLTE----------QLGE--GGKSIHE----------------------------LEKMRKQLEQE----------KSE 1541
Cdd:PRK04863 662 ERLSQpggsedprlnALAErfGGVLLSEiyddvsledapyfsalygparhaivvpdLSDAAEQLAGLedcpedlyliEGD 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1542 IQSAleeAEASLEHEEG------KILRAQLEFSQIKA----------------DIER-KLAEKDEEMEQSKRNLQRTIDT 1598
Cdd:PRK04863 742 PDSF---DDSVFSVEELekavvvKIADRQWRYSRFPEvplfgraarekrieqlRAEReELAERYATLSFDVQKLQRLHQA 818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1599 LQSSL------------ESETRSRNEALRikkKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSL--- 1663
Cdd:PRK04863 819 FSRFIgshlavafeadpEAELRQLNRRRV---ELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLadr 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1664 --RTNEDLKE-------------NTAIVERRNNLLQA---ELEELRAALEQTERGRKLAEQELLDTSERVQLLH----SQ 1721
Cdd:PRK04863 896 veEIREQLDEaeeakrfvqqhgnALAQLEPIVSVLQSdpeQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyED 975
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1722 NTSLLNQKKKLEtdiSQLQTEVEEAVQECRNAEEKAKKA---ITDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHR 1798
Cdd:PRK04863 976 AAEMLAKNSDLN---EKLRQRLEQAEQERTRAREQLRQAqaqLAQYNQVLASLKSSYDA---KRQMLQELKQELQDLGVP 1049
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 163644331 1799 LDEAEQIAMKGGKKQVQKL----EARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLV 1870
Cdd:PRK04863 1050 ADSGAEERARARRDELHARlsanRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLV 1125
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
841-1058 |
6.61e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 6.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 841 LLKSAEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAK 920
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 921 AKELTERLEDEEEMNAELTAKKRKLEDEcSELK-----KDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLT 995
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQ-PPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 163644331 996 KEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLE 1058
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1471-1679 |
6.84e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1471 SSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAE 1550
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1551 ASLEhEEGKILRAQLEFSQIKADIER-KLAEKDEEMEQSKRNL----------QRTIDTLQSSLESETRSRNEALRIKKK 1619
Cdd:COG4942 97 AELE-AQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLqylkylaparREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1620 MEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERR 1679
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1347-1589 |
7.21e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1347 EQYEEEQEAKAELQRGMSKANSEVAQWRTKyETDAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNE 1426
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1427 IEDLMVDLERSNAAAAALDKkqrnfdkvlsewkqkfeESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKN 1506
Cdd:COG4942 99 LEAQKEELAELLRALYRLGR-----------------QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1507 LQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIKADIERKLAEKDEEME 1586
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
...
gi 163644331 1587 QSK 1589
Cdd:COG4942 242 RTP 244
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1050-1600 |
7.24e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.60 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1050 LERAKRKLEGDLKLTQESLMDLENdkqqLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQA-------------- 1115
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIeynnamddynnlks 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1116 ---RIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEEATLQHEATAA 1192
Cdd:PRK01156 240 alnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1193 TLRK-----KQADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNMEhvvktkaNLEKMTRSLEDQMNEYKTKYEE 1267
Cdd:PRK01156 320 EINKyhaiiKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLK-------SIESLKKKIEEYSKNIERMSAF 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1268 GQRCINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLRE 1347
Cdd:PRK01156 393 ISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIIN 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1348 QYEEE----QEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQR---LQETEEAVEAVNAKCSSLEKTK 1420
Cdd:PRK01156 473 HYNEKksrlEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESAradLEDIKIKINELKDKHDKYEEIK 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1421 HRLQN-EIEDL---------------MVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEarcLSTELF 1484
Cdd:PRK01156 553 NRYKSlKLEDLdskrtswlnalavisLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIRE---IENEAN 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1485 KLKNSYEEaldhLETMKRENKNLQEEISDLTEQLGEggksihelekmRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQ 1564
Cdd:PRK01156 630 NLNNKYNE----IQENKILIEKLRGKIDNYKKQIAE-----------IDSIIPDLKEITSRINDIEDNLKKSRKALDDAK 694
|
570 580 590
....*....|....*....|....*....|....*.
gi 163644331 1565 LEFSQIKADIErKLAEKDEEMEQSKRNLQRTIDTLQ 1600
Cdd:PRK01156 695 ANRARLESTIE-ILRTRINELSDRINDINETLESMK 729
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
982-1821 |
7.60e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 7.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 982 EEMAALDDIIAKLTKEK---KALQEAHQQTLDDLQSEEDkvnTLTKAKAKLEQQVDDLEGSL----------EQEKKLRM 1048
Cdd:PRK04863 279 NERRVHLEEALELRRELytsRRQLAAEQYRLVEMARELA---ELNEAESDLEQDYQAASDHLnlvqtalrqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1049 DLERAKRKLEGDL---KLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQarieeleeele 1125
Cdd:PRK04863 356 DLEELEERLEEQNevvEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE----------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1126 aeraaraKVEKQRADLARELEEISERLEEAggATAAQIEMNKKREAEfQKLRrDLEEATLQHEAtAATLRKKQADSVAEl 1205
Cdd:PRK04863 425 -------RAKQLCGLPDLTADNAEDWLEEF--QAKEQEATEELLSLE-QKLS-VAQAAHSQFEQ-AYQLVRKIAGEVSR- 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1206 geqiDNLQRVKQKLEKEKSELRLELddvvsnmEHVVKTKANLEKMTRSLEDQMNEYKTKYEEGQRCINDFTMQkSKLQSE 1285
Cdd:PRK04863 492 ----SEAWDVARELLRRLREQRHLA-------EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE-DELEQL 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1286 NGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETK-------AKSALAHaVQSARHDTDLLREQYEEEQEAKAE 1358
Cdd:PRK04863 560 QEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAArapawlaAQDALAR-LREQSGEEFEDSQDVTEYMQQLLE 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1359 LQRGMSKANSEVAqwrtkyetdaiQRTEELEEAKKKLAQ-------RLQETEEAVEAV---------------------- 1409
Cdd:PRK04863 639 RERELTVERDELA-----------ARKQALDEEIERLSQpggsedpRLNALAERFGGVllseiyddvsledapyfsalyg 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1410 NAKC----SSLEKTKHRLQNEiEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFeeSQAELESSQ--------KEAR 1477
Cdd:PRK04863 708 PARHaivvPDLSDAAEQLAGL-EDCPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKI--ADRQWRYSRfpevplfgRAAR 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1478 clstelfklknsyEEaldHLETmkrenknLQEEISDLTEQLGEGGKSIHELEKMRKQL----------------EQEKSE 1541
Cdd:PRK04863 785 -------------EK---RIEQ-------LRAEREELAERYATLSFDVQKLQRLHQAFsrfigshlavafeadpEAELRQ 841
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1542 IQSALEEAEASLEHEEGKILRAQLEFSQIK---------------------ADIERKLAEKDEEMEQSKRNLQR------ 1594
Cdd:PRK04863 842 LNRRRVELERALADHESQEQQQRSQLEQAKeglsalnrllprlnlladetlADRVEEIREQLDEAEEAKRFVQQhgnala 921
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1595 TIDTLQSSLESETrSRNEALRikkkmeGDLNEMEIQLSQANRQaAEAQKQLKSVHAHMKDAQLQlddslrtnEDLKENTA 1674
Cdd:PRK04863 922 QLEPIVSVLQSDP-EQFEQLK------QDYQQAQQTQRDAKQQ-AFALTEVVQRRAHFSYEDAA--------EMLAKNSD 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1675 IVERrnnlLQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLqteveeAVQECRNAE 1754
Cdd:PRK04863 986 LNEK----LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL------GVPADSGAE 1055
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163644331 1755 EKakkaitdAAMMAEELKKEQDTSahleRMKKN-MEQTIKDLQHRLDEAEQIAMKGGKKQVQKLEARV 1821
Cdd:PRK04863 1056 ER-------ARARRDELHARLSAN----RSRRNqLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVV 1112
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1045-1260 |
8.08e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1045 KLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIeeleeel 1124
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1125 eaeraarakvEKQRADLARELEEISERLEEA-------------GGATAAQIEMNKKREAEFQKLRRDLEEATLQHEATA 1191
Cdd:COG4942 93 ----------AELRAELEAQKEELAELLRALyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644331 1192 ATLRKKQADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNMEHVVKTKANLEKMTRSLEDQMNE 1260
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1667-1932 |
9.75e-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: 57.39 E-value: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1667 EDLKENTAIVERRNNLLQAELEELRAALE--QTERGRKLAEQELLDTSERVQLlhsqnTSLLNQKKKLETDISQLQTEVE 1744
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLErlRREREKAERYQALLKEKREYEG-----YELLKEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1745 EAVQEcrnaEEKAKKAITDAAMMAEELKKEQDTSAhlERMKKNMEQTIKDLQHRLDEAEqiamkggkKQVQKLEARVREL 1824
Cdd:TIGR02169 248 SLEEE----LEKLTEEISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGELE--------AEIASLERSIAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1825 ESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKAYKRAAEEAEEQANTNLSKFRKIQHE 1904
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
250 260
....*....|....*....|....*...
gi 163644331 1905 LDEAEERADIAESQVNKLRAKSRDVSSK 1932
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEE 421
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1621-1838 |
1.03e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1621 EGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEqtERG 1700
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1701 RKLAEQElLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEqdtsah 1780
Cdd:COG3883 93 RALYRSG-GSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE------ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 163644331 1781 LERMKKNMEQTIKDLQHRLDEAEQiamkggkkQVQKLEARVRELESEVESEQKKSSEA 1838
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSA--------EEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
835-1251 |
1.04e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 56.77 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 835 FFKIKPLLKSAE-----AEKEMANMKDEFAKLKEAYAKSEARRKELEEKMvsllqekNDLQLQVQAEQDNLCDAEErcdq 909
Cdd:PRK04778 100 FRKAKHEINEIEslldlIEEDIEQILEELQELLESEEKNREEVEQLKDLY-------RELRKSLLANRFSFGPALD---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 910 liknkiQLEAKAKELTERLEDEEEMNAE---LTAKK--RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN----L 980
Cdd:PRK04778 169 ------ELEKQLENLEEEFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 981 TEEMAALDDIiaKLTKEKKALQEAHQQTLDDLQSEEdkvntLTKAKAKLEQ---QVDDLEGSLEQEKKLRMDLERAKRKL 1057
Cdd:PRK04778 243 VEEGYHLDHL--DIEKEIQDLKEQIDENLALLEELD-----LDEAEEKNEEiqeRIDQLYDILEREVKARKYVEKNSDTL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1058 EGDLKLTQEslmdlENDKQQLE-ERLKKKdFEISqlngkiEDEQTICIQLQKKLKELQARIeeleeeleaeRAARAKVEK 1136
Cdd:PRK04778 316 PDFLEHAKE-----QNKELKEEiDRVKQS-YTLN------ESELESVRQLEKQLESLEKQY----------DEITERIAE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1137 QRA---DLARELEEISERLEEAGgatAAQIEMNKK----REAEfQKLRRDLEEATLQHEATAATLRKKQADSVAElgEQI 1209
Cdd:PRK04778 374 QEIaysELQEELEEILKQLEEIE---KEQEKLSEMlqglRKDE-LEAREKLERYRNKLHEIKRYLEKSNLPGLPE--DYL 447
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 163644331 1210 DNLQRVK---QKLEKEKSELRLELDDVVSNMEHVVKTKANLEKMT 1251
Cdd:PRK04778 448 EMFFEVSdeiEALAEELEEKPINMEAVNRLLEEATEDVETLEEET 492
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1503-1874 |
1.05e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 57.23 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1503 ENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQsaleeaeasleheegkilraqlefsQIKADIERKLAEKD 1582
Cdd:PRK11281 57 EDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLR-------------------------QAQAELEALKDDND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1583 EEMEQSKRNLqrTIDTLQSSLEsETRSrnealrikkkmegDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQ---LQL 1659
Cdd:PRK11281 112 EETRETLSTL--SLRQLESRLA-QTLD-------------QLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSqrlQQI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1660 DDSLRTNEDLKEntAIVERRNNLLQAELeelrAALE-QTERGRKLAE-----QELL-----DTSERVQLLHSQNTSL--- 1725
Cdd:PRK11281 176 RNLLKGGKVGGK--ALRPSQRVLLQAEQ----ALLNaQNDLQRKSLEgntqlQDLLqkqrdYLTARIQRLEHQLQLLqea 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1726 LNQKKKLETdisqlqtevEEAVQECRNAEEKAKkaITDAAMMAEELKKEQDTSAHL----ERMKKNMEQTIKdLQHRLDE 1801
Cdd:PRK11281 250 INSKRLTLS---------EKTVQEAQSQDEAAR--IQANPLVAQELEINLQLSQRLlkatEKLNTLTQQNLR-VKNWLDR 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 163644331 1802 AEQiAMKGGKKQVQKLEARVreLESEVESEQKKSSEAVKGIRKYERRIKEL-TYQTE--EDRKNLARLQDLVDKLQ 1874
Cdd:PRK11281 318 LTQ-SERNIKEQISVLKGSL--LLSRILYQQQQALPSADLIEGLADRIADLrLEQFEinQQRDALFQPDAYIDKLE 390
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1453-1658 |
1.36e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1453 KVLSEWKQKFEESQAEL--ESSQKEARCLSTELFKLKNSYEEALDHLETMKRENK--NLQEEISDLTEQLGEGGKSIHEL 1528
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1529 EKMRKQLEQEKSEIQSAL----EEAEASLEHEEGKILRAQLefsqikADIERKLAEK--------------DEEMEQSKR 1590
Cdd:COG3206 232 RAELAEAEARLAALRAQLgsgpDALPELLQSPVIQQLRAQL------AELEAELAELsarytpnhpdvialRAQIAALRA 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 163644331 1591 NLQRTIDTLQSSLESE---TRSRNEALR-----IKKKMEgDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQ 1658
Cdd:COG3206 306 QLQQEAQRILASLEAEleaLQAREASLQaqlaqLEARLA-ELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
857-1645 |
1.39e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 857 EFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQliKNKI-QLEAKAKELTERLEDEE--- 932
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQ--QEKIeRYQADLEELEERLEEQNevv 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 933 ----EMNAELTAKKRKLEDECSELKKDIDDL-------------------------------ELTLAKVEKEKHATENKV 977
Cdd:PRK04863 372 eeadEQQEENEARAEAAEEEVDELKSQLADYqqaldvqqtraiqyqqavqalerakqlcglpDLTADNAEDWLEEFQAKE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 978 KNLTEEMAAL-------DDIIAKLTKEKKALQ---------EAHQQTLDDLQSEEDKVNTLTKAKAkLEQQVDDLEGSLE 1041
Cdd:PRK04863 452 QEATEELLSLeqklsvaQAAHSQFEQAYQLVRkiagevsrsEAWDVARELLRRLREQRHLAEQLQQ-LRMRLSELEQRLR 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1042 QEKklrmDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLngkieDEQTicIQLQKKLKELQARIEELe 1121
Cdd:PRK04863 531 QQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEA-----RERR--MALRQQLEQLQARIQRL- 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1122 eeleaeraarakveKQRADLARELEEISERLEEAGGATAAQIEMnkkREAEFQKLRRDLEEATLQHEATAAtlRKKQads 1201
Cdd:PRK04863 599 --------------AARAPAWLAAQDALARLREQSGEEFEDSQD---VTEYMQQLLERERELTVERDELAA--RKQA--- 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1202 vaeLGEQIDNLQ--------RVKQKLEKEKSELRLEL-DD--------------------VVSNMEHVVKTKANLEKmtr 1252
Cdd:PRK04863 657 ---LDEEIERLSqpggsedpRLNALAERFGGVLLSEIyDDvsledapyfsalygparhaiVVPDLSDAAEQLAGLED--- 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1253 sledqmneyktkyeegqrCINDFTMQKSKLQS-ENGELSRQLEEKDSLVsQLTRSKMSYT--------------QQIEDL 1317
Cdd:PRK04863 731 ------------------CPEDLYLIEGDPDSfDDSVFSVEELEKAVVV-KIADRQWRYSrfpevplfgraareKRIEQL 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1318 KRQLEEETkaksalahavqsarhdtdllrEQYEEEQEAKAELQRGMSKANSEVA-------QWRTKYETDAI-QRTEELE 1389
Cdd:PRK04863 792 RAEREELA---------------------ERYATLSFDVQKLQRLHQAFSRFIGshlavafEADPEAELRQLnRRRVELE 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1390 EAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHR--------LQNEIEDLMVDLERSNAAAAALDKKQRNFDK------VL 1455
Cdd:PRK04863 851 RALADHESQEQQQRSQLEQAKEGLSALNRLLPRlnlladetLADRVEEIREQLDEAEEAKRFVQQHGNALAQlepivsVL 930
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1456 SEWKQKFEESQAELESSQKEARCLSTELFKLKN--------SYEEALDHLetmkrenknlqEEISDLTEQLGEggksihe 1527
Cdd:PRK04863 931 QSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfSYEDAAEML-----------AKNSDLNEKLRQ------- 992
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1528 lekMRKQLEQEKSEIQSALEEAEAslEHEEGKILRAQLEFS-----QIKADIERKLAE----KDEEMEQSKRnLQRtiDT 1598
Cdd:PRK04863 993 ---RLEQAEQERTRAREQLRQAQA--QLAQYNQVLASLKSSydakrQMLQELKQELQDlgvpADSGAEERAR-ARR--DE 1064
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 163644331 1599 LQSSLeSETRSRNEALRIKK-KMEGDLNEMEIQLSQANRQAAEAQKQL 1645
Cdd:PRK04863 1065 LHARL-SANRSRRNQLEKQLtFCEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1463-1874 |
1.50e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 56.75 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1463 EESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQL---GEGGKSIHELEKMRKQLeqek 1539
Cdd:pfam10174 112 ELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLqskGLPKKSGEEDWERTRRI---- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1540 SEIQSALEEAEASLEHEEGKIL----------RAQLEFSQIKA---DIERKLAeKDEEMEQSKRNLQRTIDTLQSSLESE 1606
Cdd:pfam10174 188 AEAEMQLGHLEVLLDQKEKENIhlreelhrrnQLQPDPAKTKAlqtVIEMKDT-KISSLERNIRDLEDEVQMLKTNGLLH 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1607 TRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAE 1686
Cdd:pfam10174 267 TEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1687 LEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSL---LNQKKK----LETDISQLQTEVEEAVQECRNAEEKAKK 1759
Cdd:pfam10174 347 VDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLkdmLDVKERkinvLQKKIENLQEQLRDKDKQLAGLKERVKS 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1760 AITDAAMMAEELKKEQDTSAHLERMKKNM-EQTIKDLQHRLDEAEQI--AMKGGKKQVQKLEARVRELESEVESEQKKSS 1836
Cdd:pfam10174 427 LQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLkkENKDLKEKVSALQPELTEKESSLIDLKEHAS 506
|
410 420 430
....*....|....*....|....*....|....*...
gi 163644331 1837 EAVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQ 1874
Cdd:pfam10174 507 SLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH 544
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1599-1838 |
1.55e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1599 LQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVER 1678
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1679 RNNLLQAELEELRAALEQTER-----GRK------LAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAV 1747
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRalyrlGRQpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1748 QECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQhrldeaeqiamkggkKQVQKLEARVRELESE 1827
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ---------------QEAEELEALIARLEAE 235
|
250
....*....|.
gi 163644331 1828 VESEQKKSSEA 1838
Cdd:COG4942 236 AAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1469-1882 |
1.64e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1469 LESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEE 1548
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1549 AEASLEHEEgkiLRAQLEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEAlrikkkMEGDLNEME 1628
Cdd:COG4717 128 LPLYQELEA---LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA------TEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1629 IQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLL------------------------- 1683
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1684 ------------------QAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEE 1745
Cdd:COG4717 279 lflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1746 AVQE---CRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAMKGGKKQvqkLEARVR 1822
Cdd:COG4717 359 LEEElqlEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE---LEEELE 435
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1823 ELESEVESEQKKSSEAVKGIRKYERRIKELTyQTEEDRKNLARLQDLVDKLQLKVKAYKR 1882
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLE-EDGELAELLQELEELKAELRELAEEWAA 494
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
827-1238 |
1.72e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 56.30 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 827 KNWPWMKLFFKIKPLLKSA-----EAEKEMANMKDEFAKLK-EAYAKSEARRKELEEKMVsllQEKNDLQLQVQAEQDNL 900
Cdd:pfam09731 28 KDDNFRDFFEEYIPYGEEVvlyalGEDPPLAPKPKTFRPLQpSVVSAVTGESKEPKEEKK---QVKIPRQSGVSSEVAEE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 901 cdAEERCDQLIKNKIQLEAKAKELTERLEdeeEMNAELTAKKRKLEDECSELKKDiddleltlakvekEKHATENKVKNL 980
Cdd:pfam09731 105 --EKEATKDAAEAKAQLPKSEQEKEKALE---EVLKEAISKAESATAVAKEAKDD-------------AIQAVKAHTDSL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 981 TEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEEDKVNTlTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGD 1060
Cdd:pfam09731 167 KEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEE-EAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1061 LKLTQESLMDLENDKQQLEERL--------KKKDFEISQLNGKIEDEQTICIQLQKKLKELQARieeleeeleAERAARA 1132
Cdd:pfam09731 246 DQYKELVASERIVFQQELVSIFpdiipvlkEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKR---------EEKHIER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1133 KVEKQRADLARELEEISERLEEAGGATAAQIEmnKKREAEFQKLRRDLEE---ATLQHEATAATLRKKQADSVAELGEQI 1209
Cdd:pfam09731 317 ALEKQKEELDKLAEELSARLEEVRAADEAQLR--LEFEREREEIRESYEEklrTELERQAEAHEEHLKDVLVEQEIELQR 394
|
410 420
....*....|....*....|....*....
gi 163644331 1210 DNLQRVKQKLEKEKSELRLELDDVVSNME 1238
Cdd:pfam09731 395 EFLQDIKEKVEEERAGRLLKLNELLANLK 423
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
653-677 |
2.03e-07 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 52.73 E-value: 2.03e-07
10 20
....*....|....*....|....*
gi 163644331 653 HRENLNKLMTNLRSTHPHFVRCIIP 677
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1043-1493 |
2.08e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1043 EKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKkkdfEISQLNGKIEDEQTICIQLQKKLKELQARIEE--L 1120
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKleK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1121 EEELEAERAARAKVEKQRADLARELEEISERLEEaggaTAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQAD 1200
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1201 SVAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNMEHvVKTKANLEKMTRSL-------------EDQMNEYKTKYEE 1267
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA-AALEERLKEARLLLliaaallallglgGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1268 GQRCINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLRE 1347
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1348 QYEE------EQEAKAELQRGMSKANSEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKcsSLEKTKH 1421
Cdd:COG4717 359 LEEElqleelEQEIAALLAEAGVEDEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELE 435
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 163644331 1422 RLQNEIEDLMVDLERSNAAAAALDKKQRNF--DKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEA 1493
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
947-1172 |
2.10e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 947 DECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQeahqqtlDDLQSEEDKVNTLTKAK 1026
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE-------QELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1027 AKLEQQVDDLEGSLeqeKKLRMDLERAKRKLEGDLKLTQESLMDL-----------ENDKQQLEErLKKKDFEISQLNGK 1095
Cdd:COG4942 93 AELRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAvrrlqylkylaPARREQAEE-LRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163644331 1096 IEDEQTiciQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATAAQIEMNKKREAE 1172
Cdd:COG4942 169 LEAERA---ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1387-1869 |
2.58e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.13 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1387 ELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTkhrlQNEIEDLMVDLERSNAAAAALDKKQRNFDKvlseWKQKFEESQ 1466
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKE----LKHLREALQQTQQSHAYLTQKREAQEEQLK----KQQLLKQLR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1467 AELESSQKEARCLS--TELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQ----LEQEKS 1540
Cdd:TIGR00618 267 ARIEELRAQEAVLEetQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQqssiEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1541 EIQSALEEAEASLEHEEGKILRAQleFSQIKADIERKLA-----EKDEEMEQSKRNLQRTIDTLQSSLESETRSRNeALR 1615
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEVATSIREI--SCQQHTLTQHIHTlqqqkTTLTQKLQSLCKELDILQREQATIDTRTSAFR-DLQ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1616 IKKKMEGDLNEMEIQLSQANRQAAEAQKQ-LKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNllqaelEELRAAL 1694
Cdd:TIGR00618 424 GQLAHAKKQQELQQRYAELCAAAITCTAQcEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKA------VVLARLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1695 EQTERGRKLAEQELLDTSERVQLLHSQNTS-----LLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAITDAAMMAE 1769
Cdd:TIGR00618 498 ELQEEPCPLCGSCIHPNPARQDIDNPGPLTrrmqrGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQ 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1770 elkKEQDTSAHLERMKkNMEQTIKDLQHRLDEAEQIAMKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKyERRI 1849
Cdd:TIGR00618 578 ---CDNRSKEDIPNLQ-NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAL-HALQ 652
|
490 500
....*....|....*....|
gi 163644331 1850 KELTYQTEEDRKNLARLQDL 1869
Cdd:TIGR00618 653 LTLTQERVREHALSIRVLPK 672
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1574-1804 |
2.76e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1574 IERKLAEKDEEMEQSKRNLQRTIDTLQSSLEsETRSRNEALRIKKKM---EGDLNEMEIQLSQANRQAAEAQKQLKSVHA 1650
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELE-EAEAALEEFRQKNGLvdlSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1651 HMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEelRAALEQTergrklaeqeLLDTSERVQLLHSQNTSLLNQkk 1730
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAE--LAELSAR----------YTPNHPDVIALRAQIAALRAQ-- 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 163644331 1731 kLETDISQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQ 1804
Cdd:COG3206 307 -LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1460-1853 |
3.63e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.90 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1460 QKFEESQAELESSQKEARCLSTELFKLKNSYEEaldHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEK 1539
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWERQRRELES---RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1540 SEIQSALEEAEASLEHEEGKILRAQLEFSQIKADIERKLAEKDEEmEQSKRNLQRTIDTLQS---SLESETRSRNEALRI 1616
Cdd:pfam07888 125 AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE-EAERKQLQAKLQQTEEelrSLSKEFQELRNSLAQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1617 KKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRaaLEQ 1696
Cdd:pfam07888 204 RDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQAR--LQA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1697 TERGRKLAEQELLDTSERVQLlhSQNTSLLNQKKKLETD-ISQLQTEV---EEAVQECRNAEEKAKKaitdaammaeELK 1772
Cdd:pfam07888 282 AQLTLQLADASLALREGRARW--AQERETLQQSAEADKDrIEKLSAELqrlEERLQEERMEREKLEV----------ELG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1773 KEQDTSahlermkknmeqtikdlqhrldeaeQIAMKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKEL 1852
Cdd:pfam07888 350 REKDCN-------------------------RVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETV 404
|
.
gi 163644331 1853 T 1853
Cdd:pfam07888 405 A 405
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
842-1081 |
3.83e-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: 55.46 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 842 LKSAEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERcdqliknKIQLEAKA 921
Cdd:TIGR02169 784 LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ-------IKSIEKEI 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 922 KELTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMaalddiiaKLTKEKKAL 1001
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL--------SELKAKLEA 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1002 QEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEER 1081
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
842-1079 |
4.67e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 842 LKSAEAEKEMANMKDEFAKLKEAYAKSEARRKE---------LEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLik 912
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL-- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 913 nKIQLEAKAKELTERLEDEEEmnaeltakkrkledecSELKKDIDDLELTLAkvEKEKHATEN--KVKNLTEEMAALddi 990
Cdd:COG3206 246 -RAQLGSGPDALPELLQSPVI----------------QQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL--- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 991 iakltkeKKALQEAHQQTLDDLQSEedkVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRklegDLKLTQESLMD 1070
Cdd:COG3206 304 -------RAQLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLER----EVEVARELYES 369
|
....*....
gi 163644331 1071 LENDKQQLE 1079
Cdd:COG3206 370 LLQRLEEAR 378
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1539-1932 |
4.97e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1539 KSEIQSALEEAEASLEHEEGKILRAQLefsqikADIERKLAEKDEEM---EQSKRNLQRTIDTLQSSLESETRSRNEALR 1615
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERL------NGLESELAELDEEIeryEEQREQARETRDEADEVLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1616 IK---KKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRA 1692
Cdd:PRK02224 256 LEaeiEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1693 ALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELK 1772
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1773 KEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAMKGgkkqvqkleaRVRELESEVESeqkksSEAVKGIRKYERRIKEL 1852
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEALLEAG----------KCPECGQPVEG-----SPHVETIEEDRERVEEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1853 TYQTEEDRKNLARLQDLVDKLQLKVKAykraaeeaEEQANTNLSKFRKIQHELDEAEERADIAESQVNKLRAKSRDVSSK 1932
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLVEA--------EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
853-1560 |
5.50e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.84 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 853 NMKDEFAKLKEAYAKsearRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIknkIQLEAKAKELTERLEDEE 932
Cdd:pfam12128 238 KIRPEFTKLQQEFNT----LESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLL---RTLDDQWKEKRDELNGEL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 933 EMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAT-ENKVKNLTEEMAALDDIIAKLTKEKKAL-QEAHQQTLD 1010
Cdd:pfam12128 311 SAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSwQSELENLEERLKALTGKHQDVTAKYNRRrSKIKEQNNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1011 DLQSEEDKVNTLTKAKAK-LEQQVDDLEGsleQEKKLRMDLERAKRKLE----------GDLKLTQESLM---DLENDKQ 1076
Cdd:pfam12128 391 DIAGIKDKLAKIREARDRqLAVAEDDLQA---LESELREQLEAGKLEFNeeeyrlksrlGELKLRLNQATatpELLLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1077 QLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEeleeeleaeraarakvekqraDLARELEEISERLEEAg 1156
Cdd:pfam12128 468 NFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALR---------------------QASRRLEERQSALDEL- 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1157 gataaqiemnkkreaefqKLRRDLEEATLQHeataaTLRKKQADSVAELGEQIDNLQRVKQKLEKEKSE----------- 1225
Cdd:pfam12128 526 ------------------ELQLFPQAGTLLH-----FLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDgsvggelnlyg 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1226 LRLELDDVVSNMEHvvktkanleKMTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTR 1305
Cdd:pfam12128 583 VKLDLKRIDVPEWA---------ASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARL 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1306 SKMSYTQQIEDLKRQLEEETKAKSALAhavQSARHDTDLLREQYEEEQEAKAELQRGMSKANSevaqwrtkyeTDAIQRT 1385
Cdd:pfam12128 654 DLRRLFDEKQSEKDKKNKALAERKDSA---NERLNSLEAQLKQLDKKHQAWLEEQKEQKREAR----------TEKQAYW 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1386 EELEEAKK-KLAQRLQETEEAVEAVNAKCSSLEKTKHR--------------LQNEIEDLMVDLER---SNAAAAALDKK 1447
Cdd:pfam12128 721 QVVEGALDaQLALLKAAIAARRSGAKAELKALETWYKRdlaslgvdpdviakLKREIRTLERKIERiavRRQEVLRYFDW 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1448 QR--------NFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQlG 1519
Cdd:pfam12128 801 YQetwlqrrpRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKED-A 879
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 163644331 1520 EGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKI 1560
Cdd:pfam12128 880 NSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVI 920
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1065-1653 |
5.59e-07 |
|
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: 54.75 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1065 QESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIeeleeeleaeraarakvekqradlare 1144
Cdd:pfam05557 5 IESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRI--------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1145 lEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEEATLQhEATAATLRKKQADSVAELGEQIDNLQRVKQKLEKEKS 1224
Cdd:pfam05557 58 -RLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQ-LADAREVISCLKNELSELRRQIQRAELELQSTNSELE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1225 ELRLELDDVVSNMEHVVKTKANLEKMTRSLEDQMNEYKTkyeegqrcindftmqkskLQSENgelsrQLEEKDSLVSQLT 1304
Cdd:pfam05557 136 ELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKE------------------LEFEI-----QSQEQDSEIVKNS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1305 RSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLR---EQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDA 1381
Cdd:pfam05557 193 KSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKrklEREEKYREEAATLELEKEKLEQELQSWVKLAQDTG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1382 --IQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNE-------IEDLMVDLERSNAAAAALDK------ 1446
Cdd:pfam05557 273 lnLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQElaqylkkIEDLNKKLKRHKALVRRLQRrvlllt 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1447 KQRNFDKVLSEwkqKFEESQAELESSQKEARCLstelfklknsyEEALDHLETMKRENKNLQEEISDLTEQLGeggksih 1526
Cdd:pfam05557 353 KERDGYRAILE---SYDKELTMSNYSPQLLERI-----------EEAEDMTQKMQAHNEEMEAQLSVAEEELG------- 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1527 ELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEfsQIKADIERKLAEKDE-EMEQSKRNLQRTIDTLQS---- 1601
Cdd:pfam05557 412 GYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLE--TLELERQRLREQKNElEMELERRCLQGDYDPKKTkvlh 489
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 163644331 1602 -----SLESETRSRNEA----------LRIKKKMEGDLNEM----EIQLSQANRQAAEAQKQLKSVHAHMK 1653
Cdd:pfam05557 490 lsmnpAAEAYQQRKNQLeklqaeierlKRLLKKLEDDLEQVlrlpETTSTMNFKEVLDLRKELESAELKNQ 560
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1631-1882 |
6.49e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1631 LSQANRQAAEAQKQLKSVHAHMKDAQLQLDDslrtnedlkentaiVERRNNLLQAELEELRAALEQTERGRKLAEQELLD 1710
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAA--------------LKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1711 TSERVQLLHSQNTSLLNQKKKLETDISQLqteVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ 1790
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1791 TIKDLQHRLDEAEQiAMKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELtyqteedRKNLARLQDLV 1870
Cdd:COG4942 158 DLAELAALRAELEA-ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL-------QQEAEELEALI 229
|
250
....*....|..
gi 163644331 1871 DKLQLKVKAYKR 1882
Cdd:COG4942 230 ARLEAEAAAAAE 241
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1486-1851 |
7.72e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.07 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1486 LKNSYEEALDHLETMKRE--NKNLQEEISDLtEQLGEGGKSIHELEKMRKQLEQEKS----EIQSALEEAEASLE----- 1554
Cdd:PRK04778 23 LRKRNYKRIDELEERKQEleNLPVNDELEKV-KKLNLTGQSEEKFEEWRQKWDEIVTnslpDIEEQLFEAEELNDkfrfr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1555 --HEEGKILRAQLEfsQIKADIERKLAEKDEEMEQSKRNLQR------TIDTLQSSLESETRSRNEALrikKKMEGDLNE 1626
Cdd:PRK04778 102 kaKHEINEIESLLD--LIEEDIEQILEELQELLESEEKNREEveqlkdLYRELRKSLLANRFSFGPAL---DELEKQLEN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1627 MEIQLSQANRQAA-----EAQKQLKSVHAHMKDaqlqlddslrTNEDLKENTAIVERRNNLLQAELEELRAALEQ-TERG 1700
Cdd:PRK04778 177 LEEEFSQFVELTEsgdyvEAREILDQLEEELAA----------LEQIMEEIPELLKELQTELPDQLQELKAGYRElVEEG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1701 RKLAEQELLDTSERVQLLHSQNTSLL---------NQKKKLETDI----SQLQTEVEeavqeCRNAEEKAKKAITDAAMM 1767
Cdd:PRK04778 247 YHLDHLDIEKEIQDLKEQIDENLALLeeldldeaeEKNEEIQERIdqlyDILEREVK-----ARKYVEKNSDTLPDFLEH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1768 AEELKKEqdTSAHLERMKKN-------------MEQTIKDLQHRLDEAEQiAMKGGKKQVQKLEARVRELE---SEVESE 1831
Cdd:PRK04778 322 AKEQNKE--LKEEIDRVKQSytlneselesvrqLEKQLESLEKQYDEITE-RIAEQEIAYSELQEELEEILkqlEEIEKE 398
|
410 420
....*....|....*....|
gi 163644331 1832 QKKSSEAVKGIRKYERRIKE 1851
Cdd:PRK04778 399 QEKLSEMLQGLRKDELEARE 418
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1093-1429 |
9.53e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.97 E-value: 9.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1093 NGKIEDEQTICIQLQKKLKElQARIEELEEELEAERAARAKVEKQRADLARELEEiSERLEEAGGATAAQIEMNKKREAE 1172
Cdd:pfam17380 261 NGQTMTENEFLNQLLHIVQH-QKAVSERQQQEKFEKMEQERLRQEKEEKAREVER-RRKLEEAEKARQAEMDRQAAIYAE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1173 FQKL--RRDLEEATLQHEATAATLRKKQADSVAELGEQIDNLQRVKQKLEKEKSELRLELddvvsnmEHVVKTKANLEKM 1250
Cdd:pfam17380 339 QERMamERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQEL-------EAARKVKILEEER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1251 TRSLEDQMNEyktkyeegqrcindftMQKSKLQSENG---ELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKA 1327
Cdd:pfam17380 412 QRKIQQQKVE----------------MEQIRAEQEEArqrEVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRK 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1328 KSALAHAVQSARHDTDLLREQYEEEQEAKAE-----------LQRGMSKANSEVAQWRTKYETDAIQRTE-ELEEAKKKL 1395
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKILEKELEERKQamieeerkrklLEKEMEERQKAIYEEERRREAEEERRKQqEMEERRRIQ 555
|
330 340 350
....*....|....*....|....*....|....
gi 163644331 1396 AQRLQETEEaveavNAKCSSLEKTKHRLQNEIED 1429
Cdd:pfam17380 556 EQMRKATEE-----RSRLEAMEREREMMRQIVES 584
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1013-1236 |
1.02e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1013 QSEEDKVNTLTKAKAKLEQQVDDLEGSLEQ-EKKlrmdLERAKRK-----LEGDLKLTQESLMDLENDKQQLEERLKKKD 1086
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEaEAA----LEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1087 FEISQLNGKIED---------EQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEagg 1157
Cdd:COG3206 240 ARLAALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA--- 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644331 1158 ATAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRkkqadsvaELGEQIDNLQRVKQKLEKEKSELRLELDDVVSN 1236
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAELR--------RLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
869-1396 |
1.07e-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: 54.07 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 869 EARRKELEEKMVSLLQEKNDLQLQVQAE-QDNLCDAEERCDQLIKNKIQLEAKAKELTERLEdeEEMNAELTAKKRKLED 947
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALE--SELREQLEAGKLEFNE 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 948 ECSELKKDIDDLELTLAKVEKEKHATENK------VKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEEDKVNT 1021
Cdd:pfam12128 438 EEYRLKSRLGELKLRLNQATATPELLLQLenfderIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEE 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1022 LTKAKAKLEQQVDDLEGSL-------------------EQEKKLRMDLERAKRKLEGDLKLTQESL-MDLE----NDKQQ 1077
Cdd:pfam12128 518 RQSALDELELQLFPQAGTLlhflrkeapdweqsigkviSPELLHRTDLDPEVWDGSVGGELNLYGVkLDLKridvPEWAA 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1078 LEERLKKKdfeISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGG 1157
Cdd:pfam12128 598 SEEELRER---LDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALA 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1158 ATAAQIEMN-KKREAEFQKLRRDLEEATLQHEATAATLR-KKQADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDVVS 1235
Cdd:pfam12128 675 ERKDSANERlNSLEAQLKQLDKKHQAWLEEQKEQKREARtEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALET 754
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1236 NM-----------EHVVKTKANLEKMTRSLED-QMNEYK-TKYEEGQRciNDFTMQKSKLQSENGELSRQLEEkdsLVSQ 1302
Cdd:pfam12128 755 WYkrdlaslgvdpDVIAKLKREIRTLERKIERiAVRRQEvLRYFDWYQ--ETWLQRRPRLATQLSNIERAISE---LQQQ 829
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1303 LTRskmsytqQIEDLKR---QLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAK--AELQRGMSKANSEVAQWRTKY 1377
Cdd:pfam12128 830 LAR-------LIADTKLrraKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDAnsEQAQGSIGERLAQLEDLKLKR 902
|
570
....*....|....*....
gi 163644331 1378 ETDAIQRTEELEEAKKKLA 1396
Cdd:pfam12128 903 DYLSESVKKYVEHFKNVIA 921
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1502-1916 |
1.39e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1502 RENKNLQEEISDLTEQLGEggksIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEgkILRAQLEFSQIKADIERKLAEK 1581
Cdd:COG4717 71 KELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLE--KLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1582 DEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDD 1661
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1662 SLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQT 1741
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1742 EVEEAVQECRNAEEKAKKAItdaammAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiamkggKKQVQKLEARV 1821
Cdd:COG4717 305 EELQALPALEELEEEELEEL------LAALGLPPDLSPEELLELLDRIEELQELLREAEELEE------ELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1822 REL--ESEVESEQK--KSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKA--YKRAAEEAEEQANTNL 1895
Cdd:COG4717 373 AALlaEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELeeLEEELEELEEELEELR 452
|
410 420
....*....|....*....|.
gi 163644331 1896 SKFRKIQHELDEAEERADIAE 1916
Cdd:COG4717 453 EELAELEAELEQLEEDGELAE 473
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
843-1202 |
1.79e-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: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 843 KSAEAEKEMANMKDEFAKLKEAYAKSEARRKEleekmVSLLQEKNDLQLQ----VQAEQDNLCDAEERCDQLiknKIQLE 918
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQEKERAIEATNAE-----ITKLRSRVDLKLQelqhLKNEGDHLRNVQTECEAL---KLQMA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 919 AKAKE---LTERLEDEEEMNAELTAKKRKLEDECSELKKDIDD--LELTLAKVEKEKHAT-----ENKVKNLTEEMAALD 988
Cdd:pfam15921 559 EKDKVieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDrrLELQEFKILKDKKDAkirelEARVSDLELEKVKLV 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 989 DIIAKLTKEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQE-KKLRMDLERAKRKLEGdlklTQES 1067
Cdd:pfam15921 639 NAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTtNKLKMQLKSAQSELEQ----TRNT 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1068 LMDLENDKQQLEERLKKKDFEISQLNGKIEdeqticiqlqkklkELQARIEELEEELEAERAARAKVEKQRADLARELEE 1147
Cdd:pfam15921 715 LKSMEGSDGHAMKVAMGMQKQITAKRGQID--------------ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELST 780
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 163644331 1148 ISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQADSV 1202
Cdd:pfam15921 781 VATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESV 835
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1186-1869 |
1.86e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 53.27 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1186 QHEATAATLRK--KQADSVAELG-EQIDNLQRVKQKLEKEksELRLELDDVVSNMEHVVKTKANlekmtrSLEDQMNEYK 1262
Cdd:PRK10246 192 QHKSARTELEKlqAQASGVALLTpEQVQSLTASLQVLTDE--EKQLLTAQQQQQQSLNWLTRLD------ELQQEASRRQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1263 TKYEEGQRCINDFTMQKSKLqsENGELSRQL----EEKDSLVSQLTRSKmsytQQIEDLKRQLEEETKAKSALAHAVQSA 1338
Cdd:PRK10246 264 QALQQALAAEEKAQPQLAAL--SLAQPARQLrphwERIQEQSAALAHTR----QQIEEVNTRLQSTMALRARIRHHAAKQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1339 RhdtdllREQYEEEQEAKAELQR--GMSKANSEVAQWR---TKYETDAIQR---TEELEEAKKKLAQ----RLQETEEAV 1406
Cdd:PRK10246 338 S------AELQAQQQSLNTWLAEhdRFRQWNNELAGWRaqfSQQTSDREQLrqwQQQLTHAEQKLNAlpaiTLTLTADEV 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1407 EAVNAKCSSLEKTKHRL---QNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELES----SQKEARCL 1479
Cdd:PRK10246 412 AAALAQHAEQRPLRQRLvalHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADvktiCEQEARIK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1480 STELFK----------LKNSYE----EALDHLE--TMKRENKNLQEEISDLTEqlgEGGKSIHELEKMRKQLEQEKSEIQ 1543
Cdd:PRK10246 492 DLEAQRaqlqagqpcpLCGSTShpavEAYQALEpgVNQSRLDALEKEVKKLGE---EGAALRGQLDALTKQLQRDESEAQ 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1544 SALEEAEASLEHEEGKILRAQLEFsQIKADIERKLAEKDEEMEQSKRNLQRtidtlqsslesetrsrnealrikkkmegd 1623
Cdd:PRK10246 569 SLRQEEQALTQQWQAVCASLNITL-QPQDDIQPWLDAQEEHERQLRLLSQR----------------------------- 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1624 lNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDlkENTAIVER------------RNNLLQAELEELR 1691
Cdd:PRK10246 619 -HELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDE--EASWLATRqqeaqswqqrqnELTALQNRIQQLT 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1692 AALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEK---AKKAITDAAMMA 1768
Cdd:PRK10246 696 PLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQAsvfDDQQAFLAALLD 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1769 EElkkeqdTSAHLERMKKNMEQTIKDLQHRLDEAEQiamkggkKQVQKLEARVRELE--SEVESEQKKSSEAVKGIRKYE 1846
Cdd:PRK10246 776 EE------TLTQLEQLKQNLENQRQQAQTLVTQTAQ-------ALAQHQQHRPDGLDltVTVEQIQQELAQLAQQLRENT 842
|
730 740
....*....|....*....|...
gi 163644331 1847 RRIKELTYQTEEDRKNLARLQDL 1869
Cdd:PRK10246 843 TRQGEIRQQLKQDADNRQQQQAL 865
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
936-1162 |
3.04e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 936 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQ-- 1013
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1014 -SEEDKVNTLTKAK--AKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKkkdfeis 1090
Cdd:COG3883 99 gGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA------- 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 163644331 1091 QLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATAAQ 1162
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
870-1087 |
3.52e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.94 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 870 ARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEErcdqliKNKIQLEAKAKELTERLEDEEEMNAELTakkrKLEDEC 949
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRK------KNGENIARKQNKYDELVEEAKTIKAEIE----ELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 950 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAL----------------DDIIAKLTKEKKALQ---EAHQQTLD 1010
Cdd:PHA02562 244 LNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYekggvcptctqqisegPDRITKIKDKLKELQhslEKLDTAID 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1011 DLQSEEDKVNTLTKA----KAKLEQQVDDLEGSLEQEKKLRMDLERAKRKL---EGDLKLTQESLMDLENDKQQLEerlK 1083
Cdd:PHA02562 324 ELEEIMDEFNEQSKKllelKNKISTNKQSLITLVDKAKKVKAAIEELQAEFvdnAEELAKLQDELDKIVKTKSELV---K 400
|
....
gi 163644331 1084 KKDF 1087
Cdd:PHA02562 401 EKYH 404
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
846-1470 |
3.89e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 846 EAEKEMANMKDEFAKLKEAYAKSE-ARRK--------ELEEKMVSLLQEKNDLQ-----LQVQAEQDNLCDAEERCDQLI 911
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEdAREQiellepirELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 912 KNKIQLEAKAKELTERLEDEEEMNAELTAKKRKLE-DECSELKKDIDDLELTLAKVEKEKHATENKVKNL----TEEMAA 986
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALglplPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 987 LDDIIAKLTKEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGsleqeKKLRMD--LERAKRKLEGDLKLT 1064
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER-----RKSNIParLLALRDALAEALGLD 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1065 QES------LMDLENDKQQLE---ERL----------KKKDFeiSQLNGKIEDEQticiqlqkklkeLQARIEELEEELE 1125
Cdd:COG4913 457 EAElpfvgeLIEVRPEEERWRgaiERVlggfaltllvPPEHY--AAALRWVNRLH------------LRGRLVYERVRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1126 AERAARAKVEKQRadLARELE----EISERLEE--AGGATAAQIEmnkkREAEFQKLRRDL-EEATLQHEATAATL-RKK 1197
Cdd:COG4913 523 LPDPERPRLDPDS--LAGKLDfkphPFRAWLEAelGRRFDYVCVD----SPEELRRHPRAItRAGQVKGNGTRHEKdDRR 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1198 QADSVAELG----EQIDNLQRVKQKLEKEKSELRLELDDVVSNMEHVVKTKANLEKMTRSLEDQMNeyktkYEEGQRCIN 1273
Cdd:COG4913 597 RIRSRYVLGfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-----VASAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1274 DFTMQKSKLQSENGELS---RQLEEKDslvsqltrskmsytQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYE 1350
Cdd:COG4913 672 ELEAELERLDASSDDLAaleEQLEELE--------------AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1351 EEQEAKAELQRgmskanSEVAQWRTKYETDAIQRT--EELEEAKKKLAQRLQETEEAVEAVnakcssLEKTKHRLQNEIE 1428
Cdd:COG4913 738 AAEDLARLELR------ALLEERFAAALGDAVERElrENLEERIDALRARLNRAEEELERA------MRAFNREWPAETA 805
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 163644331 1429 DLMVDLERSNAAAAALDKKQRNfdkVLSEWKQKFEESQAELE 1470
Cdd:COG4913 806 DLDADLESLPEYLALLDRLEED---GLPEYEERFKELLNENS 844
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1427-1925 |
3.93e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.21 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1427 IEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKL------KNSYEEALDHLETM 1500
Cdd:PRK01156 185 IDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELssledmKNRYESEIKTAESD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1501 KRENKNLQEEISDLTEQLGEGGKS---------------IHELEKMRKQLEQEKSEIQSaLEEAEASLEHEEGKilRAQL 1565
Cdd:PRK01156 265 LSMELEKNNYYKELEERHMKIINDpvyknrnyindyfkyKNDIENKKQILSNIDAEINK-YHAIIKKLSVLQKD--YNDY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1566 EFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESEtrsRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQL 1645
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEY---SKNIERMSAFISEILKIQEIDPDAIKKELNEINVKL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1646 KSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRN------------------NLLQAELEELRAALEQTERGRKLAEQE 1707
Cdd:PRK01156 419 QDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeeksnhiiNHYNEKKSRLEEKIREIEIEVKDIDEK 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1708 LLDTSERVQLLHSQNTS-LLNQKKKLETDISQLqTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSaHLERMKK 1786
Cdd:PRK01156 499 IVDLKKRKEYLESEEINkSINEYNKIESARADL-EDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTS-WLNALAV 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1787 NMEQTIKDLQHRLDEAeqiamkggKKQVQKLEARVRELESEVESEQKKsseavkgIRKYERRIKELTYQTEEDRKNLARL 1866
Cdd:PRK01156 577 ISLIDIETNRSRSNEI--------KKQLNDLESRLQEIEIGFPDDKSY-------IDKSIREIENEANNLNNKYNEIQEN 641
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 163644331 1867 QDLVDKLQLKVKAYKRAAEEA---EEQANTNLSKFRKIQHELDEAEERADIAESQVNKLRAK 1925
Cdd:PRK01156 642 KILIEKLRGKIDNYKKQIAEIdsiIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLEST 703
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1389-1642 |
4.16e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1389 EEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKqrnfdkvLSEWKQKFEESQAE 1468
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE-------IAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1469 LE----SSQKEARCLSTELFKLK-NSYEEALDHLETMKRENKNLQEEISDLTEQlgeggksihelekmRKQLEQEKSEIQ 1543
Cdd:COG3883 88 LGerarALYRSGGSVSYLDVLLGsESFSDFLDRLSALSKIADADADLLEELKAD--------------KAELEAKKAELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1544 SALEEAEAsleheegkiLRAQLEfsQIKADIERKLAEKDEEMEQskrnLQRTIDTLQSSLESETRSRNEALRIKKKMEGD 1623
Cdd:COG3883 154 AKLAELEA---------LKAELE--AAKAELEAQQAEQEALLAQ----LSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
250
....*....|....*....
gi 163644331 1624 LNEMEIQLSQANRQAAEAQ 1642
Cdd:COG3883 219 AAAAAAAAAAAAAAAAAAA 237
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
983-1155 |
4.67e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 983 EMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLrmdLERAKRKLegDLK 1062
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---IKKYEEQL--GNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1063 LTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIeeleeeleaeRAARAKVEKQRADLA 1142
Cdd:COG1579 86 RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL----------EEKKAELDEELAELE 155
|
170
....*....|...
gi 163644331 1143 RELEEISERLEEA 1155
Cdd:COG1579 156 AELEELEAEREEL 168
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
853-1035 |
4.85e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 853 NMKDEFAKLKEaYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAKELTERLE-DE 931
Cdd:COG1579 1 AMPEDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 932 EEMNAELTAKkrkledECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDD 1011
Cdd:COG1579 80 EQLGNVRNNK------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|....
gi 163644331 1012 LQSEEDKvntLTKAKAKLEQQVDD 1035
Cdd:COG1579 154 LEAELEE---LEAEREELAAKIPP 174
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1294-1582 |
5.76e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 51.47 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1294 EEKDSLVSQLTRSKMSytqQIEDLKRQLEEETKAKsalahavqsarhdtdlLREQYEEEQEAKAELQRGMSKANSEVaqw 1373
Cdd:PRK05771 16 SYKDEVLEALHELGVV---HIEDLKEELSNERLRK----------------LRSLLTKLSEALDKLRSYLPKLNPLR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1374 rtkyETDAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLM------VDLER----SNAAAAA 1443
Cdd:PRK05771 74 ----EEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdLDLSLllgfKYVSVFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1444 LDKKQRNFDKVLSEWKQKFEEsqaELESSQKEARCLsteLFKLKNSYEEALDHLetmkRENKNLQEEISdlteqlgEGGK 1523
Cdd:PRK05771 150 GTVPEDKLEELKLESDVENVE---YISTDKGYVYVV---VVVLKELSDEVEEEL----KKLGFERLELE-------EEGT 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 163644331 1524 SIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQI--KADIERKLAEKD 1582
Cdd:PRK05771 213 PSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIEleRAEALSKFLKTD 273
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1682-1932 |
5.96e-06 |
|
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: 51.60 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1682 LLQAELEELRAALEQ-------TERgRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLetdisQLQTEVEEAVQECRNAE 1754
Cdd:TIGR02168 149 IIEAKPEERRAIFEEaagiskyKER-RKETERKLERTRENLDRLEDILNELERQLKSL-----ERQAEKAERYKELKAEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1755 EKAKKAItdAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHRLDEAEQiamkggkkQVQKLEARVRELESEVESEQKK 1834
Cdd:TIGR02168 223 RELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEELRLEVSELEEEIEELQKE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1835 SSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKAYKRAAEEAEEQANTNLSKFRKIQHELDEAEERADI 1914
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
250
....*....|....*...
gi 163644331 1915 AESQVNKLRAKSRDVSSK 1932
Cdd:TIGR02168 370 LESRLEELEEQLETLRSK 387
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1003-1187 |
6.27e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1003 EAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRM-------DLERAKRKLEGDLKLTQEslmDLENDK 1075
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEaakteleDLEKEIKRLELEIEEVEA---RIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1076 QQLEERLKKKDFEisQLNGKIEdeqticiQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEA 1155
Cdd:COG1579 80 EQLGNVRNNKEYE--ALQKEIE-------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180 190
....*....|....*....|....*....|..
gi 163644331 1156 GGATAAQIEmnkKREAEFQKLRRDLEEATLQH 1187
Cdd:COG1579 151 LAELEAELE---ELEAEREELAAKIPPELLAL 179
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
842-1337 |
6.89e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 6.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 842 LKSAEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQ---VQAEQDNLCDAEERCDQLiKNKIQLE 918
Cdd:TIGR00618 442 LCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVlarLLELQEEPCPLCGSCIHP-NPARQDI 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 919 AKAKELTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEK 998
Cdd:TIGR00618 521 DNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 999 KALQEAHQQTLDDLQSEEdkvntltkakAKLEQQVDDLEGSLEQEKKlrmdlerakrklegdlkltQESLMDLENDKQQL 1078
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALL----------RKLQPEQDLQDVRLHLQQC-------------------SQELALKLTALHAL 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1079 EERLKKKDFEISQLNGKiEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRA---DLARELEEISERLEEA 1155
Cdd:TIGR00618 652 QLTLTQERVREHALSIR-VLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELEThieEYDREFNEIENASSSL 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1156 GGATAAQIEMNKKREAEFQKLRRD-LEEATLQH-----EATAATLR-KKQADSVAELGEQIDNLQRVKQKLEKEKSELRL 1228
Cdd:TIGR00618 731 GSDLAAREDALNQSLKELMHQARTvLKARTEAHfnnneEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQ 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1229 ELDD----VVSNMEHVVKTKANLEKMTRSLEDQMNEYKTKYEEGQRCINDFTmQKSKLQSENGELSRQLEEKDSLVSQLt 1304
Cdd:TIGR00618 811 EIPSdediLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA-QLTQEQAKIIQLSDKLNGINQIKIQF- 888
|
490 500 510
....*....|....*....|....*....|...
gi 163644331 1305 rskmsytqqIEDLKRQLEEETKAKSALAHAVQS 1337
Cdd:TIGR00618 889 ---------DGDALIKFLHEITLYANVRLANQS 912
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1312-1600 |
7.20e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.49 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1312 QQIEDLKRQLEEETKAKSALAHAVQSA-----------RHDTDLLREQYE-EEQEAKAELQRGMSKansEVAQWRTKYET 1379
Cdd:COG3096 306 YRLVEMARELEELSARESDLEQDYQAAsdhlnlvqtalRQQEKIERYQEDlEELTERLEEQEEVVE---EAAEQLAEAEA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1380 DAIQRTEELEEAKKKLA--------------------QRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDL---MVDLER 1436
Cdd:COG3096 383 RLEAAEEEVDSLKSQLAdyqqaldvqqtraiqyqqavQALEKARALCGLPDLTPENAEDYLAAFRAKEQQAteeVLELEQ 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1437 ----SNAAAAALDK-------------KQRNFDK---VLSEWK---------QKFEESQAELE---SSQKEARCLSTELF 1484
Cdd:COG3096 463 klsvADAARRQFEKayelvckiageveRSQAWQTareLLRRYRsqqalaqrlQQLRAQLAELEqrlRQQQNAERLLEEFC 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1485 KLKNSYEEALDHLETMKREnknLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQS------ALEEAEASLEHEEG 1558
Cdd:COG3096 543 QRIGQQLDAAEELEELLAE---LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArapawlAAQDALERLREQSG 619
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 163644331 1559 KIL---RAQLEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQ 1600
Cdd:COG3096 620 EALadsQEVTAAMQQLLEREREATVERDELAARKQALESQIERLS 664
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1327-1477 |
7.77e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1327 AKSALAHAVQSARHDTDLLREqyEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRlqeteeaV 1406
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK-------E 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 163644331 1407 EAVNAKCSSLEKTKHRLQNEIEDlmvdlersnaaaaaLDKKQRNFDKVLSEWKQKFEESQAELES----SQKEAR 1477
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKE--------------LEQKQQELEKKEEELEELIEEQLQELERisglTAEEAK 156
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1386-1829 |
8.37e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.60 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1386 EELEEAKKKLAQ-RLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEE 1464
Cdd:PRK04778 86 EQLFEAEELNDKfRFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1465 SQAELESSQKEARCLSTELFKLKNS--YEEALDHLETMKRENKNLQEEISDLTEQLgeggksiHELEK-MRKQLEQEKSE 1541
Cdd:PRK04778 166 ALDELEKQLENLEEEFSQFVELTESgdYVEAREILDQLEEELAALEQIMEEIPELL-------KELQTeLPDQLQELKAG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1542 IQsALEEAEASLEHE--EGKILRAQLEFSQIKADIER-KLAEKDEEMEQskrnLQRTIDTLQSSLESETRSRNEalrIKK 1618
Cdd:PRK04778 239 YR-ELVEEGYHLDHLdiEKEIQDLKEQIDENLALLEElDLDEAEEKNEE----IQERIDQLYDILEREVKARKY---VEK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1619 KMEgdlnEMEIQLSQANRQAAEAQKQLksvhahmkdaqLQLDDSLRTNEDLKENTaiverrnNLLQAELEELRAALEQTE 1698
Cdd:PRK04778 311 NSD----TLPDFLEHAKEQNKELKEEI-----------DRVKQSYTLNESELESV-------RQLEKQLESLEKQYDEIT 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1699 rgRKLAEQElldtservqLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAItdaammaEELKKE-QDT 1777
Cdd:PRK04778 369 --ERIAEQE---------IAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKL-------ERYRNKlHEI 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 163644331 1778 SAHLER------------MKKNMEQTIKDLQHRLDEAeQIAMKGGKKQVQKLEARVRELESEVE 1829
Cdd:PRK04778 431 KRYLEKsnlpglpedyleMFFEVSDEIEALAEELEEK-PINMEAVNRLLEEATEDVETLEEETE 493
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
845-1000 |
9.30e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 845 AEAEKEMANMKDEfaKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLcdaEERCDQLIKNKIQLEAKAKEL 924
Cdd:PRK12704 45 EEAKKEAEAIKKE--ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENL---DRKLELLEKREEELEKKEKEL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 925 TERLEDEEEMNAELTAKKRKLEDE---CSELKKDiDDLELTLAKVEKE-KHATENKVKNLTEEmaalddiiAKLTKEKKA 1000
Cdd:PRK12704 120 EQKQQELEKKEEELEELIEEQLQElerISGLTAE-EAKEILLEKVEEEaRHEAAVLIKEIEEE--------AKEEADKKA 190
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
911-1179 |
1.24e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 50.31 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 911 IKNKIQLEAKAKELTERLEDEeeMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEkhatenkVKNLTEEMAALDDI 990
Cdd:PRK05771 45 LRKLRSLLTKLSEALDKLRSY--LPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKE-------IKELEEEISELENE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 991 IAKLTKEKKALQ--EAHQQTLDDLQSEED---KVNTLTKAKAKLEQQVDDLEGSLEqekklrmdlerAKRKLEGDLKLtq 1065
Cdd:PRK05771 116 IKELEQEIERLEpwGNFDLDLSLLLGFKYvsvFVGTVPEDKLEELKLESDVENVEY-----------ISTDKGYVYVV-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1066 esLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTIcIQLQKKLKELqarieeleeeleaeraarakvEKQRADLAREL 1145
Cdd:PRK05771 183 --VVVLKELSDEVEEELKKLGFERLELEEEGTPSELI-REIKEELEEI---------------------EKERESLLEEL 238
|
250 260 270
....*....|....*....|....*....|....
gi 163644331 1146 EEISERLEEAGGATAAQIEMNKKREAEFQKLRRD 1179
Cdd:PRK05771 239 KELAKKYLEELLALYEYLEIELERAEALSKFLKT 272
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
845-1004 |
1.25e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 845 AEAEKEMANMKDEFAKLKeayAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEER-------CDQLIKNKIQL 917
Cdd:COG4942 79 AALEAELAELEKEIAELR---AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRlqylkylAPARREQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 918 EAKAKELTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKE 997
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....*..
gi 163644331 998 KKALQEA 1004
Cdd:COG4942 236 AAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1658-1934 |
1.26e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1658 QLDDSLRTNEDLKENtaiVERRNNLLQAELEELRAALEQTERGRKlaeqELLDTSERVQLLHSQNTSLLNQKKKLETDIS 1737
Cdd:PRK03918 190 NIEELIKEKEKELEE---VLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSKRKLEEKIR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1738 QLQTEVEEAVQECRNAEEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQtikdlqhrldeaeqiamkgGKKQVQKL 1817
Cdd:PRK03918 263 ELEERIEELKKEIEELEEKVKEL--------KELKEKAEEYIKLSEFYEEYLD-------------------ELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1818 EARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKAYKRAAEEAEEqantnlsk 1897
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE-------- 387
|
250 260 270
....*....|....*....|....*....|....*..
gi 163644331 1898 frKIQHELDEAEERADIAESQVNKLRAKSRDVSSKKG 1934
Cdd:PRK03918 388 --KLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1026-1571 |
1.30e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.12 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1026 KAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLK------KKDFEISQLNGKIEDE 1099
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAeaeealREQAELNRLKKKYLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1100 QTICIQlQKKLKELQAR--IEELEEELEAERAARAKVEKQRADLARELEEISERLeeaggataaqiEMNKKREAEFQKLR 1177
Cdd:pfam05557 88 LNKKLN-EKESQLADARevISCLKNELSELRRQIQRAELELQSTNSELEELQERL-----------DLLKAKASEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1178 RDLEEAtlQHEATAATLRKK--------QADSVAELGEQIDNLQRVKqKLEKEKSELRLElddvvsnMEHVVKTKANLEk 1249
Cdd:pfam05557 156 QNLEKQ--QSSLAEAEQRIKelefeiqsQEQDSEIVKNSKSELARIP-ELEKELERLREH-------NKHLNENIENKL- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1250 mtrSLEDQMNEYKTK---YEEGQRCINDFTMQKSKLQSE----------NGELSRQLEEKDSLVSQLTRSKMSYTQQIED 1316
Cdd:pfam05557 225 ---LLKEEVEDLKRKlerEEKYREEAATLELEKEKLEQElqswvklaqdTGLNLRSPEDLSRRIEQLQQREIVLKEENSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1317 LKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEelEEAKKKLA 1396
Cdd:pfam05557 302 LTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTM--SNYSPQLL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1397 QRLQETEEAVEAVNAKCSSLEktkHRLQNEIEDLMVDLERSNAAAAALDKKQRNFD--------KVLSEWKQKFEESQAE 1468
Cdd:pfam05557 380 ERIEEAEDMTQKMQAHNEEME---AQLSVAEEELGGYKQQAQTLERELQALRQQESladpsyskEEVDSLRRKLETLELE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1469 LESSQKEARCLSTELFK--------------LKNSYEEALDHLETMKRENKNLQEEISDLteqlgeggksiheleKMRKQ 1534
Cdd:pfam05557 457 RQRLREQKNELEMELERrclqgdydpkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERL---------------KRLLK 521
|
570 580 590
....*....|....*....|....*....|....*..
gi 163644331 1535 LEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIK 1571
Cdd:pfam05557 522 KLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELK 558
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1135-1430 |
1.35e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1135 EKQRADLARELEEISERLeeaggATAAqiemnkkreAEFQKLRR---DLEEATLQH---------EATAATLRKKQADSV 1202
Cdd:COG3096 784 EKRLEELRAERDELAEQY-----AKAS---------FDVQKLQRlhqAFSQFVGGHlavafapdpEAELAALRQRRSELE 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1203 AELGEQIDNLQRVKQKLEKEKSELRLeLDDVVSNMEHVVKTkaNLEKMTRSLEDQMNEYktkyEEGQRCINDFTMQKSKL 1282
Cdd:COG3096 850 RELAQHRAQEQQLRQQLDQLKEQLQL-LNKLLPQANLLADE--TLADRLEELREELDAA----QEAQAFIQQHGKALAQL 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1283 QSENGELSRQLEEKDSLVSQLTRSKmsytQQIEDLKRQLEEETKAKSALAH-----AVQSARHDTDL---LREQYEEEQE 1354
Cdd:COG3096 923 EPLVAVLQSDPEQFEQLQADYLQAK----EQQRRLKQQIFALSEVVQRRPHfsyedAVGLLGENSDLnekLRARLEQAEE 998
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1355 AKAELQRGMSKANSEVAQW-----------RTKYET--DAIQRTEELE-----EAKKKLAQRLQETEEAVEAVNAKCSSL 1416
Cdd:COG3096 999 ARREAREQLRQAQAQYSQYnqvlaslkssrDAKQQTlqELEQELEELGvqadaEAEERARIRRDELHEELSQNRSRRSQL 1078
|
330
....*....|....
gi 163644331 1417 EKTKHRLQNEIEDL 1430
Cdd:COG3096 1079 EKQLTRCEAEMDSL 1092
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1303-1797 |
1.66e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1303 LTRSKMSYTQQIEDLKRQLEEETKAKSA---LAHAVQSARHDTDLL---------REQYEEEQEAKAELQRGMskansev 1370
Cdd:COG3096 243 MTLEAIRVTQSDRDLFKHLITEATNYVAadyMRHANERRELSERALelrrelfgaRRQLAEEQYRLVEMAREL------- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1371 aqwrtkyetdaiqrtEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRlQNEIEDLMVDLERSNAAAAALDKKQrn 1450
Cdd:COG3096 316 ---------------EELSARESDLEQDYQAASDHLNLVQTALRQQEKIERY-QEDLEELTERLEEQEEVVEEAAEQL-- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1451 fdkvlsewkqkfEESQAELESSQKEARCLSTELfklkNSYEEALDHLETmkrenKNLQEEisdlteqlgeggKSIHELEK 1530
Cdd:COG3096 378 ------------AEAEARLEAAEEEVDSLKSQL----ADYQQALDVQQT-----RAIQYQ------------QAVQALEK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1531 MRKQLEQEKSEIQSALEEAEASLEHEEgkilraqlEFSQIKADIERKLAEKDEEMEQSKRNLQrtidtLQSSLESETrSR 1610
Cdd:COG3096 425 ARALCGLPDLTPENAEDYLAAFRAKEQ--------QATEEVLELEQKLSVADAARRQFEKAYE-----LVCKIAGEV-ER 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1611 NEALRIKKKMEGDLNEMEIQLSQAN---RQAAEAQKQLKSVHahmkDAQLQLDD-SLRTNEDLkENTAIVERRNNLLQAE 1686
Cdd:COG3096 491 SQAWQTARELLRRYRSQQALAQRLQqlrAQLAELEQRLRQQQ----NAERLLEEfCQRIGQQL-DAAEELEELLAELEAQ 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1687 LEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLEtdisQLQTEVEEAVQECRnaeekakkAITDAam 1766
Cdd:COG3096 566 LEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALE----RLREQSGEALADSQ--------EVTAA-- 631
|
490 500 510
....*....|....*....|....*....|....
gi 163644331 1767 MAEELKKEQDTSA---HLERMKKNMEQTIKDLQH 1797
Cdd:COG3096 632 MQQLLEREREATVerdELAARKQALESQIERLSQ 665
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
845-1645 |
1.79e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 845 AEAEKEMANMKDefaKLKEAYAKSEARRKELEEkmvsLLQEKNDLQLQVQAEQDNLcdaeercdQLIKNKIQLEAKAK-- 922
Cdd:COG3096 288 LELRRELFGARR---QLAEEQYRLVEMARELEE----LSARESDLEQDYQAASDHL--------NLVQTALRQQEKIEry 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 923 -----ELTERLEDEEEMNAELT-------AKKRKLEDECSELKKDIDDL------------------------------- 959
Cdd:COG3096 353 qedleELTERLEEQEEVVEEAAeqlaeaeARLEAAEEEVDSLKSQLADYqqaldvqqtraiqyqqavqalekaralcglp 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 960 ELTLAKVEKEKHATENKVKNLTEEMAA----LDDIIAKLTKEKKALQ------------EAHQQTLDDLQSEEDKVNTLT 1023
Cdd:COG3096 433 DLTPENAEDYLAAFRAKEQQATEEVLEleqkLSVADAARRQFEKAYElvckiageversQAWQTARELLRRYRSQQALAQ 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1024 KAKAkLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLkltqESLMDLENDKQQLEERLKkkdfeisQLNGKIEDEQTIC 1103
Cdd:COG3096 513 RLQQ-LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQL----DAAEELEELLAELEAQLE-------ELEEQAAEAVEQR 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1104 IQLQKKLKELQARIEELeeeleaeraarakveKQRADLARELEEISERLEEAGGATAAQiemnkkreaefqklRRDLEEA 1183
Cdd:COG3096 581 SELRQQLEQLRARIKEL---------------AARAPAWLAAQDALERLREQSGEALAD--------------SQEVTAA 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1184 ---TLQHEATAATLRKKQADSVAELGEQIDNLQ--------RVKQKLEKEKSELRLEL-DDVV-------------SNME 1238
Cdd:COG3096 632 mqqLLEREREATVERDELAARKQALESQIERLSqpggaedpRLLALAERLGGVLLSEIyDDVTledapyfsalygpARHA 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1239 HVVKTKANLEKMTRSLEDqmneyktkyeegqrCINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYT------- 1311
Cdd:COG3096 712 IVVPDLSAVKEQLAGLED--------------CPEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSDRQWRYSrfpevpl 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1312 -------QQIEDLKRQLEEETKAKSALAHAVQS------------ARHDTDLLREQYEEE----QEAKAELQRGMSKANS 1368
Cdd:COG3096 778 fgraareKRLEELRAERDELAEQYAKASFDVQKlqrlhqafsqfvGGHLAVAFAPDPEAElaalRQRRSELERELAQHRA 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1369 EVAQWRtkyetdaiqrteeleeakkklaQRLQETEEAVEAVNAKCSSL----EKTkhrLQNEIEDLMVDLERSNAAAAAL 1444
Cdd:COG3096 858 QEQQLR----------------------QQLDQLKEQLQLLNKLLPQAnllaDET---LADRLEELREELDAAQEAQAFI 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1445 DKKQRNFDK------VLSEWKQKFEESQAELESSQKEARCLSTELFKLKN--------SYEEALDHLetmkrenknlqEE 1510
Cdd:COG3096 913 QQHGKALAQleplvaVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEvvqrrphfSYEDAVGLL-----------GE 981
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1511 ISDLTEQLGEggksihELEKMrkqlEQEKSEIQSALEEAEAslEHEEGKILRAQLEFS-QIKADIERKLAEK-------- 1581
Cdd:COG3096 982 NSDLNEKLRA------RLEQA----EEARREAREQLRQAQA--QYSQYNQVLASLKSSrDAKQQTLQELEQEleelgvqa 1049
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 163644331 1582 DEEMEQSKRNLQrtiDTLQSSLeSETRSR-NEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQL 1645
Cdd:COG3096 1050 DAEAEERARIRR---DELHEEL-SQNRSRrSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1086-1313 |
1.94e-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: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1086 DFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATAAQIEM 1165
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1166 NKKREAEFQKLRRDLEEATLQHEATAATLRKKQADSVAELgeqIDNLQRVKQKLEKEKSELRLELDDvvsnmehVVKTKA 1245
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADL---LEELKADKAELEAKKAELEAKLAE-------LEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163644331 1246 NLEKMTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQ 1313
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
842-1086 |
1.97e-05 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 49.77 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 842 LKSAEAEKEMANMKDEFAK----LKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDnlcdaEERCDQLIKNKIQL 917
Cdd:pfam18971 596 FNKAVAEAKSTGNYDEVKKaqkdLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQ-----KDEIFALINKEANR 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 918 EAKAKELTERLEdeeemnaeltAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKnltEEMAALDDIIAKL--T 995
Cdd:pfam18971 671 DARAIAYTQNLK----------GIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAE---ETLKALKGSVKDLgiN 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 996 KEKKALQEAHQQTLDDLQSEEDK-VNTLTKAKAKLEQQVDDLEGSLEQEKKL-RMDLERAKRKLEGDLKLTQESLMDLEN 1073
Cdd:pfam18971 738 PEWISKVENLNAALNEFKNGKNKdFSKVTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKN 817
|
250
....*....|....
gi 163644331 1074 -DKQQLEERLKKKD 1086
Cdd:pfam18971 818 fSKEQLAQQAQKNE 831
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1256-1472 |
1.98e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1256 DQMNEYKTKYEEGQRCINDFTMQKSKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAV 1335
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1336 QSARHD-TDLLREQYEEEQEAKAEL---QRGMSKAN------SEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQETEEA 1405
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALllsPEDFLDAVrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163644331 1406 VEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELESS 1472
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
892-1095 |
2.37e-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: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 892 QVQAEQDNLCDAEERCDQLIKNKIQLEAKAKELTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKH 971
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 972 ATENKVKNLTEEMAA--LDDIIAKLTKEKKaLQEAHQQTLDDLQSEEDKvntLTKAKAKLEQQVDDLEGSLEQEKKLRMD 1049
Cdd:COG3883 97 RSGGSVSYLDVLLGSesFSDFLDRLSALSK-IADADADLLEELKADKAE---LEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 163644331 1050 LERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGK 1095
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
843-1004 |
2.45e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 843 KSAEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLcdaEERCDQLIKNKIQ------ 916
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERARALYRSGGSvsyldv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 917 -LEAK---------------AKELTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNL 980
Cdd:COG3883 108 lLGSEsfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
170 180
....*....|....*....|....
gi 163644331 981 TEEMAALDDIIAKLTKEKKALQEA 1004
Cdd:COG3883 188 SAEEAAAEAQLAELEAELAAAEAA 211
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
845-1163 |
2.55e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 845 AEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKmvsLLQEKNDLQLQVQAEQdnLCDAEERCDQLikNKIQLEAKAKEL 924
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKV---LKKESELIKLKELAEQ--LKELEEKLKKY--NLEELEKKAEEY 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 925 terlEDEEEMNAELTAKKRKLEDECSELKkdidDLELTLAKVEKEKHATENKVKNLTEEMAALD-DIIAKLTKEKKALQE 1003
Cdd:PRK03918 528 ----EKLKEKLIKLKGEIKSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEP 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1004 AHQQTLDDLQSE---EDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLegdlklTQESLMDLENDKQQLEE 1080
Cdd:PRK03918 600 FYNEYLELKDAEkelEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY------SEEEYEELREEYLELSR 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1081 RLKKKDFEISQLNGKIEDeqtiCIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATA 1160
Cdd:PRK03918 674 ELAGLRAELEELEKRREE----IKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIA 749
|
...
gi 163644331 1161 AQI 1163
Cdd:PRK03918 750 SEI 752
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1163-1601 |
2.59e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1163 IEMNKKREAEFQKLrrdLEEAT-------LQHEA-------TAATLRKKQADSVAELGEQidnlqrvKQKLEkeksELRL 1228
Cdd:PRK04863 249 IRVTQSDRDLFKHL---ITESTnyvaadyMRHANerrvhleEALELRRELYTSRRQLAAE-------QYRLV----EMAR 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1229 ELDDVVSNmehvvktKANLEKMTRSLEDQMNEYKT---KYEEGQRCINDFtmqksklqsenGELSRQLEEKDSLVSQLTR 1305
Cdd:PRK04863 315 ELAELNEA-------ESDLEQDYQAASDHLNLVQTalrQQEKIERYQADL-----------EELEERLEEQNEVVEEADE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1306 SKMSYTQQiedlKRQLEEETK-AKSALAHAVQSarhdTDLLREQYEEEQEAKAELQRG------MSKANSEVAQWRTKYE 1378
Cdd:PRK04863 377 QQEENEAR----AEAAEEEVDeLKSQLADYQQA----LDVQQTRAIQYQQAVQALERAkqlcglPDLTADNAEDWLEEFQ 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1379 TDAIQRTEELEEakkkLAQRLQETEEAVEAVNAKCSSLEKtkhrlqneiedLMVDLERSNAAAAALDK-----KQRNFDK 1453
Cdd:PRK04863 449 AKEQEATEELLS----LEQKLSVAQAAHSQFEQAYQLVRK-----------IAGEVSRSEAWDVARELlrrlrEQRHLAE 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1454 VLSEWKQKFEESQAELESsQKEARCLSTELFKLKNSYEEALDHLETMKREnknLQEEISDLTEQLGEGGKSIHELEKMRK 1533
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQ-QQRAERLLAEFCKRLGKNLDDEDELEQLQEE---LEARLESLSESVSEARERRMALRQQLE 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1534 QLEQEKSEIQS---ALEEAEASLEHeegkiLRAQ-----------LEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTL 1599
Cdd:PRK04863 590 QLQARIQRLAArapAWLAAQDALAR-----LREQsgeefedsqdvTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
..
gi 163644331 1600 QS 1601
Cdd:PRK04863 665 SQ 666
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1022-1172 |
3.54e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1022 LTKAKAKLEQQVDDLEGSLEQEKKLRM-----DLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKI 1096
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEALleakeEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1097 EDEQTICIQLQKKLKELQARIeeleeeleaeraaRAKVEKQRADL----------ARE--LEEISERLEEAGGATAAQIE 1164
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEEL-------------EELIEEQLQELerisgltaeeAKEilLEKVEEEARHEAAVLIKEIE 179
|
....*...
gi 163644331 1165 MNKKREAE 1172
Cdd:PRK12704 180 EEAKEEAD 187
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1456-1912 |
3.58e-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: 48.81 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1456 SEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHElekmRKQL 1535
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE----QLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1536 EQEKSEIQSALEEAEASL-EHEEgkiLRAQLEFSQIKAdierKLAEKDEEMEQSKRNLQRTIDTLQS---SLESETRSRN 1611
Cdd:TIGR00618 259 QQLLKQLRARIEELRAQEaVLEE---TQERINRARKAA----PLAAHIKAVTQIEQQAQRIHTELQSkmrSRAKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1612 EALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQlKSVHAHmKDAQLQLDDSLRTNEDLKEntaIVERRNNLLQAELEELR 1691
Cdd:TIGR00618 332 AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVA-TSIREI-SCQQHTLTQHIHTLQQQKT---TLTQKLQSLCKELDILQ 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1692 AalEQTERGRKLAEQELLdtseRVQLLHSQNTSLLNQKKKLE-----TDISQLQTEVEEAVQECRNA-EEKAKKAITDAA 1765
Cdd:TIGR00618 407 R--EQATIDTRTSAFRDL----QGQLAHAKKQQELQQRYAELcaaaiTCTAQCEKLEKIHLQESAQSlKEREQQLQTKEQ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1766 MMAEELKKEQDTSAHLERMKKN----MEQTIKDLQHRLD----EAEQIAMKGGKKQVQKLEARVRELESEVESEQK---- 1833
Cdd:TIGR00618 481 IHLQETRKKAVVLARLLELQEEpcplCGSCIHPNPARQDidnpGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKqras 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1834 ---KSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKAYKRAAEEAEEQANTNLSKFRKIQHELDEAEE 1910
Cdd:TIGR00618 561 lkeQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQE 640
|
..
gi 163644331 1911 RA 1912
Cdd:TIGR00618 641 LA 642
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1532-1648 |
3.63e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1532 RKQLEQEKSEIQSALEEAEASLE-HEEGKILRAQLEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSR 1610
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEaIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110
....*....|....*....|....*....|....*...
gi 163644331 1611 NEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSV 1648
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
841-1115 |
3.84e-05 |
|
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: 48.96 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 841 LLKSAEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKnkiQLEAK 920
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLN---EVKTS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 921 AKELTERLEDEEEMnaeltakKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNlteeMAALDDIIAKLTKEKKA 1000
Cdd:pfam15921 666 RNELNSLSEDYEVL-------KRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS----MEGSDGHAMKVAMGMQK 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1001 LQEAHQQTLDDLQSeedKVNTLTKAKAKLEQQVDDLEgslEQEKKLRMDLERA---KRKLEGDLKLTQESLMDLENDKQQ 1077
Cdd:pfam15921 735 QITAKRGQIDALQS---KIQFLEEAMTNANKEKHFLK---EEKNKLSQELSTVateKNKMAGELEVLRSQERRLKEKVAN 808
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 163644331 1078 LEERLKKKDFEISQLNGKI--EDEQTICIQLQKKL--KELQA 1115
Cdd:pfam15921 809 MEVALDKASLQFAECQDIIqrQEQESVRLKLQHTLdvKELQG 850
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
861-1401 |
5.17e-05 |
|
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: 48.21 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 861 LKEAYAKSEARRKELEEKMVSLLQE-----KNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAK----AKELTERLED- 930
Cdd:pfam07111 120 LRAALAGAEMVRKNLEEGSQRELEEiqrlhQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKrageAKQLAEAQKEa 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 931 ----------EEEMNAELT-----------------------AKKRKLEDECSELKKDIDDL----ELTLAKVEKEKHAT 973
Cdd:pfam07111 200 ellrkqlsktQEELEAQVTlveslrkyvgeqvppevhsqtweLERQELLDTMQHLQEDRADLqatvELLQVRVQSLTHML 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 974 ENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTL---------DDLQsEEDKVNTLTKAKAKLEQQVDD-------LE 1037
Cdd:pfam07111 280 ALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVfalmvqlkaQDLE-HRDSVKQLRGQVAELQEQVTSqsqeqaiLQ 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1038 GSLeQEKKLRMDLERAKRK-LEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQAR 1116
Cdd:pfam07111 359 RAL-QDKAAEVEVERMSAKgLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNR 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1117 IeeleeeleaeRAARAKVEKQRADLARELEEISERLEEAGGATAAQiEMNKKREAEFQKLR--RDLEEATLQheaTAATL 1194
Cdd:pfam07111 438 L----------SYAVRKVHTIKGLMARKVALAQLRQESCPPPPPAP-PVDADLSLELEQLReeRNRLDAELQ---LSAHL 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1195 RKKQADSVAELGE-QIDNLQRVKQKLEKEKSELRLELDDVVSNMEHVVKTKANLEKMTRSLEDQMNEYKTKYEEGqrcin 1273
Cdd:pfam07111 504 IQQEVGRAREQGEaERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQA----- 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1274 dftmqkskLQSENGELSRQLEEkdslvsqltrskmsytqQIEDLKRQLEEetkAKSALAHAVQSARHdtdlLREQYEEEQ 1353
Cdd:pfam07111 579 --------LQEKVAEVETRLRE-----------------QLSDTKRRLNE---ARREQAKAVVSLRQ----IQHRATQEK 626
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 163644331 1354 EAKAELQRGMSKANSEVAQWRTKyetdaiqRTEELEEAKKKLAQRLQE 1401
Cdd:pfam07111 627 ERNQELRRLQDEARKEEGQRLAR-------RVQELERDKNLMLATLQQ 667
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1441-1932 |
5.55e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1441 AAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGE 1520
Cdd:pfam05483 87 AEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCAR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1521 GGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFS-QIKADIErKLAEKDEEMEQSKRNLQRTIDTL 1599
Cdd:pfam05483 167 SAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHE-KIQHLEEEYKKEINDKEKQVSLL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1600 QSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERR 1679
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1680 NNLLQAELEELRAALEQTERGRKLAEQELLDTSERVQ-LLHSQNTSLLNQKKKLETDISQLQ---TEVEEAVQECRNAE- 1754
Cdd:pfam05483 326 ICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEeLLRTEQQRLEKNEDQLKIITMELQkksSELEEMTKFKNNKEv 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1755 --EKAKKAITDAAMMAEELKKEQDTSahlERMKKNMEQTIKDLQHRLDEAE--QIAMKGGKKQVQKLEARVRELESEVES 1830
Cdd:pfam05483 406 elEELKKILAEDEKLLDEKKQFEKIA---EELKGKEQELIFLLQAREKEIHdlEIQLTAIKTSEEHYLKEVEDLKTELEK 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1831 EQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQ-DLVDKLQLKVKAYKRAAEEAEEQAN--TNLSKFRK------- 1900
Cdd:pfam05483 483 EKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQeDIINCKKQEERMLKQIENLEEKEMNlrDELESVREefiqkgd 562
|
490 500 510
....*....|....*....|....*....|...
gi 163644331 1901 -IQHELDEAEERADIAESQVNKLRAKSRDVSSK 1932
Cdd:pfam05483 563 eVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1282-1548 |
6.35e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.22 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1282 LQSENGELSRQLEEK-DSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEE----QEAK 1356
Cdd:pfam00038 23 LEQQNKLLETKISELrQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDElnlrTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1357 AELQrGMSKANSEVAQWRTKYETDAIQRTEEL-------EEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIED 1429
Cdd:pfam00038 103 NDLV-GLRKDLDEATLARVDLEAKIESLKEELaflkknhEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1430 LMvdlersnaaaaaldkkQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQE 1509
Cdd:pfam00038 182 IA----------------AKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLER 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 163644331 1510 EISDLTE----QLGEGGKSIHELEkmrKQLEQEKSEIQSALEE 1548
Cdd:pfam00038 246 QLAETEEryelQLADYQELISELE---AELQETRQEMARQLRE 285
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1523-1790 |
6.62e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.11 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1523 KSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKI---LRAQLEFSQIKADIERKLAEkdeemeqskrnLQRTIDTL 1599
Cdd:pfam15905 73 KDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLnaaVREKTSLSASVASLEKQLLE-----------LTRVNELL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1600 QSSLESETRSRN------EALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKsvHAHMKDAQLQldDSLRTNEDLKent 1673
Cdd:pfam15905 142 KAKFSEDGTQKKmsslsmELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLE--HSKGKVAQLE--EKLVSTEKEK--- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1674 aIVERRNNL-LQAELEELRAALEQTERGRklaeqelLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRN 1752
Cdd:pfam15905 215 -IEEKSETEkLLEYITELSCVSEQVEKYK-------LDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKL 286
|
250 260 270
....*....|....*....|....*....|....*...
gi 163644331 1753 AEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ 1790
Cdd:pfam15905 287 LESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQ 324
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1031-1878 |
6.89e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.12 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1031 QQVDDLEGSLEQEKKLRMDLERAKRKL--EGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQK 1108
Cdd:TIGR01612 500 MRMKDFKDIIDFMELYKPDEVPSKNIIgfDIDQNIKAKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEK 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1109 KLKELQAR----IEELEEELEAERAARAKVE---------KQRADLARELEEISERLEEAGGATAAQI------------ 1163
Cdd:TIGR01612 580 EIKDLFDKyleiDDEIIYINKLKLELKEKIKnisdkneyiKKAIDLKKIIENNNAYIDELAKISPYQVpehlknkdkiys 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1164 ----EMNKKREAEFQKLRRDLeEATLQHEATAATLRKKQADsvaELGEQIDNLQRVKQKLEKEKSELRL--------ELD 1231
Cdd:TIGR01612 660 tiksELSKIYEDDIDALYNEL-SSIVKENAIDNTEDKAKLD---DLKSKIDKEYDKIQNMETATVELHLsnienkknELL 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1232 DVVSNMEHVVKTKANLEkMTRSLEDqmneYKTKYEEGQRCINDFTMQKSKL---QSENGELSRQLEE-------KDSLVS 1301
Cdd:TIGR01612 736 DIIVEIKKHIHGEINKD-LNKILED----FKNKEKELSNKINDYAKEKDELnkyKSKISEIKNHYNDqinidniKDEDAK 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1302 QLTRSKMSYTQQI----EDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELqrgMSKANSEVAQWR-TK 1376
Cdd:TIGR01612 811 QNYDKSKEYIKTIsikeDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAEL---TNKIKAEISDDKlND 887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1377 YETDAIQRTEELEEAKKKLAQRLQETeEAVEAVNAKCSSLEKTK------HRLQNEIEDLMVDLERSNAAAAALDKKQRN 1450
Cdd:TIGR01612 888 YEKKFNDSKSLINEINKSIEEEYQNI-NTLKKVDEYIKICENTKesiekfHNKQNILKEILNKNIDTIKESNLIEKSYKD 966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1451 -FDKVLSEWKQKFEESQAELESSQKEARclSTELFKLKNSYEEAL---------DHLETMKRENKNLQEEISDLTEQLGE 1520
Cdd:TIGR01612 967 kFDNTLIDKINELDKAFKDASLNDYEAK--NNELIKYFNDLKANLgknkenmlyHQFDEKEKATNDIEQKIEDANKNIPN 1044
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1521 GGKSIH--------ELEK-MRKQLEQEKSEIqsaLEEAEASLEH-EEGKILRAQLEFSQIKADIERKLAEKDEEMEQSKR 1590
Cdd:TIGR01612 1045 IEIAIHtsiyniidEIEKeIGKNIELLNKEI---LEEAEINITNfNEIKEKLKHYNFDDFGKEENIKYADEINKIKDDIK 1121
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1591 NLQRTIDtlqsslesetRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEA--QKQLKSVHAHMKDaqlqlddsLRTNED 1668
Cdd:TIGR01612 1122 NLDQKID----------HHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisNDDPEEIEKKIEN--------IVTKID 1183
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1669 LKENtaIVERRNNLLQ--AELEELRAALEQTeRGRKLAEQELLDTSERVQLLHSQNTSlLNQKKKLETDISQLQtEVEEA 1746
Cdd:TIGR01612 1184 KKKN--IYDEIKKLLNeiAEIEKDKTSLEEV-KGINLSYGKNLGKLFLEKIDEEKKKS-EHMIKAMEAYIEDLD-EIKEK 1258
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1747 VQECRNaeEKAKKAITDAAMMAEELKKEQDTSAHLerMKKNMEQTIKDLQHRL-----DEAEQIAMKGGKKQVQKLEARV 1821
Cdd:TIGR01612 1259 SPEIEN--EMGIEMDIKAEMETFNISHDDDKDHHI--ISKKHDENISDIREKSlkiieDFSEESDINDIKKELQKNLLDA 1334
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 163644331 1822 RELESEVESEQKKSSE-----AVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVK 1878
Cdd:TIGR01612 1335 QKHNSDINLYLNEIANiynilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIK 1396
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1383-1592 |
7.66e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1383 QRTEELEEAKKKLAQRLQETEEAVEAVNAKcsslektkhrlqneiedlmvdLERSNAAAAALDKKQRNFDKVLSEWKQKF 1462
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEAR---------------------LEAAKTELEDLEKEIKRLELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1463 EESQAELES--SQKEARCLSTElfklknsyeealdhLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKS 1540
Cdd:COG1579 76 KKYEEQLGNvrNNKEYEALQKE--------------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 163644331 1541 EIQSALEEAEASLEhEEGKILRAQLEfsQIKADIERKLAEKDEEMEQSKRNL 1592
Cdd:COG1579 142 EKKAELDEELAELE-AELEELEAERE--ELAAKIPPELLALYERIRKRKNGL 190
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1380-1697 |
7.92e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1380 DAIQRTEELEEAKKKLAQRLQETEE---AVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAAlDKKQRNFDKVLS 1456
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE-ETRETLSTLSLR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1457 EWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEAldhletmkrenknlQEEISDLTEQLGEggksihelekMRKQLe 1536
Cdd:PRK11281 125 QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERA--------------QAALYANSQRLQQ----------IRNLL- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1537 qekseiqSALEEAEASLEHEEGKILRAQLEFSQIKADIERKLAEKDEEMeQSKRNLQRTIDTLQSS-LESETRSRNEALR 1615
Cdd:PRK11281 180 -------KGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQL-QDLLQKQRDYLTARIQrLEHQLQLLQEAIN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1616 IKKkmegdLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSL-----RTNEDLKENTAIVERRNNLLQAE--LE 1688
Cdd:PRK11281 252 SKR-----LTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLlkateKLNTLTQQNLRVKNWLDRLTQSErnIK 326
|
....*....
gi 163644331 1689 ELRAALEQT 1697
Cdd:PRK11281 327 EQISVLKGS 335
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1420-1798 |
9.25e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.43 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1420 KHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDK---VLSEWKQKFEESQAELESSQKEARclstelfklknsyeealdh 1496
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEER------------------- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1497 letmKRENKNL-QEEISDLTEQlgeggksIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKilraQLEFSQIKADIE 1575
Cdd:pfam17380 359 ----KRELERIrQEEIAMEISR-------MRELERLQMERQQKNERVRQELEAARKVKILEEER----QRKIQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1576 RKLAEKDEEMEQSKRNLQrtidtlqsslesETRSRnEALRIKKKMEGDLNEMEIQlsqanRQAAEAQKQLKsvhahmkda 1655
Cdd:pfam17380 424 QIRAEQEEARQREVRRLE------------EERAR-EMERVRLEEQERQQQVERL-----RQQEEERKRKK--------- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1656 qlqlddsLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQELLDtservqllhSQNTSLLNQKKKLETD 1735
Cdd:pfam17380 477 -------LELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE---------RQKAIYEEERRREAEE 540
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 163644331 1736 ISQLQTEVEEavqecrnaeekaKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHR 1798
Cdd:pfam17380 541 ERRKQQEMEE------------RRRIQEQMRKATEERSRLEA---MEREREMMRQIVESEKAR 588
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1561-1858 |
9.79e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1561 LRAQLEFSQIKADIERKLAEKDEEMEQSKRNLQrTIDTLQSSLESETRSR-------NEALRIKKKME---GDLNEMEIQ 1630
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLVEMARELA-ELNEAESDLEQDYQAAsdhlnlvQTALRQQEKIEryqADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1631 LSQANRQAAEAQKQLKSVHAHMKDAQLQLDdslrtneDLKENTAIVERRNNLLQAELEELRAALEQTERGRKL---AEQE 1707
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAAEEEVD-------ELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLcglPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1708 LLDTSERVQLLHSQNTSLLNQKKKLETDISQLQ---TEVEEAVQECRN---------AEEKAKKAITDAAMMAEELKKEQ 1775
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQaahSQFEQAYQLVRKiagevsrseAWDVARELLRRLREQRHLAEQLQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1776 DTSAHLERMKKNMEQTiKDLQHRLDEAEQIAMKGGKKQVQkLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQ 1855
Cdd:PRK04863 517 QLRMRLSELEQRLRQQ-QRAERLLAEFCKRLGKNLDDEDE-LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAR 594
|
...
gi 163644331 1856 TEE 1858
Cdd:PRK04863 595 IQR 597
|
|
| COG6 |
smart01087 |
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ... |
1374-1536 |
9.87e-05 |
|
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localisation.
Pssm-ID: 215018 Cd Length: 598 Bit Score: 47.32 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1374 RTKYETDAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQrnfdK 1453
Cdd:smart01087 9 RSDLEKRLLKINGEFLSEFKPVAEQLQRLSEDVQKLNNSCDSMKDQLNTAKNQTQDLISEASELQEELALLELKK----K 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1454 VLSEWKQKFEESQAELESSQKEARCLSTELFKlknsyeeALDHLETMKRENKNLqeeisdLTEQLGEGGKSIheLEKMRK 1533
Cdd:smart01087 85 LLDAFLSKFTLSQDELDVLTSREGPIDDEFFQ-------VLDKVQEIHEDCSVL------LQNEYQTAGLEI--MEKMNQ 149
|
...
gi 163644331 1534 QLE 1536
Cdd:smart01087 150 LLE 152
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
869-1088 |
1.07e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.59 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 869 EARRKELEEkMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKI-------QLEAKAKELTERLEDEEEMNAELTAK 941
Cdd:PLN02939 149 QARLQALED-LEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIhveileeQLEKLRNELLIRGATEGLCVHSLSKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 942 KRKLEDECSELKKDIDDL----------ELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKkalQEAHQQTLDD 1011
Cdd:PLN02939 228 LDVLKEENMLLKDDIQFLkaelievaetEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQ---YDCWWEKVEN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1012 LQSEEDKV-NTLTKAKAKLEQ------QVDDLEGSLEQE-----------------KKLRMDLERAKRKLEGDLKLTQES 1067
Cdd:PLN02939 305 LQDLLDRAtNQVEKAALVLDQnqdlrdKVDKLEASLKEAnvskfssykvellqqklKLLEERLQASDHEIHSYIQLYQES 384
|
250 260
....*....|....*....|.
gi 163644331 1068 LMDLENDKQQLEERLKKKDFE 1088
Cdd:PLN02939 385 IKEFQDTLSKLKEESKKRSLE 405
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
873-1234 |
1.27e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 873 KELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAKELTERLEDEEEMNAELTAKKRKLEDECSEL 952
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 953 KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQ 1032
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1033 VDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKE 1112
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1113 LQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEEATLQHEATAA 1192
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 163644331 1193 TLRKKQADSVAELGEQIDNLQRVKQKLEKEKSELRLELDDVV 1234
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1424-1774 |
1.29e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 46.98 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1424 QNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLST-ELFKLKNSYEEALdhLETMKR 1502
Cdd:pfam13166 95 QEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDECWKKIKRKKNSALSEAlNGFKYEANFKSRL--LREIEK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1503 ENKN-----LQEEISDLTEQLGEGGK--------SIHELEKMRKQ--LEQEKSEIQSALEE----------AEASLEHEE 1557
Cdd:pfam13166 173 DNFNagvllSDEDRKAALATVFSDNKpeiapltfNVIDFDALEKAeiLIQKVIGKSSAIEEliknpdladwVEQGLELHK 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1558 GkiLRAQLEFSQIKADIERKLAEK---DEEMEQSKRNLQRTIDTLQSSLE---------SETRSRNEALRI-KKKMEGDL 1624
Cdd:pfam13166 253 A--HLDTCPFCGQPLPAERKAALEahfDDEFTEFQNRLQKLIEKVESAISsllaqlpavSDLASLLSAFELdVEDIESEA 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1625 NEMEIQLsQANRQAAEAQKQLKSVHAHMKDAQlqlDDSLRTNEDLKENTAIVERRNNL---LQAELEELRAALEQTErgr 1701
Cdd:pfam13166 331 EVLNSQL-DGLRRALEAKRKDPFKSIELDSVD---AKIESINDLVASINELIAKHNEItdnFEEEKNKAKKKLRLHL--- 403
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 163644331 1702 klaeqelldtserVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAK---KAITDAAMMAEELKKE 1774
Cdd:pfam13166 404 -------------VEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKeleAQLRDHKPGADEINKL 466
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1572-1765 |
1.32e-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: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1572 ADIERKLAEKD-EEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHA 1650
Cdd:COG3883 14 ADPQIQAKQKElSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1651 HMKDAQLQLD--DSLRTNEDLKE-------NTAIVERRNNLL------QAELEELRAALEQTERGRKLAEQELLDTSERV 1715
Cdd:COG3883 94 ALYRSGGSVSylDVLLGSESFSDfldrlsaLSKIADADADLLeelkadKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 163644331 1716 QLLHSQNTSLLNQkkkLETDISQLQTEVEEAVQECRNAEEKAKKAITDAA 1765
Cdd:COG3883 174 EAQQAEQEALLAQ---LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1529-1876 |
1.39e-04 |
|
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: 47.27 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1529 EKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETR 1608
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1609 SRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKqlksvhahMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELE 1688
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEK--------LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1689 ELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAITDAAMMA 1768
Cdd:pfam02463 304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1769 EELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAmkggKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERR 1848
Cdd:pfam02463 384 ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLL----KEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK 459
|
330 340
....*....|....*....|....*...
gi 163644331 1849 IKELTYQTEEDRKNLARLQDLVDKLQLK 1876
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLE 487
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1135-1870 |
1.47e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.25 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1135 EKQR-ADLARELEEISER---LEEAGGATAA--QIEMNKKREAE-FQKLRRDLEEATLQHEAtaatlrkkQADSVAELGE 1207
Cdd:COG3096 304 EQYRlVEMARELEELSAResdLEQDYQAASDhlNLVQTALRQQEkIERYQEDLEELTERLEE--------QEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1208 QIDNLQRVKQKLEKEKSELRLELDDVVSNMEhvvktkanlEKMTRSLedQMNEYKTKYEEGQRCINDFTMQKSKLQSENG 1287
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALD---------VQQTRAI--QYQQAVQALEKARALCGLPDLTPENAEDYLA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1288 ELSRQLEEKDSLVSQLtRSKMSYTqqiEDLKRQLEEETKAKSALAHAV-QSARHDTdlLREQYEEEQEAKAELQRgmska 1366
Cdd:COG3096 445 AFRAKEQQATEEVLEL-EQKLSVA---DAARRQFEKAYELVCKIAGEVeRSQAWQT--ARELLRRYRSQQALAQR----- 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1367 nseVAQWRTKYeTDAIQRTEELEEAK---KKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAA 1443
Cdd:COG3096 514 ---LQQLRAQL-AELEQRLRQQQNAErllEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1444 LDKKQRNFDKVLSEWKQKF-------EESQAELESSQKEARCLSTELFKLKNsYEEALDHLETMKREnknLQEEISDLT- 1515
Cdd:COG3096 590 LRARIKELAARAPAWLAAQdalerlrEQSGEALADSQEVTAAMQQLLERERE-ATVERDELAARKQA---LESQIERLSq 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1516 -------------EQLG-----EG----------------GKSIH-----ELEKMRKQLEQEKS----------EIQSAL 1546
Cdd:COG3096 666 pggaedprllalaERLGgvllsEIyddvtledapyfsalyGPARHaivvpDLSAVKEQLAGLEDcpedlyliegDPDSFD 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1547 EEAEASLEHEEGKILRA---QLEFSQI-------KADIERKL----AEKDEEMEQ------SKRNLQRT----------- 1595
Cdd:COG3096 746 DSVFDAEELEDAVVVKLsdrQWRYSRFpevplfgRAAREKRLeelrAERDELAEQyakasfDVQKLQRLhqafsqfvggh 825
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1596 -IDTLQSSLESETRSRNEALRikkKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTN-EDLKE-- 1671
Cdd:COG3096 826 lAVAFAPDPEAELAALRQRRS---ELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRlEELREel 902
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1672 ---------------NTAIVERRNNLLQ---AELEELRAALEQTERGRKLAEQELLDTSERVQLLH----SQNTSLLNQK 1729
Cdd:COG3096 903 daaqeaqafiqqhgkALAQLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGEN 982
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1730 KKLETdisQLQTEVEEAVQECRNAEEKAKKA---ITDAAMMAEELKKEQDTSAhleRMKKNMEQTIKDLQHRLD-EAEQI 1805
Cdd:COG3096 983 SDLNE---KLRARLEQAEEARREAREQLRQAqaqYSQYNQVLASLKSSRDAKQ---QTLQELEQELEELGVQADaEAEER 1056
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163644331 1806 A---MKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLV 1870
Cdd:COG3096 1057 ArirRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLA 1124
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1752-1933 |
1.71e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1752 NAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAMKGGKKqVQKLEARVRELE---SEV 1828
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREE-LEKLEKEVKELEelkEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1829 ESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLV---DKLQLKVKAYKRaaeeaeeqantnLSKFR-KIQHE 1904
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVkelKELKEKAEEYIK------------LSEFYeEYLDE 308
|
170 180
....*....|....*....|....*....
gi 163644331 1905 LDEAEERADIAESQVNKLRAKSRDVSSKK 1933
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKE 337
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
842-1000 |
2.42e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 842 LKSAEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSL--------LQEKNDLQLQVQAEQDNLCDAEERCDQLIKN 913
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELeaqirgngGDRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 914 ----KIQLEAKAKELTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDD 989
Cdd:COG4913 368 laalGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
170
....*....|.
gi 163644331 990 IIAKLTKEKKA 1000
Cdd:COG4913 448 ALAEALGLDEA 458
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
909-1045 |
2.57e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.39 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 909 QLIKNKIQLEAKA----------KELTERLEDE-EEMNAELTAKKRKLEdECSELKKDIDDLELTL-AKVEKEKHATENK 976
Cdd:smart00787 120 QLVKTFARLEAKKmwyewrmkllEGLKEGLDENlEGLKEDYKLLMKELE-LLNSIKPKLRDRKDALeEELRQLKQLEDEL 198
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644331 977 VKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKK 1045
Cdd:smart00787 199 EDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1050-1204 |
2.60e-04 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 45.90 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1050 LERAKRKLEGDLKLTQESLMDLENDKQQLEERLKkkdfEISQLNGKIEDEQTiciQLQKKLKELQARieeleeeleaera 1129
Cdd:COG1193 502 IERARELLGEESIDVEKLIEELERERRELEEERE----EAERLREELEKLRE---ELEEKLEELEEE------------- 561
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 163644331 1130 ARAKVEKQRADLARELEEISERLEEaggaTAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQADSVAE 1204
Cdd:COG1193 562 KEEILEKAREEAEEILREARKEAEE----LIRELREAQAEEEELKEARKKLEELKQELEEKLEKPKKKAKPAKPP 632
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1073-1238 |
3.05e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1073 NDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERL 1152
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1153 EEAGG-----ATAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQADSVAELGEQIDNLQRVKQKLEKEKSELR 1227
Cdd:COG1579 83 GNVRNnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|.
gi 163644331 1228 LELDDVVSNME 1238
Cdd:COG1579 163 AEREELAAKIP 173
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1596-1765 |
3.25e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1596 IDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDdSLRTNEDLKEntai 1675
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG-NVRNNKEYEA---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1676 verrnnlLQAELEELraaleqtERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEE 1755
Cdd:COG1579 94 -------LQKEIESL-------KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|
gi 163644331 1756 KAKKAITDAA 1765
Cdd:COG1579 160 ELEAEREELA 169
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1630-1834 |
3.47e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 44.25 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1630 QLSQANRQAAEAQKQLKSVHAHMKDA-----------QLQLDDSLRTNEDLKENTAiverrnnllqaELEELRAALEQTE 1698
Cdd:pfam00261 9 ELDEAEERLKEAMKKLEEAEKRAEKAeaevaalnrriQLLEEELERTEERLAEALE-----------KLEEAEKAADESE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1699 RGRKLAEQELLDTSERVQLLHSQntslLNQKKKLETDISQLQTEVEEAV----QECRNAEEKAKKAITDAAMMAEELKKE 1774
Cdd:pfam00261 78 RGRKVLENRALKDEEKMEILEAQ----LKEAKEIAEEADRKYEEVARKLvvveGDLERAEERAELAESKIVELEEELKVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163644331 1775 QDTSAHLE-------RMKKNMEQTIKDLQHRLDEAEQIAMKGgKKQVQKLEARVRELESEVESEQKK 1834
Cdd:pfam00261 154 GNNLKSLEaseekasEREDKYEEQIRFLTEKLKEAETRAEFA-ERSVQKLEKEVDRLEDELEAEKEK 219
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1539-1757 |
3.96e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1539 KSEIQSALEEA-EASLEHEEGKILRAQLEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEalriK 1617
Cdd:COG4717 36 KSTLLAFIRAMlLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE----L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1618 KKMEGDLNEMEIQLsqanrQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKEntaiVERRNNLLQAELEELRAALEQT 1697
Cdd:COG4717 112 EELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEEL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 163644331 1698 ERGRKLA-EQELLDTSERVQllhsqntSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKA 1757
Cdd:COG4717 183 LEQLSLAtEEELQDLAEELE-------ELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
926-1178 |
4.01e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 926 ERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAAL----DDIIAKLTKEKKAL 1001
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELrekrDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1002 QEAHQQ------TLDDLQSEEDKVNTLTKAKAKLEQQVDDLEG-------SLEQEKKLRMDLERAKRKLEGDLKL--TQE 1066
Cdd:COG1340 81 DELNEKlnelreELDELRKELAELNKAGGSIDKLRKEIERLEWrqqtevlSPEEEKELVEKIKELEKELEKAKKAleKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1067 SLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELE 1146
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 163644331 1147 EISERL------EEAGGATAAQIEMNKKREAEFQKLRR 1178
Cdd:COG1340 241 ELRKELkklrkkQRALKREKEKEELEEKAEEIFEKLKK 278
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1524-1763 |
4.17e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.21 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1524 SIHELEKmRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQlEFSQIKADIERKLaekdeemeqskRNLQRTIDTLQSSL 1603
Cdd:pfam12795 1 KLDELEK-AKLDEAAKKKLLQDLQQALSLLDKIDASKQRAA-AYQKALDDAPAEL-----------RELRQELAALQAKA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1604 ESETRSRNEALRIK------KKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDD-SLRTNEDLKENTAIV 1676
Cdd:pfam12795 68 EAAPKEILASLSLEeleqrlLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQiRNRLNGPAPPGEPLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1677 ERRNNLLQAELEELRAALEQTergrklaEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEV-----EEAVQECR 1751
Cdd:pfam12795 148 EAQRWALQAELAALKAQIDML-------EQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLnekrlQEAEQAVA 220
|
250
....*....|..
gi 163644331 1752 NAEEKAKKAITD 1763
Cdd:pfam12795 221 QTEQLAEEAAGD 232
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1167-1322 |
4.39e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 45.44 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1167 KKREAEFQKLRRDLEEATLQheATAATLRKKQADS-VAELGEQIDNLqrvkqkleKEKSELRLEldDVVSNmehvvKTKa 1245
Cdd:pfam05911 20 EKAEAEALALKQQLESVTLQ--KLTAEERAAHLDGaLKECMQQLRNV--------KEEQEQKIH--DVVLK-----KTK- 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163644331 1246 NLEKMTRSLEDQMNEYktkyeeGQRCIndftmqksKLQSENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLE 1322
Cdd:pfam05911 82 EWEKIKAELEAKLVET------EQELL--------RAAAENDALSRSLQERENLLMKLSEEKSQAEAEIEALKSRLE 144
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
933-1237 |
5.06e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 933 EMNAELTAKKRkledecsELKKDIDDLELTLAKVEkEKHATENKvkNLTEEMAALDDIIAkltkEKKALQEAHQQTLDDL 1012
Cdd:PHA02562 167 EMDKLNKDKIR-------ELNQQIQTLDMKIDHIQ-QQIKTYNK--NIEEQRKKNGENIA----RKQNKYDELVEEAKTI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1013 QSEEDKVNTltkAKAKLEQQVDDLEGSLeqeKKLRMDLERAKRKLEgdlKLTQESLMDLEND-----KQQleerlkkkdf 1087
Cdd:PHA02562 233 KAEIEELTD---ELLNLVMDIEDPSAAL---NKLNTAAAKIKSKIE---QFQKVIKMYEKGGvcptcTQQ---------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1088 eISQLNGKIEDEQTICIQLQKKLKELQARIeeleeeleaerAARAKVEKQRADLARELEEISERLEEAGGATAAQIEMNK 1167
Cdd:PHA02562 294 -ISEGPDRITKIKDKLKELQHSLEKLDTAI-----------DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAK 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1168 KREAEFQKLRRDleeatlqheataatlRKKQADSVAELGEQIDNLQRVKQKLEKEKSELrleldDVVSNM 1237
Cdd:PHA02562 362 KVKAAIEELQAE---------------FVDNAEELAKLQDELDKIVKTKSELVKEKYHR-----GIVTDL 411
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1398-1587 |
5.07e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1398 RLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELES--SQKE 1475
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1476 ARCLSTELfklknsyeealdhlETMKRENKNLQEEISDLTEQLgeggksihelekmrkqleqekSEIQSALEEAEASLEH 1555
Cdd:COG1579 91 YEALQKEI--------------ESLKRRISDLEDEILELMERI---------------------EELEEELAELEAELAE 135
|
170 180 190
....*....|....*....|....*....|..
gi 163644331 1556 EEGKILRAQLEFSQIKADIERKLAEKDEEMEQ 1587
Cdd:COG1579 136 LEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
866-1081 |
5.28e-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: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 866 AKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDqliknkiQLEAKAKELTERLedeEEMNAELTAKKRKL 945
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-------ALQAEIDKLQAEI---AEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 946 EDECSELKK---DIDDLELTLAkvekekhATE-----NKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEED 1017
Cdd:COG3883 89 GERARALYRsggSVSYLDVLLG-------SESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 163644331 1018 KVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEER 1081
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
844-1610 |
5.30e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 844 SAEAEKEMANMKDEfaklkeayaksEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAKE 923
Cdd:pfam10174 38 SPELKKERALRKEE-----------AARISVLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGED 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 924 LTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELtlaKVEKEKHAtenkvknlteeMAALDDIIAKLtkekkaLQE 1003
Cdd:pfam10174 107 KFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMEL---RIETQKQT-----------LGARDESIKKL------LEM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1004 AHQQTLDDLQSEEDkvNTLTKAKAKLEQQVDDLEGSLEQEKKlrmdlerakrklegdlkltqeslmdlENdkQQLEERLK 1083
Cdd:pfam10174 167 LQSKGLPKKSGEED--WERTRRIAEAEMQLGHLEVLLDQKEK--------------------------EN--IHLREELH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1084 KKdFEISQLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEE-------ISERLEEag 1156
Cdd:pfam10174 217 RR-NQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVykshskfMKNKIDQ-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1157 gataAQIEMNKKrEAEFQKLRRDLE--------------------------EATLQHEATAATLRKKQADSVaeLGEQID 1210
Cdd:pfam10174 294 ----LKQELSKK-ESELLALQTKLEtltnqnsdckqhievlkesltakeqrAAILQTEVDALRLRLEEKESF--LNKKTK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1211 NLQRvkqkLEKEKSELRLELDDvVSNMEHVVKTKAN-LEKMTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKLQSENGEL 1289
Cdd:pfam10174 367 QLQD----LTEEKSTLAGEIRD-LKDMLDVKERKINvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTL 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1290 SRQLEEKDSLVSQLtrskmsyTQQIEDLKRQLEEETKaksALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSE 1369
Cdd:pfam10174 442 EEALSEKERIIERL-------KEQREREDRERLEELE---SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASS 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1370 VAQWRTKYETDAIQRTEELEEAKK-----KLAQRLQETEEAVEAVNAKCSSLEK-------TKHRLQNEIEDLMVDLERS 1437
Cdd:pfam10174 512 GLKKDSKLKSLEIAVEQKKEECSKlenqlKKAHNAEEAVRTNPEINDRIRLLEQevarykeESGKAQAEVERLLGILREV 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1438 NAAAAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELFklknsyEEALDHLETMKRENKNLQeeisdLTEQ 1517
Cdd:pfam10174 592 ENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLL------EEARRREDNLADNSQQLQ-----LEEL 660
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1518 LGEGGKSIHELEKMRKQLeqekSEIQSALEEAEA---SLEHEEGKILRAQLEFSQikadiERKLA---EKDE-----EME 1586
Cdd:pfam10174 661 MGALEKTRQELDATKARL----SSTQQSLAEKDGhltNLRAERRKQLEEILEMKQ-----EALLAaisEKDAniallELS 731
|
810 820 830
....*....|....*....|....*....|..
gi 163644331 1587 QSKRN--------LQRTIDTLQSSLESETRSR 1610
Cdd:pfam10174 732 SSKKKktqeevmaLKREKDRLVHQLKQQTQNR 763
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1727-1928 |
6.20e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1727 NQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIA 1806
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1807 mkggKKQVQKLEARVRELES-------EVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKA 1879
Cdd:COG4942 100 ----EAQKEELAELLRALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 163644331 1880 YKRAAEEAEEQANTNLSKFRKIQHELDEAEERADIAESQVNKLRAKSRD 1928
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
872-1032 |
6.64e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 872 RKELEEKMVSLLQEKNDLQLQvQAEQDnlcdAEErcdqlIKNKIQLEAK--AKELTERLEDE-EEMNAELTAKKRKLEDE 948
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE-EAKKE----AEA-----IKKEALLEAKeeIHKLRNEFEKElRERRNELQKLEKRLLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 949 CSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAkltKEKKALQEAHQqtlddLQSEEDKVNTLTKAKAK 1028
Cdd:PRK12704 95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIE---EQLQELERISG-----LTAEEAKEILLEKVEEE 166
|
....
gi 163644331 1029 LEQQ 1032
Cdd:PRK12704 167 ARHE 170
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
845-1097 |
6.65e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.46 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 845 AEAEKEMANMKDEFAKLKEAYAKS---EARR--KELEEKMVSLLQEKNDL-QLQVQAEQ---DNLCDAEERCDQLIKNKI 915
Cdd:pfam06160 149 DELEKQLAEIEEEFSQFEELTESGdylEAREvlEKLEEETDALEELMEDIpPLYEELKTelpDQLEELKEGYREMEEEGY 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 916 QLEakAKELTERLEDEEEMNAELTAKKRKLE-DECSELKKDIDDLELTLAKV-EKEKHATENKVKNLTEemaaLDDIIAK 993
Cdd:pfam06160 229 ALE--HLNVDKEIQQLEEQLEENLALLENLElDEAEEALEEIEERIDQLYDLlEKEVDAKKYVEKNLPE----IEDYLEH 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 994 LTKEKKALQE-----AHQQTLDDlqSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKK----LRMDLERAKRKLEG---DL 1061
Cdd:pfam06160 303 AEEQNKELKEelervQQSYTLNE--NELERVRGLEKQLEELEKRYDEIVERLEEKEVayseLQEELEEILEQLEEieeEQ 380
|
250 260 270
....*....|....*....|....*....|....*.
gi 163644331 1062 KLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIE 1097
Cdd:pfam06160 381 EEFKESLQSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1572-1790 |
6.70e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.83 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1572 ADIERklAEKDEE-MEQSKRNLQRTIDTLQSSLESE---------TRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEA 1641
Cdd:NF012221 1562 ADKER--AEADRQrLEQEKQQQLAAISGSQSQLESTdqnaletngQAQRDAILEESRAVTKELTTLAQGLDALDSQATYA 1639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1642 QKQLKSVHAH-----MKDAQLQLDDSlrtneDLKENTAIVERRNNlLQAELEELRAALEQTERGRKLAEQELLDTservq 1716
Cdd:NF012221 1640 GESGDQWRNPfagglLDRVQEQLDDA-----KKISGKQLADAKQR-HVDNQQKVKDAVAKSEAGVAQGEQNQANA----- 1708
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 163644331 1717 llhsqntsllnqkkklETDISQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ 1790
Cdd:NF012221 1709 ----------------EQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ 1766
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1571-1858 |
7.27e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.73 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1571 KADIERKLAEKDEEMEQSKrnlqrtIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKsvha 1650
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQER------LRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELE---- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1651 hmkdaQLQLDDSLRTNEDLKENTAIVE---------------RRNNLLQAELEELRA-ALEQTERGRKLAEQELLDTSER 1714
Cdd:pfam17380 352 -----RIRQEERKRELERIRQEEIAMEisrmrelerlqmerqQKNERVRQELEAARKvKILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1715 VQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQEC-----RNAEEKAKKAITDA-------------AMMAEELKKEQD 1776
Cdd:pfam17380 427 AEQEEARQREVRRLEEERAREMERVRLEEQERQQQVerlrqQEEERKRKKLELEKekrdrkraeeqrrKILEKELEERKQ 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1777 TSAHLERMKKNMEQTIKDLQHRLDEAEQ--IAMKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTY 1854
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEERQKAIYEEERrrEAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK 586
|
....
gi 163644331 1855 QTEE 1858
Cdd:pfam17380 587 ARAE 590
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1340-1518 |
8.36e-04 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 44.27 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1340 HDTDLLREQYEEEQE-AKAELQRgmsKANSEVAQwRTKYETDaIQRTEE----LEEAKKKLAQRLQETEEAVEAVNAKCS 1414
Cdd:pfam10168 539 RATQVFREEYLKKHDlAREEIQK---RVKLLKLQ-KEQQLQE-LQSLEEerksLSERAEKLAEKYEEIKDKQEKLMRRCK 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1415 SLektkHRLQNEIEDLMVDLERSNAAA-AALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARclstelfklKNSYEEA 1493
Cdd:pfam10168 614 KV----LQRLNSQLPVLSDAEREMKKElETINEQLKHLANAIKQAKKKMNYQRYQIAKSQSIRK---------KSSLSLS 680
|
170 180
....*....|....*....|....*
gi 163644331 1494 LDHLETMKRENKNLQEEISDLTEQL 1518
Cdd:pfam10168 681 EKQRKTIKEILKQLGSEIDELIKQV 705
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1704-1882 |
8.57e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1704 AEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT-SAHLE 1782
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1783 RMKKNMEQT-----------IKDLQHRLDEAEQIaMKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKE 1851
Cdd:COG3883 94 ALYRSGGSVsyldvllgsesFSDFLDRLSALSKI-ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190
....*....|....*....|....*....|.
gi 163644331 1852 LTYQTEEDRKNLARLQDLVDKLQLKVKAYKR 1882
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
893-1061 |
8.57e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 893 VQAEQDNLCDAEERCDQLIKNKIQLEAKAKELTERLEDEEEMNAELTAKKRKLED---ECSELKKDIDDLELTLAKVEKE 969
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 970 -KHATENK-VKNLTEEMAALDDIIAKLTKEKKALQ---EAHQQTLDDLQSE-EDKVNTLTKAKAKLEQQVDDLEgslEQE 1043
Cdd:COG1579 82 lGNVRNNKeYEALQKEIESLKRRISDLEDEILELMeriEELEEELAELEAElAELEAELEEKKAELDEELAELE---AEL 158
|
170
....*....|....*...
gi 163644331 1044 KKLRMDLERAKRKLEGDL 1061
Cdd:COG1579 159 EELEAEREELAAKIPPEL 176
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1495-1938 |
8.87e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.13 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1495 DHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSAL--------EEAEASLEHEEGKILRAQLE 1566
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1567 FSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLK 1646
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1647 SVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLL 1726
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1727 NQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIA 1806
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1807 MKGGKKQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKAYKRAAEE 1886
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 163644331 1887 AEEQANTNLSKFRKIQHELDEAEERADIAESQVNKLRAKSRDVSSKKGHDQE 1938
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALAS 527
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
860-1000 |
8.92e-04 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 43.60 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 860 KLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAeercdQLIKNKI-QLEAKAKELTERLEdeeEMNAEL 938
Cdd:pfam10186 23 ELRVDLARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKL-----RLLKSEVaISNERLNEIKDKLD---QLRREI 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 163644331 939 TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKA 1000
Cdd:pfam10186 95 AEKKKKIEKLRSSLKQRRSDLESASYQLEERRASQLAKLQNSIKRIKQKWTALHSKTAESRS 156
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1194-1449 |
1.31e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1194 LRKKQADSVAE-LGEQIDNLQRVKQKLEKEKSELRLELDDVvsnmehvvktkaNLEKMTRSLEDQMNEYKTKYEEGQrci 1272
Cdd:COG3206 168 LRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGLV------------DLSEEAKLLLQQLSELESQLAEAR--- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1273 ndftMQKSKLQSENGELSRQLEEKDSLVSQLTRSKM--SYTQQIEDLKRQLEEETKAKSALAHAVQSARhdtdllREQYE 1350
Cdd:COG3206 233 ----AELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAELSARYTPNHPDVIALR------AQIAA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1351 EEQEAKAELQRGMSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQETEEAVEAVNAKcsslektkhrlQNEIEDL 1430
Cdd:COG3206 303 LRAQLQQEAQRILASLEAEL---------------EALQAREASLQAQLAQLEARLAELPEL-----------EAELRRL 356
|
250
....*....|....*....
gi 163644331 1431 MVDLERSNAAAAALDKKQR 1449
Cdd:COG3206 357 EREVEVARELYESLLQRLE 375
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
1145-1363 |
1.33e-03 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 43.80 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1145 LEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLrkKQADSVAE-LGEQIDNLQRVKQKLEKEK 1223
Cdd:PRK15374 101 LSQLESRLAVWQAMIESQKEMGIQVSKEFQTALGEAQEATDLYEASIKKT--DTAKSVYDaAEKKLTQAQNKLQSLDPAD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1224 SELRLELDDVVSNMEHVVKTKANLEKMTRSLEDQMNEYKTKyeeGQRCINDFTMQKSKLQSENGELSRQLEEKDslVSQL 1303
Cdd:PRK15374 179 PGYAQAEAAVEQAGKEATEAKEALDKATDATVKAGTDAKAK---AEKADNILTKFQGTANAASQNQVSQGEQDN--LSNV 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 163644331 1304 TRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQSARH-DTDLLREQYEEEQEAKAELQRGM 1363
Cdd:PRK15374 254 ARLTMLMAMFIEIVGKNTEESLQNDLALFNALQEGRQaEMEKKSAEFQEETRKAEETNRIM 314
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1280-1476 |
1.49e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1280 SKLQSENGELSRQLEEKDSLVSQLTrskmSYTQQIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAEL 1359
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELD----ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1360 QRGMSKANSEVAQWRTKYE----TDAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKhrlqNEIEDLMVDLE 1435
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL----AELEALKAELE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 163644331 1436 RSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEA 1476
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
982-1861 |
1.54e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 982 EEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEED---KVNTLTKAKAKLEQQVDDLEgsleqekklrmdlerakrKLE 1058
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhlnLVQTALRQQEKIERYQEDLE------------------ELT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1059 GDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIED-------EQTICIQLQKKLKELQarieeleeeleaeraaR 1131
Cdd:COG3096 361 ERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADyqqaldvQQTRAIQYQQAVQALE----------------K 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1132 AKVEKQRADLAreLEEISERLEEAggATAAQIEMNKKREAEfQKLRrDLEEATLQHEATAATLRK-------KQADSVA- 1203
Cdd:COG3096 425 ARALCGLPDLT--PENAEDYLAAF--RAKEQQATEEVLELE-QKLS-VADAARRQFEKAYELVCKiageverSQAWQTAr 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1204 ELGEQIDNLQRVKQKLEkeksELRLELDDvvsnMEHVVKTKANLEKMTRSLEDQMNEYKTKYEEgqrcindFTMQKSKLQ 1283
Cdd:COG3096 499 ELLRRYRSQQALAQRLQ----QLRAQLAE----LEQRLRQQQNAERLLEEFCQRIGQQLDAAEE-------LEELLAELE 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1284 SENGELSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAKSALAHavqsarhdtdlLREQYEEEQEAKAELQRGM 1363
Cdd:COG3096 564 AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALER-----------LREQSGEALADSQEVTAAM 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1364 SKAnsevaqwrtkyetdaIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSS----LEKTKHRLQNE----------IED 1429
Cdd:COG3096 633 QQL---------------LEREREATVERDELAARKQALESQIERLSQPGGAedprLLALAERLGGVllseiyddvtLED 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1430 ---------------LMVDLErsnAAAAALDKKQRNFDKVL--SEWKQKFEESQAELESsQKEARCLSTELFKLKNSYEE 1492
Cdd:COG3096 698 apyfsalygparhaiVVPDLS---AVKEQLAGLEDCPEDLYliEGDPDSFDDSVFDAEE-LEDAVVVKLSDRQWRYSRFP 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1493 ALDHLETMKRENK--NLQEEISDLTEQLGEGGKSIHELEKMRKQLEQ----------------EKSEIQSALEEAEASLE 1554
Cdd:COG3096 774 EVPLFGRAAREKRleELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgghlavafapdpeaELAALRQRRSELERELA 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1555 HEEGKILRAQLEFSQIKADIE--RKLAE-----KDEEMEQSKRNLQRTIDTLQSSlESETRSRNEALRIKKKMEGDLN-- 1625
Cdd:COG3096 854 QHRAQEQQLRQQLDQLKEQLQllNKLLPqanllADETLADRLEELREELDAAQEA-QAFIQQHGKALAQLEPLVAVLQsd 932
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1626 -EMEIQLSQANRQAAEAQKQLKSVHAHMKD-----AQLQLDDSlrtNEDLKENTAIVERrnnllqaeleeLRAALEQter 1699
Cdd:COG3096 933 pEQFEQLQADYLQAKEQQRRLKQQIFALSEvvqrrPHFSYEDA---VGLLGENSDLNEK-----------LRARLEQ--- 995
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1700 grklAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQEcrnAEEKAKKAITDAAMMAEELKKEQDTSA 1779
Cdd:COG3096 996 ----AEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQE---LEELGVQADAEAEERARIRRDELHEEL 1068
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1780 HLERMKKNmeQTIKDLQHRldEAEqiaMKGGKKQVQKLEARVRELESEVESeQKKSSEAVKGIRK---YERRI--KELTY 1854
Cdd:COG3096 1069 SQNRSRRS--QLEKQLTRC--EAE---MDSLQKRLRKAERDYKQEREQVVQ-AKAGWCAVLRLARdndVERRLhrRELAY 1140
|
....*..
gi 163644331 1855 QTEEDRK 1861
Cdd:COG3096 1141 LSADELR 1147
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1677-1934 |
1.55e-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: 43.21 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1677 ERRNNLLQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEK 1756
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1757 AKKAITDAAMMAE----ELKKEQDTSAHLERMKKNMEQTIkdlQHRLDEAEQIamkggKKQVQKLEARVRELESEveseq 1832
Cdd:COG4942 106 LAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLA---PARREQAEEL-----RADLAELAALRAELEAE----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1833 kksseavkgirkyerrIKELTYQTEEDRKNLARLQDLVDKLQLKVKAYKRAAEEAEEQANTNLSKFRKIQHELDEAEERA 1912
Cdd:COG4942 173 ----------------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250 260
....*....|....*....|..
gi 163644331 1913 DIAESqvnklRAKSRDVSSKKG 1934
Cdd:COG4942 237 AAAAE-----RTPAAGFAALKG 253
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1455-1635 |
1.56e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.82 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1455 LSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEaldhletmkrENKNLQEEISDLTEQLGEGGKSIHELEKmrkQ 1534
Cdd:pfam09787 49 LEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQE----------EAESSREQLQELEEQLATERSARREAEA---E 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1535 LEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIKADIERKL--AEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNE 1612
Cdd:pfam09787 116 LERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSqsSSSQSELENRLHQLTETLIQKQTMLEALSTEKNS 195
|
170 180
....*....|....*....|...
gi 163644331 1613 ALRIKKKMEGDLNemEIQLSQAN 1635
Cdd:pfam09787 196 LVLQLERMEQQIK--ELQGEGSN 216
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1701-1938 |
1.63e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1701 RKLAEQELLDTSE---RVQLLHSQntsLLNQKKKLETDISQ------LQTEVEEAVQECRNAEEKAKKAitDAAMMAEEL 1771
Cdd:COG1196 174 KEEAERKLEATEEnleRLEDILGE---LERQLEPLERQAEKaeryreLKEELKELEAELLLLKLRELEA--ELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1772 KKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiamkggkkQVQKLEARVRELESEVESEQKKSSEAVKGIRKYERRIKE 1851
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELEL--------ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1852 LTYQTEEDRKNLARLQDLVDKLQLKVKAYKRAAEEAEEQANTNLSKFRKIQHELDEAEERADIAESQVNKLRAKSRDVSS 1931
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
....*..
gi 163644331 1932 KKGHDQE 1938
Cdd:COG1196 401 QLEELEE 407
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1383-1749 |
1.68e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1383 QRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKF 1462
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1463 EESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEI 1542
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1543 QSALEEAEASLEHEEGKILRAQLEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEG 1622
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1623 DLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTERGRK 1702
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 163644331 1703 LAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQE 1749
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1543-1699 |
1.69e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.80 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1543 QSALEEAEASLEHEEGKILRAQLEFSQIkadierklaekdEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEG 1622
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRL------------QALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1623 DLNEMEI----------QLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAI-VERRNNLLQAELEELR 1691
Cdd:pfam00529 125 DLARRRVlapiggisreSLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSgAQLQIAEAEAELKLAK 204
|
....*...
gi 163644331 1692 AALEQTER 1699
Cdd:pfam00529 205 LDLERTEI 212
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1438-1687 |
1.72e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.40 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1438 NAAAAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTEL-------FKLKNSYEEALDHLETMKRENKNLQEE 1510
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKAtqtlakaQQVNAESERTLGHAKELAEAIKNLIDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1511 ISDLTEQLGEGGKSIHELekmrkqleqEKSEIQSALEEAEASLEHEEGKILRAQLEfsqikadierklaEKDEEMEQSKR 1590
Cdd:pfam06008 98 IKEINEKVATLGENDFAL---------PSSDLSRMLAEAQRMLGEIRSRDFGTQLQ-------------NAEAELKAAQD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1591 NLQRtIDTLQSSLESETRSRNEALRIK-KKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDL 1669
Cdd:pfam06008 156 LLSR-IQTWFQSPQEENKALANALRDSlAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQL 234
|
250
....*....|....*...
gi 163644331 1670 KENtaIVERRNNLLQAEL 1687
Cdd:pfam06008 235 EET--LKTARDSLDAANL 250
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1370-1509 |
1.73e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1370 VAQWRTKYETDA------IQRTEELEeakKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERsnAAAAA 1443
Cdd:PRK00409 504 IEEAKKLIGEDKeklnelIASLEELE---RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK--EAQQA 578
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163644331 1444 LDKKQRNFDKVLSEWKQKFEESQAELESSQ-KEARClstelfKLKNSYEEALDHLETMKRENKNLQE 1509
Cdd:PRK00409 579 IKEAKKEADEIIKELRQLQKGGYASVKAHElIEARK------RLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1351-1640 |
1.77e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.41 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1351 EEQEAKAELQRGMSKANSEVAQWRTKYETDAI----QRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKT------- 1419
Cdd:COG5185 239 QDPESELEDLAQTSDKLEKLVEQNTDLRLEKLgenaESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATesleeql 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1420 -KHRLQNEIEDLMVDLERSNAAA-AALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARC--LSTELFKLKNSYEEAL- 1494
Cdd:COG5185 319 aAAEAEQELEESKRETETGIQNLtAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELdsFKDTIESTKESLDEIPq 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1495 --------------DHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKI 1560
Cdd:COG5185 399 nqrgyaqeilatleDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRS 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1561 LRAqlEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAE 1640
Cdd:COG5185 479 KKE--DLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNA 556
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
963-1096 |
1.95e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 40.76 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 963 LAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQ 1042
Cdd:pfam11559 16 FLRSGLLFDTAEGVEENIARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAK 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 163644331 1043 EKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKI 1096
Cdd:pfam11559 96 ERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAHEVKKRDREIEKLKERL 149
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1599-1829 |
1.99e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1599 LQSSLESETRSRNEALR----IKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTA 1674
Cdd:pfam07888 32 LQNRLEECLQERAELLQaqeaANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1675 IVERRNNLLQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNae 1754
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRS-- 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163644331 1755 ekakkaitdaamMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQ--IAMKGGKKQVQKLEARVRELESEVE 1829
Cdd:pfam07888 190 ------------LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeAENEALLEELRSLQERLNASERKVE 254
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
850-1795 |
2.02e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 850 EMANMKDEFAKLKEAYAKSEARRKEleekmvsllqekndlqlQVQAEQDNLCDaeercdqlIKNKIQLEAKAKELTERLE 929
Cdd:TIGR01612 836 EMKFMKDDFLNKVDKFINFENNCKE-----------------KIDSEHEQFAE--------LTNKIKAEISDDKLNDYEK 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 930 DEEEMNAELTAKKRKLEDECSELKkdiddlelTLAKVE---KEKHATENKVKNLTEEMAALDDIIAK---LTKEKKALQE 1003
Cdd:TIGR01612 891 KFNDSKSLINEINKSIEEEYQNIN--------TLKKVDeyiKICENTKESIEKFHNKQNILKEILNKnidTIKESNLIEK 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1004 AHQQTLDdlqseedkvNTLTKAKAKLEQQVDDLegSLEQEKKLRMDLERAKRKLEGDLKLTQESLMdlendKQQLEERLK 1083
Cdd:TIGR01612 963 SYKDKFD---------NTLIDKINELDKAFKDA--SLNDYEAKNNELIKYFNDLKANLGKNKENML-----YHQFDEKEK 1026
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1084 KkdfeISQLNGKIED--------EQTICIQLQKKLKELQARIEELEEELEAERAARAKVEkqradlARELEEISERLEEA 1155
Cdd:TIGR01612 1027 A----TNDIEQKIEDanknipniEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEIN------ITNFNEIKEKLKHY 1096
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1156 GGATAAQiEMNKKREAEFQKLRRDLEEATLQ---HEATAATLRKKQADSVAELGEQIDNLQRVKqklekekselrlelDD 1232
Cdd:TIGR01612 1097 NFDDFGK-EENIKYADEINKIKDDIKNLDQKidhHIKALEEIKKKSENYIDEIKAQINDLEDVA--------------DK 1161
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1233 VVSNmehvvKTKANLEKMTRSLEDQMNEYKTKYEEGQRCINDFTmqksklqsengelsrQLEEKDSLVSQLTRSKMSYTQ 1312
Cdd:TIGR01612 1162 AISN-----DDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIA---------------EIEKDKTSLEEVKGINLSYGK 1221
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1313 QIEDL-KRQLEEETKAKSALAHAVQSARHDTDLLREQYEE-------EQEAKAELQ------------RGMSKANSE-VA 1371
Cdd:TIGR01612 1222 NLGKLfLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEienemgiEMDIKAEMEtfnishdddkdhHIISKKHDEnIS 1301
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1372 QWRTKYE--TDAIQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQ--------NEIEDLMVDLERSNA-A 1440
Cdd:TIGR01612 1302 DIREKSLkiIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKlnkikkiiDEVKEYTKEIEENNKnI 1381
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1441 AAALDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGE 1520
Cdd:TIGR01612 1382 KDELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEM 1461
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1521 GGKSIHELEKMRKqlEQEKSEIQSALEEAEASLEHEEGkilraqlefSQIKADIERKLAEKDEEM-EQSKRNLQRTIDTL 1599
Cdd:TIGR01612 1462 ADNKSQHILKIKK--DNATNDHDFNINELKEHIDKSKG---------CKDEADKNAKAIEKNKELfEQYKKDVTELLNKY 1530
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1600 qssleSETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVhahmKDAQLQLDDSLRTNEdlKENTAIVERR 1679
Cdd:TIGR01612 1531 -----SALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEI----KKEKFRIEDDAAKND--KSNKAAIDIQ 1599
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1680 NNLLQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNT-----------------SLLNQKKKLETDISQLQtE 1742
Cdd:TIGR01612 1600 LSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTelkengdnlnslqefleSLKDQKKNIEDKKKELD-E 1678
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....
gi 163644331 1743 VEEAVQECRNAEEKAKKAITDAamMAEELKKEQDTSAH-LERMKKNMEQTIKDL 1795
Cdd:TIGR01612 1679 LDSEIEKIEIDVDQHKKNYEIG--IIEKIKEIAIANKEeIESIKELIEPTIENL 1730
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
837-1080 |
2.02e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 837 KIKPLLKSAEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQ 916
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 917 LEAKAKELTERLEDEEEMnAELTAKKRKLEDECSELKKDIDDleltLAKVEKEKhatENKVKNLTEEMAALDdiiAKLTK 996
Cdd:PRK02224 577 LNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREA----LAELNDER---RERLAEKRERKRELE---AEFDE 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 997 EK-KALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERakrklegdLKLTQESLMDLENDK 1075
Cdd:PRK02224 646 ARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREA--------LENRVEALEALYDEA 717
|
....*
gi 163644331 1076 QQLEE 1080
Cdd:PRK02224 718 EELES 722
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1684-1877 |
2.15e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1684 QAELEELRAALEQTErgRKLAEQELLDTSERVQLLHSQNTSllnqKKKLETDISQLQtEVEEAVQECRNAEEKAKKAITD 1763
Cdd:pfam05557 1 RAELIESKARLSQLQ--NEKKQMELEHKRARIELEKKASAL----KRQLDRESDRNQ-ELQKRIRLLEKREAEAEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1764 AAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRL-DEAEQIamkggKKQVQKLEARVRELESEVESEQKKSSEAVKGI 1842
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSEL-----RRQIQRAELELQSTNSELEELQERLDLLKAKA 148
|
170 180 190
....*....|....*....|....*....|....*
gi 163644331 1843 RKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKV 1877
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQE 183
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
835-1873 |
2.19e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.12 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 835 FFKIKPLLK----SAEAEKEMANMKDEFAKLKEAYAKSEarrKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQL 910
Cdd:TIGR01612 1086 FNEIKEKLKhynfDDFGKEENIKYADEINKIKDDIKNLD---QKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKA 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 911 IKNK--IQLEAKAKELTERLEDEEEMNAELtakkRKLEDECSELKKDIDDLE---------------LTLAKVEKEKHAT 973
Cdd:TIGR01612 1163 ISNDdpEEIEKKIENIVTKIDKKKNIYDEI----KKLLNEIAEIEKDKTSLEevkginlsygknlgkLFLEKIDEEKKKS 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 974 ENKVKNLTEEMAALDDIiakltKEKKALQEAHQQTLDDLQSEedkVNTLTKAKAKLEQQVDDLEGSLEQEKKLRmdlera 1053
Cdd:TIGR01612 1239 EHMIKAMEAYIEDLDEI-----KEKSPEIENEMGIEMDIKAE---METFNISHDDDKDHHIISKKHDENISDIR------ 1304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1054 krklEGDLKLTQESL--MDLENDKQQLEERL---KKKDFEISQLNGKIEDEQTICiqlqkKLKELQARIeeleeelEAER 1128
Cdd:TIGR01612 1305 ----EKSLKIIEDFSeeSDINDIKKELQKNLldaQKHNSDINLYLNEIANIYNIL-----KLNKIKKII-------DEVK 1368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1129 AARAKVEKQRADLARELEEiSERLeeaggatAAQIEMNKKREAEFQKLrrdleEATLQHEATAATLRKKQADSVAELGEQ 1208
Cdd:TIGR01612 1369 EYTKEIEENNKNIKDELDK-SEKL-------IKKIKDDINLEECKSKI-----ESTLDDKDIDECIKKIKELKNHILSEE 1435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1209 IDNLQRVKQKLEKEKSEL----RLELDDvvSNMEHVVKTKANleKMTRSLEDQMNEYKTKYEEGQRCINDftMQKSKLQS 1284
Cdd:TIGR01612 1436 SNIDTYFKNADENNENVLllfkNIEMAD--NKSQHILKIKKD--NATNDHDFNINELKEHIDKSKGCKDE--ADKNAKAI 1509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1285 E-NGELSRQLEEKDS----------LVSQLTRSKMSYTQQIEDLKrqleeETKAKSALaHAVQSARHDTDLLREQYEEEQ 1353
Cdd:TIGR01612 1510 EkNKELFEQYKKDVTellnkysalaIKNKFAKTKKDSEIIIKEIK-----DAHKKFIL-EAEKSEQKIKEIKKEKFRIED 1583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1354 EA-------KAELQRGMSKANSE-----VAQWRTKyETDAIQRTEELEEAKKKLAQRLQETE--EAVEAVNAKCSSLEKT 1419
Cdd:TIGR01612 1584 DAakndksnKAAIDIQLSLENFEnkflkISDIKKK-INDCLKETESIEKKISSFSIDSQDTElkENGDNLNSLQEFLESL 1662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1420 KHRLQNeIEDLMVDLERSNAAAAAL----DKKQRNFD-KVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYE-EA 1493
Cdd:TIGR01612 1663 KDQKKN-IEDKKKELDELDSEIEKIeidvDQHKKNYEiGIIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDlEG 1741
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1494 LDHLETMKRENKNLQ---EE-------ISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKilra 1563
Cdd:TIGR01612 1742 IDPNEKLEEYNTEIGdiyEEfielyniIAGCLETVSKEPITYDEIKNTRINAQNEFLKIIEIEKKSKSYLDDIEAK---- 1817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1564 qlEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQK 1643
Cdd:TIGR01612 1818 --EFDRIINHFKKKLDHVNDKFTKEYSKINEGFDDISKSIENVKNSTDENLLFDILNKTKDAYAGIIGKKYYSYKDEAEK 1895
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1644 QLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTERGRKLAEQ--ELLDTSERVQLLH-- 1719
Cdd:TIGR01612 1896 IFINISKLANSINIQIQNNSGIDLFDNINIAILSSLDSEKEDTLKFIPSPEKEPEIYTKIRDSydTLLDIFKKSQDLHkk 1975
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1720 -SQNTSLLNQKKKLETDISQlQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKK----EQDTSAHLERMKKNMEQTIKD 1794
Cdd:TIGR01612 1976 eQDTLNIIFENQQLYEKIQA-SNELKDTLSDLKYKKEKILNDVKLLLHKFDELNKlscdSQNYDTILELSKQDKIKEKID 2054
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1795 LQHRldEAEQIAMKGGKKQV-QKLEARVRELE------SEVESEQKKSSEAVKGIRKYERRIKELT--YQTE----EDRk 1861
Cdd:TIGR01612 2055 NYEK--EKEKFGIDFDVKAMeEKFDNDIKDIEkfennyKHSEKDNHDFSEEKDNIIQSKKKLKELTeaFNTEikiiEDK- 2131
|
1130
....*....|..
gi 163644331 1862 nLARLQDLVDKL 1873
Cdd:TIGR01612 2132 -IIEKNDLIDKL 2142
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1633-1873 |
2.35e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.71 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1633 QANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKE-------NTAIVERRNNLLQAELEE-LRAALEQTERGRKLA 1704
Cdd:pfam05667 216 LAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEqlrsaalAGTEATSGASRSAQDLAElLSSFSGSSTTDTGLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1705 EQELLDTSERVQLLHSQN----------TSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKE 1774
Cdd:pfam05667 296 KGSRFTHTEKLQFTNEAPaatsspptkvETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEEL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1775 QDTSAHLERMKKNMEQT----------IKDLQHRLDEAEQ----IAMKGGKKQVQKLEArVRELESEVESEQKKSSEAVK 1840
Cdd:pfam05667 376 KEQNEELEKQYKVKKKTldllpdaeenIAKLQALVDASAQrlveLAGQWEKHRVPLIEE-YRALKEAKSNKEDESQRKLE 454
|
250 260 270
....*....|....*....|....*....|...
gi 163644331 1841 GIRKYERRIKELTYQTEEDRKNLARLQDLVDKL 1873
Cdd:pfam05667 455 EIKELREKIKEVAEEAKQKEELYKQLVAEYERL 487
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
843-1032 |
2.55e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 843 KSAEAEKEMANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQL---IKNKIQ--- 916
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERreeLGERARaly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 917 ------------LEAK-AKELTERL-------EDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENK 976
Cdd:COG3883 97 rsggsvsyldvlLGSEsFSDFLDRLsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 163644331 977 VKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQ 1032
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
870-1024 |
2.56e-03 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 41.48 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 870 ARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQL---------------IKNKI--------QLEAKAKELTE 926
Cdd:pfam15934 41 ENKNEQEQQLKEFTVQNQRLACQIDNLHETLKDRDHQIKQLqsmitgysdisennrLKEEIhdlkqkncVQARVVRKMGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 927 RLEDEEEMNAELTAKKRKL----EDECSELK---KDIDDLELTLAKVEKEKHATENKVKNLTEEMAALddiiakltKEKK 999
Cdd:pfam15934 121 ELKGQEEQRVELCDKYESLlgsfEEQCQELKranRRVQSLQTRLSQVEKLQEELRTERKILREEVIAL--------KEKD 192
|
170 180
....*....|....*....|....*....
gi 163644331 1000 ALQEAHQQTLDD----LQSEEDKVNTLTK 1024
Cdd:pfam15934 193 AKSNGRERALQDqlkcCQTEIEKSRTLIR 221
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
860-1088 |
2.67e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 860 KLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAKELtERLEDEEEMNAELT 939
Cdd:COG1340 54 ELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEI-ERLEWRQQTEVLSP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 940 AKKRKLEDECSELKKDIDDleltlAKVEKEKHateNKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEEDKV 1019
Cdd:COG1340 133 EEEKELVEKIKELEKELEK-----AKKALEKN---EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEA 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644331 1020 NTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFE 1088
Cdd:COG1340 205 DELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
852-1194 |
2.78e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 852 ANMKDEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQLEAKAKELTERLEDE 931
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 932 EEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAH-QQTLD 1010
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1011 DLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEIS 1090
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1091 QLNGKIEDEQTICIQLQKKLKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATAAQIEMNKKRE 1170
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
330 340
....*....|....*....|....
gi 163644331 1171 AEFQKLRRDLEEATLQHEATAATL 1194
Cdd:COG4372 347 LVGLLDNDVLELLSKGAEAGVADG 370
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1683-1777 |
2.93e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1683 LQAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQEcrnaEEKAKKAIT 1762
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQE----RKQKRKEIT 222
|
90
....*....|....*
gi 163644331 1763 DAAMMAEELkKEQDT 1777
Cdd:PRK11448 223 DQAAKRLEL-SEEET 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
845-1088 |
3.02e-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: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 845 AEAEKEMANMK---DEFAKLKEAYAKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLikNKIQLEAKA 921
Cdd:COG4913 671 AELEAELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDLARLELR 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 922 KELTERLEDEEEMNAELTAKKRkLEDECSELKKDIDDLELTLAKVEKE-KHATENKVKNLTEEMAALDDIIAKLT----- 995
Cdd:COG4913 749 ALLEERFAAALGDAVERELREN-LEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLDrleed 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 996 -------KEKKALQEAHQQTLDDLQSEedkvntLTKAKAKLEQQVDDLEGSLEQ-----EKKLRMDLERAKRKlegDLKL 1063
Cdd:COG4913 828 glpeyeeRFKELLNENSIEFVADLLSK------LRRAIREIKERIDPLNDSLKRipfgpGRYLRLEARPRPDP---EVRE 898
|
250 260
....*....|....*....|....*
gi 163644331 1064 TQESLMDLENDKQQLEERLKKKDFE 1088
Cdd:COG4913 899 FRQELRAVTSGASLFDEELSEARFA 923
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1508-1660 |
3.03e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1508 QEEISDLTEQLGEggkSIHELEKMRKQLEQEKSEIQSALEEAEasleheegkilraqlefsQIKADIERKLAEKDEEMEQ 1587
Cdd:PRK00409 508 KKLIGEDKEKLNE---LIASLEELERELEQKAEEAEALLKEAE------------------KLKEELEEKKEKLQEEEDK 566
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 163644331 1588 SKRNLQRTIdtlqsslesetrsrNEALRIKKKmEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLD 1660
Cdd:PRK00409 567 LLEEAEKEA--------------QQAIKEAKK-EADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKE 624
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1481-1707 |
3.22e-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: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1481 TELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLeheeGKI 1560
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL----GER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1561 LRAQLEFSQIKADIE------------------RKLAEKDEEMEQSKRNLQRTIDTLQSSLESEtrsrnealriKKKMEG 1622
Cdd:COG3883 92 ARALYRSGGSVSYLDvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAK----------LAELEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1623 DLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAELEELRAALEQTERGRK 1702
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
....*
gi 163644331 1703 LAEQE 1707
Cdd:COG3883 242 AAASA 246
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1269-1612 |
3.24e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.73 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1269 QRCINDFTMQKSKLQSE--------NGELSRQLEEKDSLVSQLTR-----------SKMSYTQQIEDLKRQLEEETKAKS 1329
Cdd:PTZ00108 998 EYLLGKLERELARLSNKvrfikhviNGELVITNAKKKDLVKELKKlgyvrfkdiikKKSEKITAEEEEGAEEDDEADDED 1077
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1330 ALAHAVQSARHD-------TDLLREQYE--EEQEAKAELQRGMSKANSEVAQWRTKYET--DAIQRTEELEEAKKKLAQR 1398
Cdd:PTZ00108 1078 DEEELGAAVSYDyllsmpiWSLTKEKVEklNAELEKKEKELEKLKNTTPKDMWLEDLDKfeEALEEQEEVEEKEIAKEQR 1157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1399 LQETEEAVEAVNAKCSSLEKTKHRLQNE------IEDLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKFEESQAELESS 1472
Cdd:PTZ00108 1158 LKSKTKGKASKLRKPKLKKKEKKKKKSSadkskkASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKK 1237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1473 QKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQlgeggksihELEKMRKQLEQEKSEIQSALEEAEAS 1552
Cdd:PTZ00108 1238 SSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQ---------YSPPPPSKRPDGESNGGSKPSSPTKK 1308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1553 LEHEEGKILRAQLEFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNE 1612
Cdd:PTZ00108 1309 KVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDD 1368
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1323-1605 |
3.50e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1323 EETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAE--LQRGMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLaQRLQ 1400
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEvlIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQL-QELK 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1401 ETEEAVEAVNAKCSSLEKTKHRLQNEIE-DLMVDLERSNAAAAALDKKQRNFDKVLSEWKQKfeESQAELESSQKEARCL 1479
Cdd:COG5022 889 IDVKSISSLKLVNLELESEIIELKKSLSsDLIENLEFKTELIARLKKLLNNIDLEEGPSIEY--VKLPELNKLHEVESKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1480 STELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKsiheLEKMRKQLEQEKSEIQSAleEAEASLEHEEGK 1559
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGA----LQESTKQLKELPVEVAEL--QSASKIISSEST 1040
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 163644331 1560 ILRAQLEFSQIKADIERKLAEKDEEMEQSK--RNLQRTIDTLQSSLES 1605
Cdd:COG5022 1041 ELSILKPLQKLKGLLLLENNQLQARYKALKlrRENSLLDDKQLYQLES 1088
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1137-1924 |
3.57e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1137 QRADLARELEEISERLEEAGGAT--AAQIEMNKKR---EAEFQKLRRDLEEATLQHEATAATLRKKQADSVAELGEQIDN 1211
Cdd:NF041483 365 QLAKAARTAEEVLTKASEDAKATtrAAAEEAERIRreaEAEADRLRGEAADQAEQLKGAAKDDTKEYRAKTVELQEEARR 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1212 LQRVKQKL--------EKEKSELRLElddVVSNMEHVVKTKANLEKMTRSLEDQMNEYKTKyeEGQRCINDFTMQKSKLQ 1283
Cdd:NF041483 445 LRGEAEQLraeavaegERIRGEARRE---AVQQIEEAARTAEELLTKAKADADELRSTATA--ESERVRTEAIERATTLR 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1284 SENGE-LSRQLEEKDSLVSQLTRSKMSYTQQIEDLKRQLEEETKAksalAHAVQSARHDTDLLREQYEEEQ--------- 1353
Cdd:NF041483 520 RQAEEtLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETER----AIAARQAEAAEELTRLHTEAEErltaaeeal 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1354 -EAKAELQRGMSKANSEVAQWRTkyetDAIQRTEELEEAKKKLAQRLQeTEEAVEAVNAKC----------SSLEKTKHR 1422
Cdd:NF041483 596 aDARAEAERIRREAAEETERLRT----EAAERIRTLQAQAEQEAERLR-TEAAADASAARAegenvavrlrSEAAAEAER 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1423 LQNEIEDlMVDLERSNAAAAA----------LDKKQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELF-----KLK 1487
Cdd:NF041483 671 LKSEAQE-SADRVRAEAAAAAervgteaaeaLAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasarkRVE 749
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1488 NSYEEALDHLETMKRENKNL-----------QEEISDLTEQLGE---GGKSI--HELEKMRKQLEQEKSEIQS-ALEEAE 1550
Cdd:NF041483 750 EAQAEAQRLVEEADRRATELvsaaeqtaqqvRDSVAGLQEQAEEeiaGLRSAaeHAAERTRTEAQEEADRVRSdAYAERE 829
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1551 ASLEHEEGKILRAQLEFSQIKADIERKLAEKDEEME--------QSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEG 1622
Cdd:NF041483 830 RASEDANRLRREAQEETEAAKALAERTVSEAIAEAErlrsdaseYAQRVRTEASDTLASAEQDAARTRADAREDANRIRS 909
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1623 DlnemeiQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLK--ENTAIVERRNNLLQAELEELRAALEQTERG 1700
Cdd:NF041483 910 D------AAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVraDAAAQAEQLIAEATGEAERLRAEAAETVGS 983
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1701 RKLAEQELLDTSERVqllhsqntsllnqKKKLETDISQLQTEV-EEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSA 1779
Cdd:NF041483 984 AQQHAERIRTEAERV-------------KAEAAAEAERLRTEArEEADRTLDEARKDANKRRSEAAEQADTLITEAAAEA 1050
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1780 hlermKKNMEQTIKDLQHRLDEAEQIA--MKG-GKKQVQKL--EARVrELESEVESEQKKSSEAVKGIRKYERRIKElty 1854
Cdd:NF041483 1051 -----DQLTAKAQEEALRTTTEAEAQAdtMVGaARKEAERIvaEATV-EGNSLVEKARTDADELLVGARRDATAIRE--- 1121
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1855 QTEEDRKNL----------ARLQ---------DLVDKL---------QLKVKAYKRAAEEAEEQANTNLSKFRKIQHELD 1906
Cdd:NF041483 1122 RAEELRDRItgeieelherARREsaeqmksagERCDALvkaaeeqlaEAEAKAKELVSDANSEASKVRIAAVKKAEGLLK 1201
|
890
....*....|....*...
gi 163644331 1907 EAEERADIAESQVNKLRA 1924
Cdd:NF041483 1202 EAEQKKAELVREAEKIKA 1219
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1313-1552 |
3.66e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1313 QIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYEtdaiQRTEELeeak 1392
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE----ERREEL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1393 KKLAQRLQETEEAVEAVNA------------KCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKqrnfdkvlsewKQ 1460
Cdd:COG3883 89 GERARALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAK-----------LA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1461 KFEESQAELESSQKEARclstelfKLKNSYEEALDHLETmkrENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKS 1540
Cdd:COG3883 158 ELEALKAELEAAKAELE-------AQQAEQEALLAQLSA---EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250
....*....|..
gi 163644331 1541 EIQSALEEAEAS 1552
Cdd:COG3883 228 AAAAAAAAAAAA 239
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
962-1208 |
3.79e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 962 TLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLE 1041
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1042 qekklrmdlERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQTICIQLQKKLKELQARIEELE 1121
Cdd:COG3883 90 ---------ERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1122 EELEaeraaraKVEKQRADLARELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQADS 1201
Cdd:COG3883 161 ALKA-------ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
....*..
gi 163644331 1202 VAELGEQ 1208
Cdd:COG3883 234 AAAAAAA 240
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1465-1697 |
3.96e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1465 SQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLgeggksihelekmrKQLEQEKSEIQS 1544
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------------DKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1545 ALEEAEASLeheeGKILRAQLEFSQIKADIE------------------RKLAEKDEEMEQSKRNLQRTIDTLQSSLESE 1606
Cdd:COG3883 80 EIEERREEL----GERARALYRSGGSVSYLDvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1607 trsRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNEDLKENTAIVERRNNLLQAE 1686
Cdd:COG3883 156 ---LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
250
....*....|.
gi 163644331 1687 LEELRAALEQT 1697
Cdd:COG3883 233 AAAAAAAAAAA 243
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
873-995 |
4.00e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 873 KELEEKMVSLLQEKNDLQlqvqAEQDNLcdAEERCDQLIKNKIQLEAKAKELTERLEDEEEMNAELTAKKRKLEDECSEl 952
Cdd:COG0542 414 DELERRLEQLEIEKEALK----KEQDEA--SFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGK- 486
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 163644331 953 kkdIDDLELTLAKVEKEKHATENKVKN-LTEEMAAldDIIAKLT 995
Cdd:COG0542 487 ---IPELEKELAELEEELAELAPLLREeVTEEDIA--EVVSRWT 525
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1494-1749 |
4.12e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1494 LDHLETMKRENKNLQEEISDLTEQLGEGGKSIH-----ELEKMRKQLEQ---EKSEIQSALEEAEASLEH---------- 1555
Cdd:pfam00038 17 IDKVRFLEQQNKLLETKISELRQKKGAEPSRLYslyekEIEDLRRQLDTltvERARLQLELDNLRLAAEDfrqkyedeln 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1556 ------EEGKILRAQL-EFSQIKADIERKLAEKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEME 1628
Cdd:pfam00038 97 lrtsaeNDLVGLRKDLdEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1629 IQL-SQANRQAAEAQKQLKSVHAHMKDAQLQLDDSLRTNedlKENTAIVERRNNLLQAELEELRAALEQTErgRKLAEQE 1707
Cdd:pfam00038 177 AQYeEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSA---KEEITELRRTIQSLEIELQSLKKQKASLE--RQLAETE 251
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 163644331 1708 lldtsERVQLLHSQNTSLLNQkkkLETDISQLQTEVEEAVQE 1749
Cdd:pfam00038 252 -----ERYELQLADYQELISE---LEAELQETRQEMARQLRE 285
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1183-1412 |
4.17e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1183 ATLQHEATAATLRKKQADsVAELGEQIDNLQRVKQKLEKEKSELRLELDDVVSNMEhvvKTKANLEKMTRSLEDQMNEYK 1262
Cdd:COG3883 14 ADPQIQAKQKELSELQAE-LEAAQAELDALQAELEELNEEYNELQAELEALQAEID---KLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1263 TKYEEGQRCINDFTMQKSKLQSEN-GELSRQLeekdSLVSQLTRSKMSYTQQIEDLKRQLEEETKAksalahavqsarhd 1341
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESfSDFLDRL----SALSKIADADADLLEELKADKAELEAKKAE-------------- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 163644331 1342 tdlLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRtEELEEAKKKLAQRLQETEEAVEAVNAK 1412
Cdd:COG3883 152 ---LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE-AAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
953-1221 |
4.37e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.34 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 953 KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQeAHQQTLDDLQSEEDKVNTLTKAKAKLEqq 1032
Cdd:pfam15905 72 SKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLS-ASVASLEKQLLELTRVNELLKAKFSED-- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1033 vddleGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGK---IEDEQTICIQLQKK 1109
Cdd:pfam15905 149 -----GTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKlvsTEKEKIEEKSETEK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1110 LKELQARIEELEEELEAERAARAKVEKQRADLARELEEISERLEEAGGATAAQIemnKKREAEFQKLRRDLEEATLQHEA 1189
Cdd:pfam15905 224 LLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQI---KDLNEKCKLLESEKEELLREYEE 300
|
250 260 270
....*....|....*....|....*....|..
gi 163644331 1190 TAATLrkkqadsVAELGEQIDNLQRVKQKLEK 1221
Cdd:pfam15905 301 KEQTL-------NAELEELKEKLTLEEQEHQK 325
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1684-1879 |
4.47e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1684 QAELEELRAALEQTERGRKLAEQELLDTSERVQLLHSQNTSLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAITD 1763
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1764 AAM------MAEELKKEQDTSAHLERMK---------KNMEQTIKDLQHRLDEAEQIAmkggKKQVQKLEARVRELESEV 1828
Cdd:COG3883 95 LYRsggsvsYLDVLLGSESFSDFLDRLSalskiadadADLLEELKADKAELEAKKAEL----EAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 163644331 1829 ESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKA 1879
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1277-1550 |
4.54e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1277 MQKSKLQSENGELSRQLEEKDSLV-------SQLTRSKMSYTQQ---------------IEDLKRQLEEETKAKSALAHA 1334
Cdd:pfam17380 296 MEQERLRQEKEEKAREVERRRKLEeaekarqAEMDRQAAIYAEQermamererelerirQEERKRELERIRQEEIAMEIS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1335 VQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEtEEAVEAVNAKCS 1414
Cdd:pfam17380 376 RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE-ERAREMERVRLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1415 SLEKtkhrlQNEIEDLMVDLERSNAAAAALDKKQRNFDKVLSEWK----QKFEESQAELESSQKEARCLSTELFKLKNS- 1489
Cdd:pfam17380 455 EQER-----QQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRkileKELEERKQAMIEEERKRKLLEKEMEERQKAi 529
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 163644331 1490 YEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAE 1550
Cdd:pfam17380 530 YEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
911-1220 |
4.70e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 911 IKNKIQLEAKAKELTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDdi 990
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRE-- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 991 IAKLTKEKKALQEAHQQTLDDLQSEEDKVN--------TLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAK----RKLE 1058
Cdd:pfam17380 362 LERIRQEEIAMEISRMRELERLQMERQQKNervrqeleAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARqrevRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1059 GDLKLTQESLMDLENDKQQLEERLKKKDFEISQLNGKIEDEQticiQLQKKLKELQARIEELEEEleAERAARAKVEKQR 1138
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK----RDRKRAEEQRRKILEKELE--ERKQAMIEEERKR 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1139 ADLARELEEISERLEEAGGATAAQIEMNKKREAEfqkLRRDLEEATLQheATAATLRKKQADSVAELGEQIDNLQRVKQK 1218
Cdd:pfam17380 516 KLLEKEMEERQKAIYEEERRREAEEERRKQQEME---ERRRIQEQMRK--ATEERSRLEAMEREREMMRQIVESEKARAE 590
|
..
gi 163644331 1219 LE 1220
Cdd:pfam17380 591 YE 592
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
950-1080 |
4.83e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.60 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 950 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDL----------------- 1012
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQLDAAfrqgehtglqlilsgee 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1013 ---------------QSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLEN---- 1073
Cdd:PRK11637 151 sqrgerilayfgylnQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESslqk 230
|
....*..
gi 163644331 1074 DKQQLEE 1080
Cdd:PRK11637 231 DQQQLSE 237
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
931-1227 |
5.16e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 931 EEEMNAEL-TAKKRKL-EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQT 1008
Cdd:PRK11281 38 EADVQAQLdALNKQKLlEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1009 LDDLQSE--EDKVNTLTKAKAKLEQQVDDLEGSLeqeKKLRMDLERAKRKLEGDLKLTQE--SLMD--LENDKQQLEERL 1082
Cdd:PRK11281 118 LSTLSLRqlESRLAQTLDQLQNAQNDLAEYNSQL---VSLQTQPERAQAALYANSQRLQQirNLLKggKVGGKALRPSQR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1083 KKKDFEISQLNGKIEDEQTIC-----IQ--LQKKLKELQARIeeleeeleaeraarAKVEKQRADL-----ARELEEISE 1150
Cdd:PRK11281 195 VLLQAEQALLNAQNDLQRKSLegntqLQdlLQKQRDYLTARI--------------QRLEHQLQLLqeainSKRLTLSEK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1151 RLEEAGGAT-AAQIEMNK--KREAEF-QKLRRDLEEATLQ-HEATAATLRKKQadsvaelgeQIDNLQRVKQKLEKEKSE 1225
Cdd:PRK11281 261 TVQEAQSQDeAARIQANPlvAQELEInLQLSQRLLKATEKlNTLTQQNLRVKN---------WLDRLTQSERNIKEQISV 331
|
..
gi 163644331 1226 LR 1227
Cdd:PRK11281 332 LK 333
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1432-1795 |
5.78e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1432 VDLERSNAAAAALDKKQRNFdkvlsewKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEI 1511
Cdd:PLN02939 100 ASMQRDEAIAAIDNEQQTNS-------KDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1512 SDLTEQLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIKadiERKLAEKDEemeqskrn 1591
Cdd:PLN02939 173 NILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLK---EENMLLKDD-------- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1592 lqrtIDTLQSSLESETRSRNEALRIKKK---MEGDLNEMEIQLSQAnrQAAEAQKQLKSVHAHMKDAQlQLDDSLRTNED 1668
Cdd:PLN02939 242 ----IQFLKAELIEVAETEERVFKLEKErslLDASLRELESKFIVA--QEDVSKLSPLQYDCWWEKVE-NLQDLLDRATN 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1669 LKENTAIVERRNNLLQAELEELRAALEQTergrklaeqelldtseRVQLLHSQNTSLLNQKKKLetdisqlqteVEEAVQ 1748
Cdd:PLN02939 315 QVEKAALVLDQNQDLRDKVDKLEASLKEA----------------NVSKFSSYKVELLQQKLKL----------LEERLQ 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 163644331 1749 ECrNAEekakkaITDAAMMAEELKKE-QDTSAHL--ERMKKNMEQTIKDL 1795
Cdd:PLN02939 369 AS-DHE------IHSYIQLYQESIKEfQDTLSKLkeESKKRSLEHPADDM 411
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
846-1115 |
5.92e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 41.38 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 846 EAEKEMANMKDEFAKLKEAYAKSEarrKELEEKMVSL--------LQEK---NDL-----QLQVQAEQDNLcdaeERCDQ 909
Cdd:pfam03148 61 ELEKELEELDEEIELLLEEKRRLE---KALEALEEPLhiaqecltLREKrqgIDLvhdevEKELLKEVELI----EGIQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 910 LIKNKIQleaKAKELTERLED-EEEMNAELTAKKR--KLEDECSELKKDIDDLEL--TLAKVEK--------EKHATENK 976
Cdd:pfam03148 134 LLQRTLE---QAWEQLRLLRAaRHKLEKDLSDKKEalEIDEKCLSLNNTSPNISYkpGPTRIPPnsstpeewEKFTQDNI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 977 VKNLTEEMAAlddiiAKLtkeKKALQEAHQQTLDDLQSEEDKVNT--------LTKAKAKLEQQVDDLEGSLEQEKKLRM 1048
Cdd:pfam03148 211 ERAEKERAAS-----AQL---RELIDSILEQTANDLRAQADAVNFalrkrieeTEDAKNKLEWQLKKTLQEIAELEKNIE 282
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 163644331 1049 DLERAKRKLEGDLKLTQESL--------MDLENDKQQLeeRLKKkdfEISQLNGKIEDeqticiqLQKKLKELQA 1115
Cdd:pfam03148 283 ALEKAIRDKEAPLKLAQTRLenrtyrpnVELCRDEAQY--GLVD---EVKELEETIEA-------LKQKLAEAEA 345
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1460-1656 |
5.94e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1460 QKFEEsqaELESSQKEARClstelfKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLGEGGKSiheLEKMRKQLEQEK 1539
Cdd:PHA02562 201 NKNIE---EQRKKNGENIA------RKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAA---LNKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1540 SEIQSALEEAEASLEHEEGKILRAQLEFSQikaDIERKLAEKDEEMEQSKRNLQRTIDTLQSSLesetrsrNEALRIKKK 1619
Cdd:PHA02562 269 SKIEQFQKVIKMYEKGGVCPTCTQQISEGP---DRITKIKDKLKELQHSLEKLDTAIDELEEIM-------DEFNEQSKK 338
|
170 180 190
....*....|....*....|....*....|....*..
gi 163644331 1620 megdLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQ 1656
Cdd:PHA02562 339 ----LLELKNKISTNKQSLITLVDKAKKVKAAIEELQ 371
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1313-1553 |
5.95e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 40.47 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1313 QIEDLKRQLEEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKANSEVaqwrtkyeTDAIQRTEELEEAK 1392
Cdd:pfam06008 20 NLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAES--------ERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1393 KKLAQRLQETEEAVEAVNAKCSSL-EKTKHRLQNEIEDLMVDLERSNaaaaaLDKKQRNFDKVLSEWKQKFEESQAELES 1471
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGENDFALpSSDLSRMLAEAQRMLGEIRSRD-----FGTQLQNAEAELKAAQDLLSRIQTWFQS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1472 SQKEARCLSTELFKLKNSYEEALDHLETMKRENKNLQEEISDLteqLGEGGKSIHELEKMRKQLEQEKSEIQSALEEAEA 1551
Cdd:pfam06008 167 PQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRL---NLANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
..
gi 163644331 1552 SL 1553
Cdd:pfam06008 244 SL 245
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1503-1929 |
6.07e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 41.58 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1503 ENKNLQEEISdlteqlgeggksihelekmrkQLEQEKSEIQSALEEAEASLEheegkilraqlefsqiKADIERKLAEKD 1582
Cdd:pfam13166 90 ESIEIQEKIA---------------------KLKKEIKDHEEKLDAAEANLQ----------------KLDKEKEKLEAD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1583 EEMEQSKRNLQRTIDTLQSSLESETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQK---QLKSVhahmkdAQLQL 1659
Cdd:pfam13166 133 FLDECWKKIKRKKNSALSEALNGFKYEANFKSRLLREIEKDNFNAGVLLSDEDRKAALATVfsdNKPEI------APLTF 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1660 DDSLRtneDLKENTAIVERRNNLLQAELEELRA---ALEQTERGRKLAEQELLD--------TSERVQLLHSQ-NTSLLN 1727
Cdd:pfam13166 207 NVIDF---DALEKAEILIQKVIGKSSAIEELIKnpdLADWVEQGLELHKAHLDTcpfcgqplPAERKAALEAHfDDEFTE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1728 QKKKLETDISQLQTEVEEAVQECRNAEEKAKKAItdaammAEELKKEQdtsahLERMKKNMEQTIKDLQHRLDEAeqiam 1807
Cdd:pfam13166 284 FQNRLQKLIEKVESAISSLLAQLPAVSDLASLLS------AFELDVED-----IESEAEVLNSQLDGLRRALEAK----- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1808 kggKKQVqkleARVRELES---EVESEQKKSSEAVKGIRKYERRIKELTYQTEEDRKNLARlqDLVDKLQLKVKAYKRAA 1884
Cdd:pfam13166 348 ---RKDP----FKSIELDSvdaKIESINDLVASINELIAKHNEITDNFEEEKNKAKKKLRL--HLVEEFKSEIDEYKDKY 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 163644331 1885 EEAEEQANtnlskfrKIQHELDEAEERADIAESQVNKLRAKSRDV 1929
Cdd:pfam13166 419 AGLEKAIN-------SLEKEIKNLEAEIKKLREEIKELEAQLRDH 456
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1580-1920 |
6.13e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1580 EKDEEMEQSKRNLQRTIDTLQSSLESETRSRNEALR----IKKKMEGDLNEMEIQLSQANRQAAEA-QKQLKSVHAHMKD 1654
Cdd:PLN02939 46 QKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRtvmeLPQKSTSSDDDHNRASMQRDEAIAAIdNEQQTNSKDGEQL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1655 AQLQLDDSLRTNEDLKENTAIVER--------------RNNLLQAELEELRAALEQTERGRKLAEQELLDtserVQLLHS 1720
Cdd:PLN02939 126 SDFQLEDLVGMIQNAEKNILLLNQarlqaledlekiltEKEALQGKINILEMRLSETDARIKLAAQEKIH----VEILEE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1721 QntsLLNQKKKLETDISQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTS---AHLERMKKNMEQTIKDLQH 1797
Cdd:PLN02939 202 Q---LEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEervFKLEKERSLLDASLRELES 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1798 RLDEAEQIAMKGGKKQVQKLEARVRELESEVESEQKKSSEAVkgirkyerrikeLTYQTEEDrknlarLQDLVDKLQLKV 1877
Cdd:PLN02939 279 KFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAA------------LVLDQNQD------LRDKVDKLEASL 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 163644331 1878 KAykraaeeaeeqanTNLSKFRK-----IQHELDEAEERADIAESQVN 1920
Cdd:PLN02939 341 KE-------------ANVSKFSSykvelLQQKLKLLEERLQASDHEIH 375
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1383-1550 |
6.13e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1383 QRTEELEEAKKKLAQRLQE--TEEAVEAVNAKCSSLEKTKHR---LQNEIEDLMVDLE-----------RSNAAAAALDK 1446
Cdd:pfam09787 14 QKAARILQSKEKLIASLKEgsGVEGLDSSTALTLELEELRQErdlLREEIQKLRGQIQqlrtelqeleaQQQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1447 KQRNFDKVLSEWKQKFEESQAELESSQKEARCLSTELFKLKNSYEEALDHLET---------MKRENKNLQEeiSDLTEQ 1517
Cdd:pfam09787 94 QLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAeieklrnqlTSKSQSSSSQ--SELENR 171
|
170 180 190
....*....|....*....|....*....|...
gi 163644331 1518 LGEGGKSIHELEKMRKQLEQEKSEIQSALEEAE 1550
Cdd:pfam09787 172 LHQLTETLIQKQTMLEALSTEKNSLVLQLERME 204
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
955-1085 |
6.16e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 955 DIDDLELTLAKVEKEKHATENkvknltEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVD 1034
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1035 DLEGSLEQEKKLRMDLERAKRKLEGDL------------------KLTQEslmdlENDK-QQLEERLKKK 1085
Cdd:COG0542 486 KIPELEKELAELEEELAELAPLLREEVteediaevvsrwtgipvgKLLEG-----EREKlLNLEEELHER 550
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1451-1587 |
6.28e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1451 FDKVLSEWKQKFEESQAE--LESSQKEARCLSTElfKLKNSYEEALDHLETMKRENKNLQEEISDLTEQLgeggksihel 1528
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKriLEEAKKEAEAIKKE--ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRL---------- 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 163644331 1529 eKMRKQLEQEKSEiqsALEEAEASLEHEEGKILRAQLEFSQIKADIERKLAEKDEEMEQ 1587
Cdd:PRK12704 92 -LQKEENLDRKLE---LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| Mrs2_Mfm1p-like |
cd12823 |
Saccharomyces cerevisiae inner mitochondrial membrane Mg2+ transporters Mfm1p and Mrs2p-like ... |
780-991 |
6.33e-03 |
|
Saccharomyces cerevisiae inner mitochondrial membrane Mg2+ transporters Mfm1p and Mrs2p-like family; A eukaryotic subfamily belonging to the Escherichia coli CorA-Salmonella typhimurium ZntB_like family (EcCorA_ZntB-like) family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. This functionally diverse subfamily includes the inner mitochondrial membrane Mg2+ transporters Saccharomyces cerevisiae Mfm1p/Lpe10p, Mrs2p, and human MRS2/ MRS2L. It also includes a family of Arabidopsis thaliana proteins (AtMGTs) some of which are localized to distinct tissues, and not all of which can transport Mg2+. Structures of the intracellular domain of two EcCorA_ZntB-like family transporters: Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, as in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport.
Pssm-ID: 213357 Cd Length: 323 Bit Score: 41.08 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 780 DDRLSLIISGIQARSRGLLARVEFQKIVERRDALLVI------QWNVRAFMGvknwpwmKLFFKIKPLLKSAEAEKEMAN 853
Cdd:cd12823 35 DPTLTSYPPSILVRENAILVNLEHIRAIITADEVLLFdpdgssSALVSAFLE-------ELQRRLASSNGSESESGGEDS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 854 MKDEF----AKLKEAYAKSEARRKELEEKMVSLLQEkndlqLQVQAEQDNLCDAeercdQLIKNKI-QLEAKAK----EL 924
Cdd:cd12823 108 LPFEFraleAALEEVCSHLEAELKRLEPEALPLLDE-----LTDKISTSNLERL-----LPLKRRLvELETRVQkvrdAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644331 925 TERLEDEEEMNA-ELTAK-KRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDII 991
Cdd:cd12823 178 EELLDDDEDMADmYLTDKaAGPERLESSRKEDDHEEVEMLLEAYLQQVDELLNKLEELREYIDDTEELI 246
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
974-1391 |
7.03e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 974 ENKVKNLTEEMAALDDIIAKLTKEKKALQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERA 1053
Cdd:COG5185 172 LNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQT 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1054 KRKLEGDLKLTQESLMDLENDKQQLEERLK----KKDFEISQLNGKI-EDEQTICI-QLQKKLKELQARIEELEEELEAE 1127
Cdd:COG5185 252 SDKLEKLVEQNTDLRLEKLGENAESSKRLNenanNLIKQFENTKEKIaEYTKSIDIkKATESLEEQLAAAEAEQELEESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1128 RAARAKVEKQRADLARELEEISERLEEAGGAtaaqiEMNKKREAEFQKLRRDLEEATLQHEATAATLRKKQADSVAELGE 1207
Cdd:COG5185 332 RETETGIQNLTAEIEQGQESLTENLEAIKEE-----IENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1208 QIDNLQRVKQKLEKEKSELRLELDDVVSNMEHVVKTKANLEK-MTRSLEDQMNEYKTKYEEGQRCINdftmqkSKLQSEN 1286
Cdd:COG5185 407 ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISeLNKVMREADEESQSRLEEAYDEIN------RSVRSKK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1287 GELSRQLEekdslvsQLTRSKMSYTQQIEDLKRQLEEETKAKSALAHAVQ-----SARHDTDLLREQYEEEQEAKAELQR 1361
Cdd:COG5185 481 EDLNEELT-------QIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAeslkdFMRARGYAHILALENLIPASELIQA 553
|
410 420 430
....*....|....*....|....*....|
gi 163644331 1362 GMSKANSEVAQWRTKYETDAIQRTEELEEA 1391
Cdd:COG5185 554 SNAKTDGQAANLRTAVIDELTQYLSTIESQ 583
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1529-1862 |
7.51e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.15 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1529 EKMRKQLEQEKSEIQSALEEAEASLEHEEGKILRA-QLEFSQIKADIERKLAEKDEEMEQSkrnlqrtidtlqssLESET 1607
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVAlNKKLSDIKTEYLYELNVLKEKSEAE--------------LTSKT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1608 RSRNEALRikKKMEGDLNEMEIQLSQANRQAAEAQKQLKsvhahmkdaqlqlddslrtneDLKEntaivERRNNLLQAEL 1687
Cdd:NF033838 120 KKELDAAF--EQFKKDTLEPGKKVAEATKKVEEAEKKAK---------------------DQKE-----EDRRNYPTNTY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1688 EELRAALEQTERGRKLAEQELLdtseRVQLLHSQNTSLLNQ-------KKKLETDISQLQTEVEEAVQEC-RNAEEKAKK 1759
Cdd:NF033838 172 KTLELEIAESDVEVKKAELELV----KEEAKEPRDEEKIKQakakvesKKAEATRLEKIKTDREKAEEEAkRRADAKLKE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1760 AITDAAMMAEElkkeqdtsahlERMKKNMEQTIKDLQHRLDEAEQIAmKGGKKQVQKlearvRELESEVESEQKKSSEAV 1839
Cdd:NF033838 248 AVEKNVATSEQ-----------DKPKRRAKRGVLGEPATPDKKENDA-KSSDSSVGE-----ETLPSPSLKPEKKVAEAE 310
|
330 340
....*....|....*....|...
gi 163644331 1840 KGIRKYERRIKEltyQTEEDRKN 1862
Cdd:NF033838 311 KKVEEAKKKAKD---QKEEDRRN 330
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1210-1456 |
7.73e-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: 41.38 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1210 DNLQRVKQKLEKEKSELRLElddvvSNMEHVVKTKAN-LEKMTRSLEDQMNEYKTKYEEGQRCINDFTMQKSKLQSENGE 1288
Cdd:pfam09726 395 DALVRLEQDIKKLKAELQAS-----RQTEQELRSQISsLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1289 LSRQLEEKdslvsqlTRSKMSYTQQI-EDLKRQLEEETKAKSALAHAVQSARHDTDLLReqyeeeqeakaelqrgmskan 1367
Cdd:pfam09726 470 LEKRLKAE-------QEARASAEKQLaEEKKRKKEEEATAARAVALAAASRGECTESLK--------------------- 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1368 sevaqwrtkyetdaiQRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRlQNEIEDLMvdlersnAAAAALDKK 1447
Cdd:pfam09726 522 ---------------QRKRELESEIKKLTHDIKLKEEQIRELEIKVQELRKYKES-EKDTEVLM-------SALSAMQDK 578
|
....*....
gi 163644331 1448 QRNFDKVLS 1456
Cdd:pfam09726 579 NQHLENSLS 587
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
849-1085 |
8.31e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 849 KEMANMKDEFAKLKEAYAKSEARRKELE-EKMVSLLQEKNDLQLQVQAEQDNLCDAEERCDQLIKNKIQ-LEAKAKELTE 926
Cdd:PRK01156 493 KDIDEKIVDLKKRKEYLESEEINKSINEyNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEdLDSKRTSWLN 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 927 RLEDEEEMNAElTAKKRKledecSELKKDIDDLELTLAKVEKE----KHATENKVKNLTEEMAALDDIIaKLTKEKKALQ 1002
Cdd:PRK01156 573 ALAVISLIDIE-TNRSRS-----NEIKKQLNDLESRLQEIEIGfpddKSYIDKSIREIENEANNLNNKY-NEIQENKILI 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1003 EAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLEERL 1082
Cdd:PRK01156 646 EKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETL 725
|
...
gi 163644331 1083 KKK 1085
Cdd:PRK01156 726 ESM 728
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1289-1694 |
8.58e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 41.04 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1289 LSRQLEEKDSLVSQLT--RSKMSYTQQiedlkrqleEETKAKSALAHAVQSARHDTDLLREQYEEEQEAKAELQRGMSKA 1366
Cdd:pfam15964 302 IERLTKERDDLMSALVsvRSSLAEAQQ---------RESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1367 NSEVAQWRTKyetdaiqRTEELEEAKKKLAQRLQETEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLErsnAAAAALDK 1446
Cdd:pfam15964 373 EKELASQQEK-------RAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLE---EAQKQLAS 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1447 KQRNFDKVLSEWKQKFEESQAELESSQKEARCLST-----------ELFKLKNSYEEALDHLETMKRENKNLQEEISDLT 1515
Cdd:pfam15964 443 QEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTktgrqleikdqEIEKLGLELSESKQRLEQAQQDAARAREECLKLT 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1516 EQLGEGGKSIH--ELEK----------------MRKQLEQEKSEIQSALEEAEASLEHEEGKILRAQLEFSQIKADIERK 1577
Cdd:pfam15964 523 ELLGESEHQLHltRLEKesiqqsfsneakaqalQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCT 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1578 LAEKDEEMEQSKRnlqrtidTLQSSLESETRSRNEALrikKKMEGDLNEMEIQLSQANRQAAEAQKQLKSVHAHMKDAQL 1657
Cdd:pfam15964 603 LAKKLEEITQKSR-------SEVEQLSQEKEYLQDRL---EKLQKRNEELEEQCVQHGRMHERMKQRLRQLDKHCQATAQ 672
|
410 420 430
....*....|....*....|....*....|....*..
gi 163644331 1658 QLDDSLRtnedlKENTAIVERRNnlLQAELEELRAAL 1694
Cdd:pfam15964 673 QLVQLLS-----KQNQLFKERQN--LTEEVQSLRSQV 702
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
902-1042 |
8.85e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.43 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 902 DAEERCDQLIKNKIQLEAKAKELTERLedeeemnaeltakkRKLEDECSELKKDIDDLELTL-AKVEKEKHATENK-VKN 979
Cdd:cd22656 118 TIKALLDDLLKEAKKYQDKAAKVVDKL--------------TDFENQTEKDQTALETLEKALkDLLTDEGGAIARKeIKD 183
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 163644331 980 LTEEMAALDDIIAKLTKEKkalQEAHQQTLDDLQSEEDKVNTLTKAKAKLEQQVDDLEGSLEQ 1042
Cdd:cd22656 184 LQKELEKLNEEYAAKLKAK---IDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGP 243
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1142-1336 |
9.30e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1142 ARELEEISERLEEAGGATAAQIEMNKKREA--EFQKLRRDLEEatlqheataatlrkkqadsvaELGEQIDNLQRVKQKL 1219
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEALLEAkeEIHKLRNEFEK---------------------ELRERRNELQKLEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1220 EKEKSELRLELDDVVSNMEHVVKTKANLEKMTRSLEDQMNEYKTKYEEgqrcindftmQKSKLQSENGeLSRQlEEK--- 1296
Cdd:PRK12704 92 LQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE----------QLQELERISG-LTAE-EAKeil 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 163644331 1297 -DSLVSQLTRSKMSYTQQIEDlKRQLEEETKAKSALAHAVQ 1336
Cdd:PRK12704 160 lEKVEEEARHEAAVLIKEIEE-EAKEEADKKAKEILAQAIQ 199
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
841-1098 |
9.46e-03 |
|
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: 40.93 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 841 LLKSAEAEKEMANMKDEFAKLKEAYAKSEARRKeleekmvsllqekndlqlQVQAEQDNLcdAEERCDQLIKNKIQLEak 920
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASERARR------------------QAQQERDEL--ADEIASGASGKSALQD-- 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 921 akelterledeeemnaeltaKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDDIIAKLTKEKKA 1000
Cdd:pfam01576 883 --------------------EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQ 942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644331 1001 LQEAHQQTLDDLQSEEDKVNTLTKAK-AKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLTQESLMDLENDKQQLE 1079
Cdd:pfam01576 943 LERQNKELKAKLQEMEGTVKSKFKSSiAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYK 1022
|
250
....*....|....*....
gi 163644331 1080 ERLKKKDFEISQLNGKIED 1098
Cdd:pfam01576 1023 DQAEKGNSRMKQLKRQLEE 1041
|
|
| |
