|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
117-778 |
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: 1430.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 276
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 277 DIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFLPD 356
Cdd:cd14929 161 DIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDILGFLPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 357 EKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAV 436
Cdd:cd14929 241 EKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTYAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 437 GALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKE 516
Cdd:cd14929 321 GALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 517 SIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFELVHYAG 596
Cdd:cd14929 401 GIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHFELVHYAG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 597 VVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKKRKKGASFQTVASLHKENLNKLMTNLKS 676
Cdd:cd14929 481 VVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQFGEKKRKKGASFQTVASLHKENLNKLMTNLKS 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 677 TAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVSSRKAAEE 756
Cdd:cd14929 561 TAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSSRKAAEE 640
|
650 660
....*....|....*....|..
gi 119600132 757 LLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14929 641 LLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
117-778 |
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: 1244.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAAMIESR----KKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 272
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKkesgKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 273 SVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDIL 351
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADpELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 352 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQ 431
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 432 VTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQE 511
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 512 EYKKESIEWVSIGFGLDLQACIDLIEKP-MGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPdkKKFEAHFE 590
Cdd:cd01377 401 EYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKP--KKSEAHFI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 591 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAipfGEKKRKKGASFQTVASLHKENLNKL 670
Cdd:cd01377 479 LKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGG---GGKKKKKGGSFRTVSQLHKEQLNKL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 671 MTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSkFVSS 750
Cdd:cd01377 556 MTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKG-FDDG 634
|
650 660
....*....|....*....|....*...
gi 119600132 751 RKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd01377 635 KAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
117-778 |
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: 1179.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAAMIESRKKQ---------GALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGA 267
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKaqflatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 268 RGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQ 346
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKpELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 347 AMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRG 426
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 427 QTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMF 506
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 507 VLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKK-KF 585
Cdd:cd14927 401 ILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKrKY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 586 EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFG---EKKRKKGASFQTVASL 662
Cdd:cd14927 481 EAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEDPKsgvKEKRKKAASFQTVSQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 663 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTF 742
Cdd:cd14927 561 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAI 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 119600132 743 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14927 641 PDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
118-778 |
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: 1066.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 197
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 198 SGAGKTVNSKHIIQYFATIAAMIESRKKQ-----GALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 272
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKKdskmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 273 SVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDIL 351
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKpELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 352 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQ 431
Cdd:cd14913 242 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 432 VTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQE 511
Cdd:cd14913 322 VHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 512 EYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFEL 591
Cdd:cd14913 402 EYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFSL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 592 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKKRKKGASFQTVASLHKENLNKLM 671
Cdd:cd14913 482 IHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKLM 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 672 TNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVSSR 751
Cdd:cd14913 562 SNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSK 641
|
650 660
....*....|....*....|....*..
gi 119600132 752 KAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14913 642 KACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
118-778 |
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: 986.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 197
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 198 SGAGKTVNSKHIIQYFATIAAMIESRKK-----QGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 272
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKdqtpgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 273 SVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDIL 351
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKpELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 352 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQ 431
Cdd:cd14917 242 GFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 432 VTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQE 511
Cdd:cd14917 322 VIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 512 EYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFEL 591
Cdd:cd14917 402 EYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHFSL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 592 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKKRKKGASFQTVASLHKENLNKLM 671
Cdd:cd14917 482 IHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLM 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 672 TNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVSSR 751
Cdd:cd14917 562 TNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSR 641
|
650 660
....*....|....*....|....*..
gi 119600132 752 KAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14917 642 KGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
118-778 |
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: 961.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 197
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 198 SGAGKTVNSKHIIQYFATIAAMIESRKK------QGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 271
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKenpnanKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 272 SSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDI 350
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKpELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 351 LGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIE 430
Cdd:cd14916 242 LGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 431 QVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQ 510
Cdd:cd14916 322 QVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 511 EEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFE 590
Cdd:cd14916 402 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHFS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 591 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIP-FGEKKRKKGASFQTVASLHKENLNK 669
Cdd:cd14916 482 LVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSgKGKGGKKKGSSFQTVSALHRENLNK 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 670 LMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVS 749
Cdd:cd14916 562 LMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFID 641
|
650 660
....*....|....*....|....*....
gi 119600132 750 SRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14916 642 SRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
105-778 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 959.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 105 IEDMAMLTHLNEASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDML 184
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 185 HNRENQSILFTGESGAGKTVNSKHIIQYFATIAAmIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMH 264
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSG-SGSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 265 FGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLvsANPSDFHFCS-CGAVTVESLDDAEEL 341
Cdd:pfam00063 160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGasAQLKKELRL--TNPKDYHYLSqSGCYTIDGIDDSEEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 342 LATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNE 421
Cdd:pfam00063 238 KITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 422 YVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAK-LSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQF 500
Cdd:pfam00063 318 TVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKtIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 501 FNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKLFDnHFGKSVHLQKPK 579
Cdd:pfam00063 398 FNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYS-TFSKHPHFQKPR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 580 PdkkKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGE----KKRKKGAS 655
Cdd:pfam00063 476 L---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESgkstPKRTKKKR 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 656 FQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYC 735
Cdd:pfam00063 553 FITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYR 632
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 119600132 736 ILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:pfam00063 633 ILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
118-778 |
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: 954.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 197
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 198 SGAGKTVNSKHIIQYFATIAAMIESRKK------QGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 271
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqpgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 272 SSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDI 350
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKpELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAIDI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 351 LGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIE 430
Cdd:cd14923 242 LGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 431 QVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQ 510
Cdd:cd14923 322 QVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 511 EEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFE 590
Cdd:cd14923 402 EEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHFS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 591 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKK--RKKGASFQTVASLHKENLN 668
Cdd:cd14923 482 LVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSGGSKKggKKKGSSFQTVSAVFRENLN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 669 KLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFV 748
Cdd:cd14923 562 KLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQFI 641
|
650 660 670
....*....|....*....|....*....|
gi 119600132 749 SSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14923 642 DSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
119-778 |
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: 936.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 119 VLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGES 198
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 199 GAGKTVNSKHIIQYFATIAAMIESRKK-----QGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 273
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 274 VDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILG 352
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 353 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQV 432
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 433 TCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEE 512
Cdd:cd14918 323 YNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 513 YKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFELV 592
Cdd:cd14918 403 YKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFSLI 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 593 HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKKRKKGASFQTVASLHKENLNKLMT 672
Cdd:cd14918 483 HYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAKKKGSSFQTVSALFRENLNKLMT 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 673 NLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVSSRK 752
Cdd:cd14918 563 NLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDSKK 642
|
650 660
....*....|....*....|....*.
gi 119600132 753 AAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14918 643 ASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
118-778 |
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: 934.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 197
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 198 SGAGKTVNSKHIIQYFATIAAMIESRKK-------QGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 270
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 271 LSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 349
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 350 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTI 429
Cdd:cd14915 242 ILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 430 EQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLE 509
Cdd:cd14915 322 QQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 510 QEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHF 589
Cdd:cd14915 402 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAHF 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 590 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEK-KRKKGASFQTVASLHKENLN 668
Cdd:cd14915 482 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKgGKKKGSSFQTVSALFRENLN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 669 KLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFV 748
Cdd:cd14915 562 KLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI 641
|
650 660 670
....*....|....*....|....*....|
gi 119600132 749 SSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14915 642 DSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
98-790 |
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: 933.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 98 NPPEFEMIEDMAMLTHLNEASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVAN 177
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 178 NAFQDMLHNRENQSILFTGESGAGKTVNSKHIIQYFATIAAmieSRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRF 257
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG---SNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 258 GKFIRMHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLvsANPSDFHFCS-CGAVTVES 334
Cdd:smart00242 158 GKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGasEELKKELGL--KSPEDYRYLNqGGCLTVDG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 335 LDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEA-DGTENADKAAFLMGINSSELVKCLIH 413
Cdd:smart00242 236 IDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTvKDKEELSNAAELLGVDPEELEKALTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 414 PRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFT 493
Cdd:smart00242 316 RKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 494 NEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKLfDNHFGKS 572
Cdd:smart00242 396 NEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKL-NQHHKKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 573 VHLQKPkpdKKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYmstdsaipfgEKKRKK 652
Cdd:smart00242 474 PHFSKP---KKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG----------VSNAGS 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 653 GASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQ 732
Cdd:smart00242 541 KKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQ 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 119600132 733 RYCILNPRTFPkSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFKAGFLGQLEAIRD 790
Cdd:smart00242 621 RYRVLLPDTWP-PWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
118-778 |
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: 931.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 197
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 198 SGAGKTVNSKHIIQYFATIAAM-------IESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 270
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTgekkkeeATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 271 LSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 349
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 350 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTI 429
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 430 EQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLE 509
Cdd:cd14910 322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 510 QEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHF 589
Cdd:cd14910 402 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAHF 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 590 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEK-KRKKGASFQTVASLHKENLN 668
Cdd:cd14910 482 SLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKgGKKKGSSFQTVSALFRENLN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 669 KLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFV 748
Cdd:cd14910 562 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI 641
|
650 660 670
....*....|....*....|....*....|
gi 119600132 749 SSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14910 642 DSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
118-778 |
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: 927.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 197
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 198 SGAGKTVNSKHIIQYFATIAAMIESRKK-------QGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 270
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 271 LSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 349
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 350 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTI 429
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 430 EQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLE 509
Cdd:cd14912 322 EQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 510 QEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHF 589
Cdd:cd14912 402 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAHF 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 590 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKK---RKKGASFQTVASLHKEN 666
Cdd:cd14912 482 SLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKkggKKKGSSFQTVSALFREN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 667 LNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSK 746
Cdd:cd14912 562 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 641
|
650 660 670
....*....|....*....|....*....|..
gi 119600132 747 FVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14912 642 FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
117-778 |
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: 923.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAAM-IESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 275
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTgKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 276 IDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFL 354
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKpELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 355 PDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTC 434
Cdd:cd14934 241 AEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 435 AVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYK 514
Cdd:cd14934 321 SIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 515 KESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDK-KKFEAHFELVH 593
Cdd:cd14934 401 REGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKgKGPEAHFELVH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 594 YAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEnymstDSAIPFGEKKRKKGASFQTVASLHKENLNKLMTN 673
Cdd:cd14934 481 YAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFK-----EEEAPAGSKKQKRGSSFMTVSNFYREQLNKLMTT 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 674 LKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSkFVSSRKA 753
Cdd:cd14934 556 LHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVDNKKA 634
|
650 660
....*....|....*....|....*
gi 119600132 754 AEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14934 635 SELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
117-778 |
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: 908.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAAMI---ESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 273
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKktdEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 274 VDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQ-KELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILG 352
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSvPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 353 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQV 432
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 433 TCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEE 512
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 513 YKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEA-HFEL 591
Cdd:cd14909 401 YKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAaHFAI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 592 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYmSTDSAIPFGEK--KRKKGASFQTVASLHKENLNK 669
Cdd:cd14909 481 AHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADH-AGQSGGGEQAKggRGKKGGGFATVSSAYKEQLNS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 670 LMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKfvS 749
Cdd:cd14909 560 LMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE--D 637
|
650 660
....*....|....*....|....*....
gi 119600132 750 SRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14909 638 PKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
53-1460 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 817.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 53 KCWIPDGENAYIEAEVKGSEDDGTVIVETAD---GESLSIKEDKIQQ--MNPPEFEMIEDMAMLTHLNEASVLHTLKRRY 127
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKEAFNKGKVTEEGKkedGESVSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPAVLHNLEKRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 128 GQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGESGAGKTVNSK 207
Cdd:COG5022 91 NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 208 HIIQYFATIAAMIESRKKQgaLEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDIDIYLLEKSRVI 287
Cdd:COG5022 171 RIMQYLASVTSSSTVEISS--IEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 288 FQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVT-VESLDDAEELLATEQAMDILGFLPDEKYGCYKLTG 366
Cdd:COG5022 249 HQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 367 AIMHFGNMKFKqKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYER 446
Cdd:COG5022 329 AILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 447 MFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFg 526
Cdd:COG5022 408 LFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY- 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 527 LDLQACIDLIEK--PMGILSILEEECMFPKATDLTFKTKLFDN-HFGKSVHLQKPKPDKKKfeahFELVHYAGVVPYNIS 603
Cdd:COG5022 487 FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVKHYAGDVEYDVE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 604 GWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTdsaipfgEKKRKkgasFQTVASLHKENLNKLMTNLKSTAPHFVR 683
Cdd:COG5022 563 GFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENI-------ESKGR----FPTLGSRFKESLNSLMSTLNSTQPHYIR 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 684 CINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNP---RTFPKSKFVSSRKAAEELLGS 760
Cdd:COG5022 632 CIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPsksWTGEYTWKEDTKNAVKSILEE 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 761 LEIDHTQYRFGITKVFFKAGFLGQLEAIRDERLSKVFTLFQARAQGKLMRIKFQKILEERDALILIQWNIRAFMAVKNWP 840
Cdd:COG5022 712 LVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYEL 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 841 WMRLFFKIKPLVKSSEVGEEVaGLKEECAQlqkaleksEFQREELKAKQVSLTQEKNDLIlqlqaeqetlanveeQCEWL 920
Cdd:COG5022 792 KWRLFIKLQPLLSLLGSRKEY-RSYLACII--------KLQKTIKREKKLRETEEVEFSL---------------KAEVL 847
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 921 IKSKIQLEARVKELSERVEEEEEINSelTARGRKLEDECFELKKEIDDLETM-LVKSEKEKRTTEHK---VKNLTEEVEF 996
Cdd:COG5022 848 IQKFGRSLKAKKRFSLLKKETIYLQS--AQRVELAERQLQELKIDVKSISSLkLVNLELESEIIELKkslSSDLIENLEF 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 997 LNEDISKL-----NRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCER---ELHKLE 1068
Cdd:COG5022 926 KTELIARLkkllnNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNfkkELAELS 1005
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1069 GNLKLNRESMENLESSQRHLAeELRKKELELSQMNSKVENEKGlvaqLQKTVKELQTQIKDLKEKLEAerttrAKMERER 1148
Cdd:COG5022 1006 KQYGALQESTKQLKELPVEVA-ELQSASKIISSESTELSILKP----LQKLKGLLLLENNQLQARYKA-----LKLRREN 1075
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1149 adltQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAELegqVENLQQVKQK 1228
Cdd:COG5022 1076 ----SLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQL---VNTLEPVFQK 1148
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1229 LEKDksdlQLEVDDLLTrvEQMTRAKANAEKLCTLYEERLHEA-------TAKLDKVTQLANDLAAQKTKLWSES--GEF 1299
Cdd:COG5022 1149 LSVL----QLELDGLFW--EANLEALPSPPPFAALSEKRLYQSalydeksKLSSSEVNDLKNELIALFSKIFSGWprGDK 1222
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1300 LRRLEEKEALINQLSR--EKSNFTRQIEDLRGQLEKEtksqsALAHALQKAQRDCDLLREQYEEE--------QEVKAEL 1369
Cdd:COG5022 1223 LKKLISEGWVPTEYSTslKGFNNLNKKFDTPASMSNE-----KLLSLLNSIDNLLSSYKLEEEVLpatinsllQYINVGL 1297
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1370 HRTLSKVNAEMvqwRMKYENNVIQRTEDLEDAKKELAI-RLQEAAEamgvanarnaSLERARHQLQLELGDaLSDLGKVR 1448
Cdd:COG5022 1298 FNALRTKASSL---RWKSATEVNYNSEELDDWCREFEIsDVDEELE----------ELIQAVKVLQLLKDD-LNKLDELL 1363
|
1450
....*....|..
gi 119600132 1449 SAAARLDQKQLQ 1460
Cdd:COG5022 1364 DACYSLNPAEIQ 1375
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
117-778 |
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: 786.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRR-SEAPPHIFAVANNAFQDMLHNRENQSILFT 195
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 196 GESGAGKTVNSKHIIQYFATIAA--MIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 273
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGsgSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 274 VDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQ-----KELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAM 348
Cdd:cd00124 161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLsdgarEELKLELLLSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 349 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREE--QLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRG 426
Cdd:cd00124 241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 427 QTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQF--FIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWH 504
Cdd:cd00124 321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEStsFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 505 MFVLEQEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKK 583
Cdd:cd00124 401 VFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 584 kfeaHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSsnrllaslfenymstdsaipfgekkrkkgasfqtvaSLH 663
Cdd:cd00124 480 ----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG------------------------------------SQF 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 664 KENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRtFP 743
Cdd:cd00124 520 RSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPG-AT 598
|
650 660 670
....*....|....*....|....*....|....*
gi 119600132 744 KSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd00124 599 EKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
117-778 |
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: 737.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAA------------MIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMH 264
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAskpkgsgavphpAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 265 FGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLAT 344
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 345 EQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVT 424
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 425 RGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFN 502
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLD-RTKRQgaSFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 503 WHMFVLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHfgkSVHlqkPKPDK 582
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH---SMH---PKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 583 KKFE--AHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSA------IPFGEKKRKkgA 654
Cdd:cd14911 474 TDFRgvADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAqqaltdTQFGARTRK--G 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 655 SFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRY 734
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 119600132 735 CILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14911 632 ELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
117-778 |
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: 725.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAAMIESRKK---QGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 273
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDhniPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 274 VDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKE--LHDLLLVSANpsDFHFCSCGAVTVESLDDAEELLATEQAMDIL 351
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEhlKSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 352 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQ 431
Cdd:cd14920 239 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 432 VTCAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLE 509
Cdd:cd14920 319 ADFAVEALAKATYERLFRWLVHRINKALD-RTKRQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 510 QEEYKKESIEWVSIGFGLDLQACIDLIEKPM---GILSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKpdKKKFE 586
Cdd:cd14920 398 QEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPR--QLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 587 AHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY-----MSTDSAIP---FGEKKRKKGASFQT 658
Cdd:cd14920 475 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgLDQVTGMTetaFGSAYKTKKGMFRT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 659 VASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILN 738
Cdd:cd14920 555 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 119600132 739 PRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14920 635 PNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
118-778 |
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: 673.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQW-MIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAAmieSRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 276
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGG---SSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 277 DIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLVSANpSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFL 354
Cdd:cd01380 159 RTYLLEKSRVVFQAEEERNYHIFYQLCAAasLPELKELHLGSAE-DFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGIS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 355 PDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTC 434
Cdd:cd01380 238 EEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 435 AVGALSKSMYERMFKWLVARINRALDAKLSRQF--FIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEE 512
Cdd:cd01380 318 ARDALAKHIYAQLFDWIVDRINKALASPVKEKQhsFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 513 YKKESIEWVSIGFgLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSV-HLQKPKPDKKKfeahFEL 591
Cdd:cd01380 398 YVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkHFKKPRFSNTA----FIV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 592 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRllaslfenymstdsaipfgeKKrkkgasfqTVASLHKENLNKLM 671
Cdd:cd01380 473 KHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR--------------------KK--------TVGSQFRDSLILLM 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 672 TNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKfvSSR 751
Cdd:cd01380 525 ETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRD--DKK 602
|
650 660
....*....|....*....|....*..
gi 119600132 752 KAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd01380 603 KTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
117-778 |
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: 670.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAAMIESRKKQGA-------LEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARG 269
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSialshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 270 MLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 349
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 350 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTI 429
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 430 EQVTCAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFV 507
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALD-KTKRQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 508 LEQEEYKKESIEWVSIGFGLDLQACIDLIEKPM---GILSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKpdKKK 584
Cdd:cd14932 400 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQ-GNNPKFQKPK--KLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 585 FEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY--------MSTDSAIPFGEKKRKKGAsF 656
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdrivgldkVAGMGESLHGAFKTRKGM-F 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 657 QTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCI 736
Cdd:cd14932 556 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 119600132 737 LNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14932 636 LTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
117-778 |
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: 649.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAAMIESRKKQ---GALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 273
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 274 VDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKEL--HDLLLVSANpsDFHFCSCGAVTVESLDDAEELLATEQAMDIL 351
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKmrSDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETLEAMSIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 352 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQ 431
Cdd:cd14921 239 GFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 432 VTCAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLE 509
Cdd:cd14921 319 ADFAIEALAKATYERLFRWILTRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 510 QEEYKKESIEWVSIGFGLDLQACIDLIEKPM---GILSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKPDKKKFE 586
Cdd:cd14921 398 QEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 587 ahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY----------MSTDSAIPFGEKKRKkgASF 656
Cdd:cd14921 477 --FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqmaKMTESSLPSASKTKK--GMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 657 QTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCI 736
Cdd:cd14921 553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 119600132 737 LNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14921 633 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
117-778 |
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: 644.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 276
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 277 DIYLLEKSRVIFQQAGERNYHIFYQILSGQKE--LHDLLLVSANpsDFHFCSCGAVTVESLDDAEELLATEQAMDILGFL 354
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEhlKTDLLLEPYN--KYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 355 PDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTC 434
Cdd:cd14919 239 EEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 435 AVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEE 512
Cdd:cd14919 319 AIEALAKATYERMFRWLVLRINKALD-KTKRQgaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 513 YKKESIEWVSIGFGLDLQACIDLIEKPM---GILSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKPDKKKfeAHF 589
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK--ADF 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 590 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMS----------TDSAIPFGEKKRKkgASFQTV 659
Cdd:cd14919 475 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmSETALPGAFKTRK--GMFRTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 660 ASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNP 739
Cdd:cd14919 553 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 632
|
650 660 670
....*....|....*....|....*....|....*....
gi 119600132 740 RTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14919 633 NSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
117-778 |
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: 638.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAAMIESRKKQ-------GALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARG 269
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQnslalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 270 MLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILS--GQKELHDLLLVSANpsDFHFCSCGAVTVESLDDAEELLATEQA 347
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTgaGDKLRSELLLENYN--NYRFLSNGNVTIPGQQDKDLFTETMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 348 MDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQ 427
Cdd:cd15896 239 FRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 428 TIEQVTCAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHM 505
Cdd:cd15896 319 TQEQAEFAVEALAKATYERMFRWLVMRINKALD-KTKRQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 506 FVLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPM---GILSILEEECMFPKATDLTFKTKLFDNhfgKSVHLQKPKPDK 582
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQE---QGTHPKFFKPKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 583 KKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY--------MSTDSAIPFGEKKRKkgA 654
Cdd:cd15896 475 LKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVdrivgldkVSGMSEMPGAFKTRK--G 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 655 SFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRY 734
Cdd:cd15896 553 MFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 119600132 735 CILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd15896 633 EILTPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
117-778 |
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: 618.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAAMIESRKKQGA---LEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 273
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 274 VDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESlDDAEELLATEQAMDILGF 353
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 354 LPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVT 433
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 434 CAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQE 511
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 512 EYKKESIEWVSIGFGLDLQACIDLIEKPM---GILSILEEECMFPKATDLTFKTKLFDNhfgKSVHLQKPKPDKKKFEAH 588
Cdd:cd14930 399 EYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQE---QGGHPKFQRPRHLRDQAD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 589 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF---------ENYMSTDSAIPFGEKKRkkgASFQTV 659
Cdd:cd14930 476 FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegivglEQVSSLGDGPPGGRPRR---GMFRTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 660 ASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNP 739
Cdd:cd14930 553 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 632
|
650 660 670
....*....|....*....|....*....|....*....
gi 119600132 740 RTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14930 633 NAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
118-778 |
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: 607.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYkGKRRSEaPPHIFAVANNAFQDMLHNRENQSILFTGE 197
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY-RQKLLD-SPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 198 SGAGKTVNSKHIIQYFATIAAmiesrkKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDID 277
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGG------GSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 278 IYLLEKSRVIFQQAGERNYHIFYQILSG-QKELHDLLLVSAnPSDFHFCS-CGAVTVESLDDAEELLATEQAMDILGFLP 355
Cdd:cd01383 154 TYLLEKSRVVQLANGERSYHIFYQLCAGaSPALREKLNLKS-ASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGISK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 356 DEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCA 435
Cdd:cd01383 233 EDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 436 VGALSKSMYERMFKWLVARINRALDAKLSRQF-FIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYK 514
Cdd:cd01383 313 RDALAKAIYASLFDWLVEQINKSLEVGKRRTGrSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 515 KESIEWVSIGFgLDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKLfdnhfgkSVHLQKPKPDKKKFEAHFELVH 593
Cdd:cd01383 393 LDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-------KQHLKSNSCFKGERGGAFTIRH 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 594 YAGVVPYNISGWLEKNKDLLNETVVAVFQkSSNRLLASLFENYMSTDSAIPFGEKKRKKGASF-QTVASLHKENLNKLMT 672
Cdd:cd01383 465 YAGEVTYDTSGFLEKNRDLLHSDLIQLLS-SCSCQLPQLFASKMLDASRKALPLTKASGSDSQkQSVATKFKGQLFKLMQ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 673 NLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVSSRK 752
Cdd:cd01383 544 RLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLSTS 623
|
650 660
....*....|....*....|....*.
gi 119600132 753 AAeeLLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd01383 624 VA--ILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
117-778 |
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: 606.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAAmiesrkKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 276
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISG------QHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 277 DIYLLEKSRVIFQQAGERNYHIFYQILSG----QKELHDLllvsANPSDFHFCSCG-AVTVESLDDAEELLATEQAMDIL 351
Cdd:cd01381 155 EQYLLEKSRIVSQAPDERNYHIFYCMLAGlsaeEKKKLEL----GDASDYYYLTQGnCLTCEGRDDAAEFADIRSAMKVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 352 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPRE--EQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTI 429
Cdd:cd01381 231 MFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 430 EQVTCAVGALSKSMYERMFKWLVARINRAL---DAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMF 506
Cdd:cd01381 311 EQALDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 507 VLEQEEYKKESIEWVSIGFgLDLQACIDLI-EKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLqKPKPDkkkF 585
Cdd:cd01381 391 KLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYL-KPKSD---L 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 586 EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMStdsaipFGEKKRKKGasfQTVASLHKE 665
Cdd:cd01381 466 NTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDIS------MGSETRKKS---PTLSSQFRK 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 666 NLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTfPKS 745
Cdd:cd01381 537 SLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGI-PPA 615
|
650 660 670
....*....|....*....|....*....|...
gi 119600132 746 KFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd01381 616 HKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
118-778 |
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: 604.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 197
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 198 SGAGKTVNSKHIIQYFATIAAMIESrkKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDID 277
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSES--EVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 278 IYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLVSaNPSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFLP 355
Cdd:cd01378 160 NYLLEKSRVVGQIKGERNFHIFYQLLKGasQEYLQELGLQR-PEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 356 DEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTEnADKAAFLMGINSSELVKCLIHPRIKVGNEY---VTRGQTIEQV 432
Cdd:cd01378 239 EEQDSIFRILAAILHLGNIQFAEDEEGNAAISDTSV-LDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 433 TCAVGALSKSMYERMFKWLVARINRALDAKLSRQ-FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFnwHMFVL--E 509
Cdd:cd01378 318 AYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF--IELTLkaE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 510 QEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGILSILEEECMFP-KATDLTFKTKLfDNHFGKSVHLQKPKPDKKKFEA 587
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHFELRRG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 588 HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSaipfgeKKRKKGASFQTVASlhkenL 667
Cdd:cd01378 474 EFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDS------KKRPPTAGTKFKNS-----A 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 668 NKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKF 747
Cdd:cd01378 543 NALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDG 622
|
650 660 670
....*....|....*....|....*....|.
gi 119600132 748 vSSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd01378 623 -TWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
118-778 |
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: 602.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 197
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 198 SGAGKTVNSKHIIQYFATIAAmiesrkKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDID 277
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTN------NHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 278 IYLLEKSRVIFQQAGERNYHIFYQILSG---QKELHDLLLVSaNPSDFHFCS-CGAVTVESLDDAEELLATEQAMDILGF 353
Cdd:cd14883 156 DYLLEQSRITFQAPGERNYHVFYQLLAGakhSKELKEKLKLG-EPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVLGI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 354 LPDEKYGCYKLTGAIMHFGNMKFKQKPREE-QLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQV 432
Cdd:cd14883 235 PEEMQEGIFSVLSAILHLGNLTFEDIDGETgALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 433 TCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEE 512
Cdd:cd14883 315 RDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 513 YKKESIEWVSIGFGlDLQACIDLIEK-PMGILSILEEECMFPKATDLTFKTKLFDNHfgkSVHLQKPKPDKKKFEAHFEL 591
Cdd:cd14883 395 YEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH---EKHPYYEKPDRRRWKTEFGV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 592 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF---ENYMSTDSAIPFGE----KKRKKGASfqTVASLHK 664
Cdd:cd14883 471 KHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtypDLLALTGLSISLGGdttsRGTSKGKP--TVGDTFK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 665 ENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPK 744
Cdd:cd14883 549 HQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSA 628
|
650 660 670
....*....|....*....|....*....|....
gi 119600132 745 SKfVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14883 629 DH-KETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
117-778 |
3.94e-179 |
|
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: 558.06 E-value: 3.94e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 195
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 196 GESGAGKTVNSKHIIQYFATIAAMIESrkKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 275
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVT--EGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 276 IDIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLvsANPSDFHF---CSCgaVTVESLDDAEELLATEQAMDI 350
Cdd:cd01384 159 IRTYLLERSRVVQVSDPERNYHCFYQLCAGapPEDREKYKL--KDPKQFHYlnqSKC--FELDGVDDAEEYRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 351 LGFLPDEKYGCYKLTGAIMHFGNMKFKQKPreeqlEADGTENADK--------AAFLMGINSSELVKCLIHPRIKVGNEY 422
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGNIEFSKGE-----EDDSSVPKDEksefhlkaAAELLMCDEKALEDALCKRVIVTPDGI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 423 VTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFN 502
Cdd:cd01384 310 ITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 503 WHMFVLEQEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKLFDNhFGKSVHLQKPKPD 581
Cdd:cd01384 390 QHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPKLS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 582 KKKfeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEnymstdsaiPFGEKKRKKGASFQTVAS 661
Cdd:cd01384 468 RTD----FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFP---------PLPREGTSSSSKFSSIGS 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 662 LHKENLNKLMTNLKSTAPHFVRCINPN-VNKiPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPR 740
Cdd:cd01384 535 RFKQQLQELMETLNTTEPHYIRCIKPNnLLK-PGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPE 613
|
650 660 670
....*....|....*....|....*....|....*...
gi 119600132 741 TFPKSKfvSSRKAAEELLGSLEIDhtQYRFGITKVFFK 778
Cdd:cd01384 614 VLKGSD--DEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
117-778 |
1.30e-169 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 532.21 E-value: 1.30e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 195
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 196 GESGAGKTVNSKHIIQYfatiaaMIESR-KKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSV 274
Cdd:cd01382 81 GESGAGKTESTKYILRY------LTESWgSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 275 DIDIYLLEKSRVIFQQAGERNYHIFYQILSG------QKELHDLLlvsanpsdfhfcscgavtvesLDDAEELLATEQAM 348
Cdd:cd01382 155 FVSHYLLEKSRICVQSKEERNYHIFYRLCAGapedlrEKLLKDPL---------------------LDDVGDFIRMDKAM 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 349 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREE----QLEADGTENADKAAFLMGINSSELVKCLIHpRIKVGNEYVT 424
Cdd:cd01382 214 KKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSgggcNVKPKSEQSLEYAAELLGLDQDELRVSLTT-RVMQTTRGGA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 425 RGQTI------EQVTCAVGALSKSMYERMFKWLVARINRALDAKLSrQFFIGILDITGFEILEYNSLEQLCINFTNEKLQ 498
Cdd:cd01382 293 KGTVIkvplkvEEANNARDALAKAIYSKLFDHIVNRINQCIPFETS-SYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 499 QFFNWHMFVLEQEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGILSILEEECMFPKATdltfktklfDNHFGKSVHLQK 577
Cdd:cd01382 372 QFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPS---------DQHFTSAVHQKH 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 578 PK------PDKKKFEAHFELV--------HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSai 643
Cdd:cd01382 442 KNhfrlsiPRKSKLKIHRNLRddegflirHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK-- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 644 pfGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPN 723
Cdd:cd01382 520 --DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPS 597
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119600132 724 RLQYADFKQRY--------CILNPRTFPKSKFvssrKAaeelLGSLEIDhtqYRFGITKVFFK 778
Cdd:cd01382 598 RTSFHDLYNMYkkylppklARLDPRLFCKALF----KA----LGLNEND---FKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
117-778 |
2.68e-166 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 523.18 E-value: 2.68e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAAmiesrkKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 276
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAG------STNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 277 DIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSAnpSDFHFCSC-GAVTVESLDDAEELLATEQAMDILGFLP 355
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSS--AAYGYLSLsGCIEVEGVDDVADFEEVVLAMEQLGFDD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 356 DEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENAD---KAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQ-TIEQ 431
Cdd:cd14872 233 ADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDvlkEVATLLGVDAATLEEALTSRLMEIKGCDPTRIPlTPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 432 VTCAVGALSKSMYERMFKWLVARINRALD-AKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQ 510
Cdd:cd14872 313 ATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 511 EEYKKESIEWVSIGFgLDLQACIDLIEK-PMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKpkpDKKKFEAHF 589
Cdd:cd14872 393 ALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYA---EVRTSRTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 590 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEnymstdsaiPF-GEKKRKKgasfQTVASLHKENLN 668
Cdd:cd14872 469 IVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP---------PSeGDQKTSK----VTLGGQFRKQLS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 669 KLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILnPRTFPKSKFV 748
Cdd:cd14872 536 ALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIAKRVGP 614
|
650 660 670
....*....|....*....|....*....|
gi 119600132 749 SSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14872 615 DDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
118-778 |
7.29e-166 |
|
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: 521.45 E-value: 7.29e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 197
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 198 SGAGKTVNSKHIIQYFATIaamieSRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDID 277
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-----GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 278 IYLLEKSRVIFQQAGERNYHIFYQILSG---QKELHDLLLVSANPSD-FHFCSCGAVTVESLD-DAEELLATEQAMDILG 352
Cdd:cd01379 157 EYLLEKSRVVHQAIGERNFHIFYYIYAGlaeDKKLAKYKLPENKPPRyLQNDGLTVQDIVNNSgNREKFEEIEQCFKVIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 353 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEAD----GTENADKAAFLMGINSSELVKCLIHprikvgNEYVTRGQT 428
Cdd:cd01379 237 FTKEEVDSVYSILAAILHIGDIEFTEVESNHQTDKSsrisNPEALNNVAKLLGIEADELQEALTS------HSVVTRGET 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 429 I------EQVTCAVGALSKSMYERMFKWLVARINRALdaKLSR-----QFFIGILDITGFEILEYNSLEQLCINFTNEKL 497
Cdd:cd01379 311 IirnntvEEATDARDAMAKALYGRLFSWIVNRINSLL--KPDRsasdePLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 498 QQFFNWHMFVLEQEEYKKESIEWVSIGFG-----LDLqacidLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHfgKS 572
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 573 VHLQKPKPDkkkfEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLAslfenymstdsaipfgekkrkk 652
Cdd:cd01379 462 KYYWRPKSN----ALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR---------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 653 gasfQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQ 732
Cdd:cd01379 516 ----QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLK 591
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 119600132 733 RYCILnprTFPKSKFV-SSRKAAEELLGSLEIDHtqYRFGITKVFFK 778
Cdd:cd01379 592 RYYFL---AFKWNEEVvANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
117-778 |
3.89e-164 |
|
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: 518.09 E-value: 3.89e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSeAPPHIFAVANNAFQDMLHNRENQSILFT 195
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSIS-KSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 196 GESGAGKTVNSKHIIQYFATiaAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHF---------G 266
Cdd:cd14888 80 GESGAGKTESTKYVMKFLAC--AGSEDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklkskrmsG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 267 ARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKEL-----------------HDLLLVSANPSDFH------ 323
Cdd:cd14888 158 DRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAkntglsyeendeklakgADAKPISIDMSSFEphlkfr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 324 --FCScGAVTVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFK-QKPREE--QLEADGTENADKAAF 398
Cdd:cd14888 238 ylTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEnNEACSEgaVVSASCTDDLEKVAS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 399 LMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALD-AKLSRQFFIGILDITGF 477
Cdd:cd14888 317 LLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGVLDIFGF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 478 EILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLI-EKPMGILSILEEECMFPKAT 556
Cdd:cd14888 397 ECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEECFVPGGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 557 DLTFKTKLFDNHFG-KSVHLQKPKPDKkkfeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN 635
Cdd:cd14888 476 DQGLCNKLCQKHKGhKRFDVVKTDPNS------FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 636 YMstDSAIPFGEKKRKkgasFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTR 715
Cdd:cd14888 550 YL--RRGTDGNTKKKK----FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQ 623
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119600132 716 ICREGFPNRLQYADFKQRYCILNPrtfpkskfvssrkaaeellGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14888 624 VSRAGYPVRLSHAEFYNDYRILLN-------------------GEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
117-778 |
9.54e-162 |
|
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: 511.24 E-value: 9.54e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 195
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 196 GESGAGKTVNSKHIIQYFATIAamiesrkkqGALED----QIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 271
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA---------GGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 272 SSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFcSCGAVTVESLDDAEELLATEQAMDIL 351
Cdd:cd14903 152 VGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 352 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLE--ADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTI 429
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 430 EQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLE 509
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 510 QEEYKKESIEWVSIGFgLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHf 589
Cdd:cd14903 391 QIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIK- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 590 elvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEK----KRKKGA-SFQTVASLHK 664
Cdd:cd14903 469 ---HYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLArgarRRRGGAlTTTTVGTQFK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 665 ENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPK 744
Cdd:cd14903 546 DSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGRNT 625
|
650 660 670
....*....|....*....|....*....|....*
gi 119600132 745 SKFVssRKAAEELLGSLEIDH-TQYRFGITKVFFK 778
Cdd:cd14903 626 DVPV--AERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
117-778 |
8.14e-159 |
|
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: 503.14 E-value: 8.14e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQ-KEVMAAYK-GKRRSEAPPHIFAVANNAFQDMLHNR----EN 189
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPlLYDvPGFDSQRKeEATASSPPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 190 QSILFTGESGAGKTVNSKHIIQYFATIAAMIESRKKQGA-------LEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIR 262
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGaanahesIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 263 MHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCG-AVTVESLDDAEEL 341
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 342 LATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQ--KPREEQLEADGTENADKAAFLMGINSSELVKCLIhPRIKVG 419
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLV-TQTTST 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 420 neyvTRGQ------TIEQVTCAVGALSKSMYERMFKWLVARINRA----------LDAKLSRQFFIGILDITGFEILEYN 483
Cdd:cd14892 320 ----ARGSvleiklTAREAKNALDALCKYLYGELFDWLISRINAChkqqtsgvtgGAASPTFSPFIGILDIFGFEIMPTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 484 SLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIEK-PMGILSILEEECMFP-KATDLTFK 561
Cdd:cd14892 396 SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 562 TKLFDNHFGKSVHLQKPkpdkkKFEA-HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNrllaslfenymstd 640
Cdd:cd14892 475 TIYHQTHLDKHPHYAKP-----RFECdEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK-------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 641 saipfgekkrkkgasFQTvaslhkeNLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREG 720
Cdd:cd14892 536 ---------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREG 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119600132 721 FPNRLQYADFKQRYCIL---------NPRTfpKSKFVSSRKAAEELLGSLEIDHTQyrFGITKVFFK 778
Cdd:cd14892 594 FPIRRQFEEFYEKFWPLarnkagvaaSPDA--CDATTARKKCEEIVARALERENFQ--LGRTKVFLR 656
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
117-778 |
2.18e-156 |
|
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: 497.67 E-value: 2.18e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIaamieSRKKQGA-LEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 275
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTAL-----SQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 276 IDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGA-VTVESLDDAEELLATEQAMDILGFL 354
Cdd:cd01385 156 VEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDcYTLEGEDEKYEFERLKQAMEMVGFL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 355 PDEKYGCYKLTGAIMHFGNMKFKQKP--REEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQV 432
Cdd:cd01385 236 PETQRQIFSVLSAVLHLGNIEYKKKAyhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 433 TCAVGALSKSMYERMFKWLVARINRALDAKLS----RQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVL 508
Cdd:cd01385 316 IATRDAMAKCLYSALFDWIVLRINHALLNKKDleeaKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 509 EQEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKlFDNHFGKSVHLQKPkpdkKKFEA 587
Cdd:cd01385 396 EQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKP----QVMEP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 588 HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSN------------------------RLLASLFE--------- 634
Cdd:cd01385 470 AFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSafvreligidpvavfrwavlraffRAMAAFREagrrraqrt 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 635 ---NYMSTDSAIPFGEKKRKK------GASFQTvaslhkeNLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQL 705
Cdd:cd01385 550 aghSLTLHDRTTKSLLHLHKKkkppsvSAQFQT-------SLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQL 622
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119600132 706 RCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKfvSSRKaaeELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd01385 623 RYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSK--EDIK---DFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
117-776 |
3.65e-156 |
|
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: 495.85 E-value: 3.65e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAY------KGKRRSEAPPHIFAVANNAFQDMLHNRE-- 188
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 189 --NQSILFTGESGAGKTVNSKHIIQYFATIAamieSRKKQGA-------LEDQIMQANTILEAFGNAKTLRNDNSSRFGK 259
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVS----SATTHGQnaterenVRDRVLESNPILEAFGNARTNRNNNSSRFGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 260 FIRMHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLVSANPSDFHFCSCGAVTVESLDD 337
Cdd:cd14901 157 FIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGasSDELHALGLTHVEEYKYLNSSQCYDRRDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 338 AEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPRE-EQLEADGTENADKAAFLMGINSSELVKCLIHPRI 416
Cdd:cd14901 237 SVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEgGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 417 KVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLS--RQFFIGILDITGFEILEYNSLEQLCINFTN 494
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 495 EKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKLFDNhFGKSV 573
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 574 HLQKPKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASlfenymstdsaipfgekkrkkg 653
Cdd:cd14901 475 SFSVSKLQQGK--RQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS---------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 654 asfqTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQR 733
Cdd:cd14901 531 ----TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHT 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 119600132 734 YCILNPRTfpKSKFVSSRKAAEELLGSLEI------DHTQYRFGITKVF 776
Cdd:cd14901 607 YSCLAPDG--ASDTWKVNELAERLMSQLQHselnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
117-778 |
2.10e-154 |
|
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: 491.19 E-value: 2.10e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAamiesrKKQGAL-EDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFgARGMLSSVD 275
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN------QRRNNLvTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 276 IDIYLLEKSRVIFQQAGERNYHIFYQILSG----QKELHDLLlvsaNPSDFHFC----SCGAVTVESLDDAEELLAteqA 347
Cdd:cd01387 154 TSQYLLEKSRIVTQAKNERNYHVFYELLAGlpaqLRQKYGLQ----EAEKYFYLnqggNCEIAGKSDADDFRRLLA---A 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 348 MDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPRE---EQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVT 424
Cdd:cd01387 227 MQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 425 RGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWH 504
Cdd:cd01387 307 TPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKH 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 505 MFVLEQEEYKKESIEWVSIGFgLDLQACIDLI-EKPMGILSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKPDkk 583
Cdd:cd01387 387 VFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPRMP-- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 584 kfEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMS-TDSAIPFGEKKRKKGASFQ--TVA 660
Cdd:cd01387 463 --LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAqTDKAPPRLGKGRFVTMKPRtpTVA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 661 SLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPR 740
Cdd:cd01387 541 ARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVAL 620
|
650 660 670
....*....|....*....|....*....|....*....
gi 119600132 741 TFPKS-KFVSSRKAAEELLGSLEIDhtQYRFGITKVFFK 778
Cdd:cd01387 621 KLPRPaPGDMCVSLLSRLCTVTPKD--MYRLGATKVFLR 657
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
117-778 |
1.26e-153 |
|
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: 489.29 E-value: 1.26e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAF----QDMLHNRENQS 191
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtqliQSGVLDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 192 ILFTGESGAGKTVNSKHIIQYFATI-------------AAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFG 258
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARItsgfaqgasgegeAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 259 KFIRMHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKE--LHDLLLVSANPSDFHFCSCGAVtvESLD 336
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEalRERLKLQTPVEYFYLRGECSSI--PSCD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 337 DAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGT-ENADKAAFLMGINSSELVKCLIHPR 415
Cdd:cd14890 239 DAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 416 IKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNE 495
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 496 KLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGILSILE--EEC--MFPKATDLTFKTKLFDNHFG 570
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFItlDDCwrFKGEEANKKFVSQLHASFGR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 571 KSV------------HLQKPKPDKKKfeaHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLlaslfenyms 638
Cdd:cd14890 478 KSGsggtrrgssqhpHFVHPKFDADK---QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI---------- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 639 tdsaipfgekkrkKGASfqtVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICR 718
Cdd:cd14890 545 -------------REVS---VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQ 608
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 719 EGFPNRLQYADFKQRYCILNPRTFPKSKFVssrkaaEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14890 609 QGFALREEHDSFFYDFQVLLPTAENIEQLV------AVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
117-778 |
1.07e-149 |
|
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: 478.14 E-value: 1.07e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 195
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 196 GESGAGKTVNSKHIIQYFATIAAMI---ESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 272
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSlelSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 273 SVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCS-CGAVTVESLDDAEELLATEQAMDIL 351
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 352 GFLPDEKYGCYKLTGAIMHFGNMKFkqkpreeqLEADGTENADKAAF-----LMGINSSELVKCLIHPRIKVGNEYVTRG 426
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKTALgrsaeLLGLDPTQLTDALTQRSMFLRGEEILTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 427 QTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQfFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMF 506
Cdd:cd14873 313 LNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 507 VLEQEEYKKESIEWVSIGFgLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLfdnhfgKSVHLQKPKPDKKKFE 586
Cdd:cd14873 392 SLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKL------HSQHANNHFYVKPRVA 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 587 AH-FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSA-IPFGEKKRKKgasfQTVASLHK 664
Cdd:cd14873 465 VNnFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQdTLKCGSKHRR----PTVSSQFK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 665 ENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTfpk 744
Cdd:cd14873 541 DSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL--- 617
|
650 660 670
....*....|....*....|....*....|....
gi 119600132 745 SKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14873 618 ALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
117-778 |
4.06e-147 |
|
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: 470.33 E-value: 4.06e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKR-RSEAPPHIFAVANNAFQDMLHNRENQSILFT 195
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 196 GESGAGKTVNSKHIIQYFATIaamieSRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 275
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKL-----SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 276 IDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQA-------M 348
Cdd:cd14897 156 IDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDSEELEYYRQMfhdltniM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 349 DILGFLPDEKYGCYKLTGAIMHFGNMKFkqkprEEQLEADGTENADK-----AAFLMGINSSELVKCLIHPRIKVGNEYV 423
Cdd:cd14897 236 KLIGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTIRGERI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 424 TRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAK-----LSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQ 498
Cdd:cd14897 311 QSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDkdfqiMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 499 QFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLI-EKPMGILSILEEECMFPKATDLTFKTKLfDNHFGKSVHLQK 577
Cdd:cd14897 391 QYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVA 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 578 PKPDKKKFEAHfelvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMstdsaipfgekkrkkgasfq 657
Cdd:cd14897 469 SPGNRVAFGIR----HYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSYF-------------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 658 tvaslhKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCIL 737
Cdd:cd14897 525 ------KRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEI 598
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 119600132 738 NPrtFPKSKFVSSRKAAEELLGSLEIDhtQYRFGITKVFFK 778
Cdd:cd14897 599 CD--FSNKVRSDDLGKCQKILKTAGIK--GYQFGKTKVFLK 635
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
119-778 |
9.29e-144 |
|
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: 462.07 E-value: 9.29e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 119 VLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDML----HNRENQSILF 194
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 195 TGESGAGKTVNSKHIIQYfatiaaMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFgARGMLSSV 274
Cdd:cd14889 83 SGESGAGKTESTKLLLRQ------IMELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 275 DIDIYLLEKSRVIFQQAGERNYHIFYQILSG----QKELHDLLlvsaNPSDFHFCSCGAVTVESLD----DAEELLateQ 346
Cdd:cd14889 156 KINEYLLEKSRVVHQDGGEENFHIFYYMFAGisaeDRENYGLL----DPGKYRYLNNGAGCKREVQywkkKYDEVC---N 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 347 AMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQkpreEQLEADGTENADK-----AAFLMGINSSELVKCLIHPRIKVGNE 421
Cdd:cd14889 229 AMDMVGFTEQEEVDMFTILAGILSLGNITFEM----DDDEALKVENDSNgwlkaAAGQFGVSEEDLLKTLTCTVTFTRGE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 422 YVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQF---FIGILDITGFEILEYNSLEQLCINFTNEKLQ 498
Cdd:cd14889 305 QIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVelrEIGILDIFGFENFAVNRFEQACINLANEQLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 499 QFFNWHMFVLEQEEYKKESIEWVSIGFgLDLQACIDL-IEKPMGILSILEEECMFPKATDLTFKTKLfDNHFGKSVHLQK 577
Cdd:cd14889 385 YFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 578 PKPDKKKfeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMS-TDSAIPFGEKKRKKGASF 656
Cdd:cd14889 463 SRSKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSrTGTLMPRAKLPQAGSDNF 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 657 -----QTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFK 731
Cdd:cd14889 539 nstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFA 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 119600132 732 QRYCILnprtFPKSKFVSSRKAAEELLGSLEIdhTQYRFGITKVFFK 778
Cdd:cd14889 619 ERYKIL----LCEPALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
118-737 |
4.42e-137 |
|
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: 442.05 E-value: 4.42e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAY-----------KGKRRSEAPPHIFAVANNAFQDMLH 185
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 186 NR----ENQSILFTGESGAGKTVNSKHIIQYFATI-----AAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSR 256
Cdd:cd14900 82 GLngvmSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 257 FGKFIRMHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHdlllvsanpsdfhfcscgavtvESLD 336
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAA----------------------RKRD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 337 DAEELLAteqAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENA-------DKAAFLMGINSSELVK 409
Cdd:cd14900 220 MYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 410 CLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRAL---DAKLSRQ--FFIGILDITGFEILEYNS 484
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGglHFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 485 LEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLI-EKPMGILSILEEECMFPKATDLTFKTK 563
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLASK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 564 LFdNHFGKSVHLQKPKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQkssnrllaslfenymstdsai 643
Cdd:cd14900 456 LY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV--------------------- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 644 pfgekkrkKGASFqtvaslhKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPN 723
Cdd:cd14900 512 --------YGLQF-------KEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPI 576
|
650
....*....|....
gi 119600132 724 RLQYADFKQRYCIL 737
Cdd:cd14900 577 RLLHDEFVARYFSL 590
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
117-757 |
6.76e-136 |
|
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: 442.02 E-value: 6.76e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYK--------GKRRSEAPPHIFAVANNAFQDMLHN- 186
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 187 RENQSILFTGESGAGKTVNSKHIIQYFATIAAMIESRKKQGA----LEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIR 262
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSdaveIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 263 MHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG-QKELHDLLLVSAN----PSDFHFCSCGAVTVESLDD 337
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGaDKTLLDLLGLQKGgkyeLLNSYGPSFARKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 338 AEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFK---QKPREEQLEADGTENADKAAFLMGINSSELVKCLIHP 414
Cdd:cd14902 241 AQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTaenGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 415 RIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFF---------IGILDITGFEILEYNSL 485
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 486 EQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKL 564
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSNQALSTKF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 565 FDNHFGksvhlqkpkpdkkkfEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIP 644
Cdd:cd14902 480 YRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSPGAD 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 645 FGEKKRKKGASFQT--VASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFP 722
Cdd:cd14902 545 NGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYS 624
|
650 660 670
....*....|....*....|....*....|....*
gi 119600132 723 NRLQYADFKQRYCILNPrtFPKSKFVSSRKAAEEL 757
Cdd:cd14902 625 VRLAHASFIELFSGFKC--FLSTRDRAAKMNNHDL 657
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
117-778 |
3.29e-131 |
|
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: 426.67 E-value: 3.29e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 195
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 196 GESGAGKTVNSKHIIQYFATIAAmieSRKKQGAleDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 275
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTI--AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 276 IDIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILGF 353
Cdd:cd14904 156 CETYLLEKSRVVSIAEGERNYHIFYQLLAGlsSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 354 LPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGtENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVT 433
Cdd:cd14904 236 DNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNG-SQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 434 CAVGALSKSMYERMFKWLVARINRAL---DAKLSRQffIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQ 510
Cdd:cd14904 315 ENRDALAKAIYSKLFDWMVVKINAAIstdDDRIKGQ--IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 511 EEYKKESIEWVSIGFGlDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNH--FGKSVHLQKPKPDKKKFEAH 588
Cdd:cd14904 393 EEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKRTQFIIN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 589 felvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIpfGEKKRKKGASFQTVASLHKENLN 668
Cdd:cd14904 472 ----HYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETK--EGKSGKGTKAPKSLGSQFKTSLS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 669 KLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILnprtFPKSKFV 748
Cdd:cd14904 546 QLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM----FPPSMHS 621
|
650 660 670
....*....|....*....|....*....|..
gi 119600132 749 -SSRKAAEELLGSL-EIDHTQYRFGITKVFFK 778
Cdd:cd14904 622 kDVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
117-746 |
7.31e-131 |
|
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: 426.37 E-value: 7.31e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGK--------RRSEAPPHIFAVANNAFQDMLHNR 187
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 188 ENQSILFTGESGAGKTVNSKHIIQYFATIAA--------------MIESRKKQGALEDQIMQANTILEAFGNAKTLRNDN 253
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 254 SSRFGKFIRMHFGAR-GMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLVSANPSDFHFC--SCG 328
Cdd:cd14907 161 SSRFGKYVSILVDKKkRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGadQQLLQQLGLKNQLSGDRYDYlkKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 329 AVTVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKP--REEQLEADGTENADKAAFLMGINSSE 406
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 407 LVKCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRAL--------DAKLSRQFFIGILDITGFE 478
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 479 ILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIE-WVS-IGFgLDLQACIDLIEK-PMGILSILEEECMFPKA 555
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdYLNqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 556 TDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEahfeLVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFen 635
Cdd:cd14907 480 TDEKLLNKIKKQHKNNSKLIFPNKINKDTFT----IRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF-- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 636 YMSTDSAIPFGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTR 715
Cdd:cd14907 554 SGEDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIR 633
|
650 660 670
....*....|....*....|....*....|..
gi 119600132 716 ICREGFPNRLQYADFKQRYCILNP-RTFPKSK 746
Cdd:cd14907 634 VRKQGYPYRKSYEDFYKQYSLLKKnVLFGKTK 665
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
79-838 |
1.11e-128 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 425.21 E-value: 1.11e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 79 VETADGESLSIKEDKIQQMNPP-EFEMIEDMAMLTHLNEASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVM 157
Cdd:PTZ00014 71 IDPPTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 158 AAYKGKRRSEA-PPHIFAVANNAFQDMLHNRENQSILFTGESGAGKTVNSKHIIQYFATIAAMIESRKKQGAledqIMQA 236
Cdd:PTZ00014 151 RRYRDAKDSDKlPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNA----IMAA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 237 NTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG-----QKELHD 311
Cdd:PTZ00014 227 NPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGandemKEKYKL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 312 LLLvsanpSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTE 391
Cdd:PTZ00014 307 KSL-----EEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAIS 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 392 NADKAAF-----LMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQ 466
Cdd:PTZ00014 382 DESLEVFneaceLLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFK 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 467 FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSIL 546
Cdd:PTZ00014 462 VFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSIL 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 547 EEECMFPKATDLTFkTKLFDNHFGKSVHLQKPKPDKKKfeaHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSN 626
Cdd:PTZ00014 542 EDQCLAPGGTDEKF-VSSCNTNLKNNPKYKPAKVDSNK---NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPN 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 627 RLLASLFENYMSTDSAIpfgekkrKKGasfQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLR 706
Cdd:PTZ00014 618 PLVRDLFEGVEVEKGKL-------AKG---QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLH 687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 707 CNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKfVSSRKAAEELLGSLEIDHTQYRFGITKVFFKAGFLGQLE 786
Cdd:PTZ00014 688 SLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSS-LDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELT 766
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 119600132 787 AIRDERLSKVFTLFQArAQGKLMRIKFQKILEER-DALILIQWNIRAFMAVKN 838
Cdd:PTZ00014 767 QIQREKLAAWEPLVSV-LEALILKIKKKRKVRKNiKSLVRIQAHLRRHLVIAE 818
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
117-778 |
1.24e-126 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 413.29 E-value: 1.24e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRY---GQwMIYTYSGLFCVTINPYKWLPVYQKEvmaAYKGKRRSEAPPHIFAVANNAFQDMLHNRE---NQ 190
Cdd:cd14891 1 AGILHNLEERSkldNQ-RPYTFMANVLIAVNPLRRLPEPDKS---DYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 191 SILFTGESGAGKTVNSKHIIQY------------FATIAAMIESRKKQGA-LEDQIMQANTILEAFGNAKTLRNDNSSRF 257
Cdd:cd14891 77 SIVISGESGAGKTETSKIILRFlttravggkkasGQDIEQSSKKRKLSVTsLDERLMDTNPILESFGNAKTLRNHNSSRF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 258 GKFIRMHFGARGM-LSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCS-CGAVTVESL 335
Cdd:cd14891 157 GKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 336 DDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKA----AFLMGINSSELVKCL 411
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEAlataAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 412 IHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILE-YNSLEQLCI 490
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 491 NFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLI-EKPMGILSILEEECMFPKATDLTFKTKLfDNHF 569
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETL-HKTH 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 570 GKSVHLQKPKPDKKKFEahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFqKSSNRLLASLFEnymstdsaipfgekk 649
Cdd:cd14891 475 KRHPCFPRPHPKDMREM--FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLL-ASSAKFSDQMQE--------------- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 650 rkkgasfqtvaslhkenlnkLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYAD 729
Cdd:cd14891 537 --------------------LVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAE 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 119600132 730 FKQRYCILNPrTFPKSKFVSSRKA-AEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14891 597 LVDVYKPVLP-PSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
117-746 |
2.39e-125 |
|
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: 411.22 E-value: 2.39e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYK--GKRRS---EAP----PHIFAVANNAFQDMLHN- 186
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 187 RENQSILFTGESGAGKTVNSKHIIQYFATI------AAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKF 260
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLgngeegAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 261 IRMHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG-------QKELHDLLLVSAN-PSDFHFCSCG-AVT 331
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGgdeeeheKYEFHDGITGGLQlPNEFHYTGQGgAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 332 VESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENAD---KAAFLMGINSSELV 408
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKclaRVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 409 KCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQF--FIGILDITGFEILEYNSLE 486
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrsSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 487 QLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGILSILEEECMFP-KATDLTFKTKL 564
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 565 FDNHFGKSvhlQKPKPDKKKFEAH--------FELVHYAGVVPYNI-SGWLEKNKDLLNETVvavfqkssnrllASLFEN 635
Cdd:cd14908 480 YETYLPEK---NQTHSENTRFEATsiqktkliFAVRHFAGQVQYTVeTTFCEKNKDEIPLTA------------DSLFES 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 636 ymstdsaipfgekkrkkGASFqtvaslhKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTR 715
Cdd:cd14908 545 -----------------GQQF-------KAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVR 600
|
650 660 670
....*....|....*....|....*....|.
gi 119600132 716 ICREGFPNRLQYADFKQRYCILNPrTFPKSK 746
Cdd:cd14908 601 VARSGYPVRLPHKDFFKRYRMLLP-LIPEVV 630
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
117-778 |
6.33e-124 |
|
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: 405.70 E-value: 6.33e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIaamieSRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFgARGMLSSVDI 276
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL-----YQDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 277 DIYLLEKSRVIFQQAGERNYHIFYQILSG----QKElhdLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILG 352
Cdd:cd14896 155 SHYLLETSRVVFQAQAERSFHVFYELLAGldpeERE---QLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 353 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENAD--KAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIE 430
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 431 QVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFF--IGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVL 508
Cdd:cd14896 312 GAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 509 EQEEYKKESIEWVSIgFGLDLQACIDLI-EKPMGILSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKPDKKKFEA 587
Cdd:cd14896 392 EEEECQRELLPWVPI-PQPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQLPLPVFTV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 588 HfelvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENymstdsaipfGEKKRKKGASFQTVASLHKENL 667
Cdd:cd14896 470 R----HYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE----------AEPQYGLGQGKPTLASRFQQSL 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 668 NKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRtfpKSKF 747
Cdd:cd14896 536 GDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSE---RQEA 612
|
650 660 670
....*....|....*....|....*....|..
gi 119600132 748 VSSRKAAEELLGSLEIDHTQ-YRFGITKVFFK 778
Cdd:cd14896 613 LSDRERCGAILSQVLGAESPlYHLGATKVLLK 644
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
118-778 |
7.48e-122 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 402.02 E-value: 7.48e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQ----KEVMAAYKGKrrseaPPHIFAVANNAFQDM---LH---- 185
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYDlhkyREEMPGWTAL-----PPHVFSIAEGAYRSLrrrLHepga 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 186 NRENQSILFTGESGAGKTVNSKHIIQYFATIA----AMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFI 261
Cdd:cd14895 77 SKKNQTILVSGESGAGKTETTKFIMNYLAESSkhttATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 262 RMHFGARGMLSSV-----DIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKE--LHDLLLVSANPSDFHFCSCGAVTV-- 332
Cdd:cd14895 157 RMFFEGHELDTSLrmigtSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADdmKLELQLELLSAQEFQYISGGQCYQrn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 333 ESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENA------------------D 394
Cdd:cd14895 237 DGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqhlD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 395 KAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDaklSRQF------- 467
Cdd:cd14895 317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASP---QRQFalnpnka 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 468 -------FIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGLDlQACIDLIE-KP 539
Cdd:cd14895 394 ankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEqRP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 540 MGILSILEEECMFPKATDLTFKTKLFDNHFGKSvHLQKPKPDKKKFEahFELVHYAGVVPYNISGWLEKNKDLLNETVVA 619
Cdd:cd14895 473 SGIFSLLDEECVVPKGSDAGFARKLYQRLQEHS-NFSASRTDQADVA--FQIHHYAGAVRYQAEGFCEKNKDQPNAELFS 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 620 VFQKSSNRLLASLFENY-MSTDSAIPFGE---KKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGI 695
Cdd:cd14895 550 VLGKTSDAHLRELFEFFkASESAELSLGQpklRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQ 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 696 LDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYcilnpRTFPKSKFVSSRKAAeELLGSLEIDHTQyrFGITKV 775
Cdd:cd14895 630 FDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQY-----RLLVAAKNASDATAS-ALIETLKVDHAE--LGKTRV 701
|
...
gi 119600132 776 FFK 778
Cdd:cd14895 702 FLR 704
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
859-1935 |
4.60e-116 |
|
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: 396.47 E-value: 4.60e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 859 EEVAGLKEEcaQLQKALE---KSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELS 935
Cdd:pfam01576 4 EEEMQAKEE--ELQKVKErqqKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 936 ERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAH 1015
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1016 QQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKK 1095
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1096 ELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEI 1175
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1176 TKKQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKA 1255
Cdd:pfam01576 322 RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1256 NAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKET 1335
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEET 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1336 KSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYEnNVIQRTEDLEDAKKELAIRLQEAAEA 1415
Cdd:pfam01576 482 RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE-EDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1416 MGVANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQ-----KHEESQALLDASQKEVQALS 1490
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAisaryAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1491 tellkLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKI 1570
Cdd:pfam01576 641 -----LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAK 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1571 LHFQLELLEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSE 1650
Cdd:pfam01576 716 LRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREE 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1651 ATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYT 1730
Cdd:pfam01576 796 AVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGAS 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1731 QNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLA 1810
Cdd:pfam01576 876 GKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQ 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1811 EAEQMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNY 1890
Cdd:pfam01576 956 EMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQL 1035
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*
gi 119600132 1891 KQQVEVAETQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIK 1935
Cdd:pfam01576 1036 KRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
117-778 |
1.00e-114 |
|
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: 379.72 E-value: 1.00e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKG-KRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 195
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 196 GESGAGKTVNSKHIIQYFATIAAMIESRKKQGAledqIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 275
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAKSGNMDLRIQTA----IMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 276 IDIYLLEKSRVIFQQAGERNYHIFYQILSG----QKELHDLLLVSanpsDFHFCSCGAVTVESLDDAEELLATEQAMDIL 351
Cdd:cd14876 157 VVAFLLEKSRIVTQDDNERSYHIFYQLLKGadseMKSKYHLLGLK----EYKFLNPKCLDVPGIDDVADFEEVLESLKSM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 352 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAF-----LMGINSSELVKCLIHPRIKVGNEYVTRG 426
Cdd:cd14876 233 GLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISNESLEVFkeacsLLFLDPEALKRELTVKVTKAGGQEIEGR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 427 QTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMF 506
Cdd:cd14876 313 WTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 507 VLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTF----KTKLFDNhfgksvhlQKPKPDK 582
Cdd:cd14876 393 ERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFvsacVSKLKSN--------GKFKPAK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 583 KKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENymstdsaIPFGEKKRKKGasfQTVASL 662
Cdd:cd14876 465 VDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG-------VVVEKGKIAKG---SLIGSQ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 663 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPrTF 742
Cdd:cd14876 535 FLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDL-GI 613
|
650 660 670
....*....|....*....|....*....|....*.
gi 119600132 743 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14876 614 ANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
117-776 |
2.29e-111 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 370.33 E-value: 2.29e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEA-PPHIFAVANNAFQDMLHNRE--NQSI 192
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 193 LFTGESGAGKTVNSKHIIQYFATIAA---MIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARG 269
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAsptSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 270 MLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESlDDAEellATEQAMD 349
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNLEE-DCFE---VTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 350 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQ---LEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRG 426
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQpcqPMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQVFK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 427 QTIEQVTCAV--GALSKSMYERMFKWLVARINRALDAKLSR-QFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNW 503
Cdd:cd14880 317 KPCSRAECDTrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 504 HMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGILSILEEECMFPKATDLT-FKTKLfdnhfgKSVHLQKPKPD 581
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSAAqLQTRI------ESALAGNPCLG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 582 KKKF--EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF--------ENYMSTDSAIPfgekkrk 651
Cdd:cd14880 470 HNKLsrEPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFpanpeektQEEPSGQSRAP------- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 652 kgasFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFK 731
Cdd:cd14880 543 ----VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFV 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 119600132 732 QRYCILNPRTFPKSKFVSSRKAAEELLGSLEIdhtqyrfGITKVF 776
Cdd:cd14880 619 ERYKLLRRLRPHTSSGPHSPYPAKGLSEPVHC-------GRTKVF 656
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
117-734 |
1.23e-109 |
|
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: 367.50 E-value: 1.23e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYK-------GKRRSEA---PPHIFAVANNAFQDMLH 185
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 186 NRENQSILFTGESGAGKTVNSKHIIQYFA------------TIAAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDN 253
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnnnltnSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 254 SSRFGKFIRMHF-GARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG-----QKELHDLLLVSANPSDFHFC-- 325
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLnq 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 326 SCGAVTVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKP--REEQLEADGTENA---------- 393
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPhkGDDTVFADEARVMssttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 394 DKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQF------ 467
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 468 ---------FIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGLDlQACIDLIE- 537
Cdd:cd14899 401 vddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEh 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 538 KPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETV 617
Cdd:cd14899 480 RPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 618 VAVFQKSSNRLLASL-----FENYMSTDSAIPFGEKKRKKGASFQ---TVASLHKENLNKLMTNLKSTAPHFVRCINPNV 689
Cdd:cd14899 560 AQLLAGSSNPLIQALaagsnDEDANGDSELDGFGGRTRRRAKSAIaavSVGTQFKIQLNELLSTVRATTPRYVRCIKPND 639
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 119600132 690 NKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRY 734
Cdd:cd14899 640 SHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
117-778 |
3.30e-109 |
|
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: 365.09 E-value: 3.30e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAAMIESRKKQgaleDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 276
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSV----EKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 277 DIYLLEKSRVIFQQAGERNYHIFYQILSG-----QKELH-DLLLVS--------ANPSDFHfcscgavtveslDDAEELL 342
Cdd:cd01386 157 QTLLLERSRVARRPEGESNFNVFYYLLAGadaalRTELHlNQLAESnsfgivplQKPEDKQ------------KAAAAFS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 343 ATEQAMDILGFLPDEKYGCYKLTGAIMHFGN---MKFKQKPREEQLEadgTENADKAAFLMGINSSELVKCLIHPRIKVG 419
Cdd:cd01386 225 KLQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFAR---PEWAQRAAYLLGCTLEELSSAIFKHHLSGG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 420 NEYVTRGQTIEQVTC------------AVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYN---- 483
Cdd:cd01386 302 PQQSTTSSGQESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqr 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 484 --SLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEwVSIGFGLD-LQACIDLIEK---------------PMGILSI 545
Cdd:cd01386 382 gaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVE-VDFDLPELsPGALVALIDQapqqalvrsdlrdedRRGLLWL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 546 LEEECMFPKATDLTFKTKLFdNHFGKSVHLQKPKPDKKKFEA-HFELVHYAGV--VPYNISGWLEKNK-DLLNETVVAVF 621
Cdd:cd01386 461 LDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLL 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 622 QkSSNRLLASLfenymstdsaipfgekkRKKGASFQTvaslhKENLNKLMTNLKSTAPHFVRCINPNVNKIPG------- 694
Cdd:cd01386 540 Q-ESQKETAAV-----------------KRKSPCLQI-----KFQVDALIDTLRRTGLHFVHCLLPQHNAGKDerstssp 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 695 -----ILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNP----RTFPKSKFVSSRKAAEELLGSLEIDH 765
Cdd:cd01386 597 aagdeLLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkKLGLNSEVADERKAVEELLEELDLEK 676
|
730
....*....|...
gi 119600132 766 TQYRFGITKVFFK 778
Cdd:cd01386 677 SSYRIGLSQVFFR 689
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
117-738 |
2.71e-107 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 360.45 E-value: 2.71e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRR-SEAPPHIFAVANNAFQDMLHNRENQSILF 194
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 195 TGESGAGKTVNSKHIIQYF-----ATIAAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHF-GAR 268
Cdd:cd14906 81 SGESGSGKTEASKTILQYLintssSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 269 GMLSSVDIDIYLLEKSRVIFQ-QAGERNYHIFYQILSG-QKELHDLLLVSANPSDFHFCSCGAVTVESL----------- 335
Cdd:cd14906 161 GKIDGASIETYLLEKSRISHRpDNINLSYHIFYYLVYGaSKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsnh 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 336 ----DDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKP---REEQLEADGTENADKAAFLMGINSSELV 408
Cdd:cd14906 241 nnktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 409 KCLIHPRIKVGNE--YVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRA---------LDAKLSRQ--FFIGILDIT 475
Cdd:cd14906 321 QALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKfnqntqsndLAGGSNKKnnLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 476 GFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGILSILEEECMFPK 554
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 555 ATDLTFKTKlfdnhFGKSVHlQKPKPDKKKF-EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF 633
Cdd:cd14906 480 GSEQSLLEK-----YNKQYH-NTNQYYQRTLaKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 634 enymSTDSAIPFGEKKRKKGASfqTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEG 713
Cdd:cd14906 554 ----QQQITSTTNTTKKQTQSN--TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNT 627
|
650 660
....*....|....*....|....*.
gi 119600132 714 TRICREGFPNRLQYADFKQRY-CILN 738
Cdd:cd14906 628 IKVRKMGYSYRRDFNQFFSRYkCIVD 653
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
117-778 |
5.26e-103 |
|
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: 346.41 E-value: 5.26e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMI-YTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEA-PPHIFAVANNAF-QDMLHNRENQSIL 193
Cdd:cd14875 1 ATLLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 194 FTGESGAGKTVNSKHIIQYFATIAAMIESRKKQGALEDQIMQ----ANTILEAFGNAKTLRNDNSSRFGKFIRMHF-GAR 268
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFdPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 269 GMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG-----QKELHDLllvsANPSDFHFCSCG------AVTVESLDD 337
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGlspeeKKELGGL----KTAQDYKCLNGGntfvrrGVDGKTLDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 338 AEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENAdKAAFLMGINSSELVKCLIhprIK 417
Cdd:cd14875 237 AHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL---VK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 418 VGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKL--SRQFFIGILDITGFEILEYNSLEQLCINFTNE 495
Cdd:cd14875 313 SKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQLCINYANE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 496 KLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVH 574
Cdd:cd14875 393 SLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 575 LQKPK---PDKkkfeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFenymSTDSaipfGEKKRK 651
Cdd:cd14875 472 FVLPKstiPNQ------FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL----STEK----GLARRK 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 652 kgasfQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFK 731
Cdd:cd14875 538 -----QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFC 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 119600132 732 QRYCILNPRTfPKSKFVSSR--KAAEELLGS----LEIDHTQYRFGITKVFFK 778
Cdd:cd14875 613 RYFYLIMPRS-TASLFKQEKysEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
117-778 |
8.29e-99 |
|
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: 333.78 E-value: 8.29e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRS-----EAPPHIFAVANNAFQDMLHNRENQ 190
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 191 SILFTGESGAGKTVNSKHIIQYFATIAAMiESRKKQGAledqIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 270
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHST-SSTDVQSL----ILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 271 LSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG----QKELHDLLLVSAnpsdFHFCSCG-AVTVESLDDAEELLATE 345
Cdd:cd14886 156 LKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGlspeEKKSLGFKSLES----YNFLNASkCYDAPGIDDQKEFAPVR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 346 QAMDILgFLPDEKYGCYKLTGAIMHFGNMKFKQKPR---EEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEY 422
Cdd:cd14886 232 SQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNET 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 423 VTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFN 502
Cdd:cd14886 311 IISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 503 WHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIEKP-MGILSILEEECMFPKATDLTF----KTKLFDNHFGKSvhlqk 577
Cdd:cd14886 391 NQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFtsscKSKIKNNSFIPG----- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 578 pkpdkKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIpfgekkrkKGasfQ 657
Cdd:cd14886 465 -----KGSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNM--------KG---K 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 658 TVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCIL 737
Cdd:cd14886 529 FLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKIL 608
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 119600132 738 NPRTFPKSKFVSSRKAA-EELLGSLEIDHTQYRFGITKVFFK 778
Cdd:cd14886 609 ISHNSSSQNAGEDLVEAvKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
117-778 |
2.04e-98 |
|
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: 332.36 E-value: 2.04e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEvmaaYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFatiaamIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 276
Cdd:cd14937 77 ESGSGKTEASKLVIKYY------LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 277 DIYLLEKSRVIFQQAGERNYHIFYQILSG-QKELHDLLLVSANpSDFHFCSCGAVTVESLDDAEELLATEQAMDILGfLP 355
Cdd:cd14937 151 EIFLLENIRVVSQEEEERGYHIFYQIFNGmSQELKNKYKIRSE-NEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMN-MH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 356 DEKYGCYKLTGAIMHFGNMKFKQ-----KPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIE 430
Cdd:cd14937 229 DMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 431 QVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQ 510
Cdd:cd14937 309 ESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKET 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 511 EEYKKESIEWVSIGFGLDlQACIDLIEKPMGILSILEEECMFPKATDLTFkTKLFDNHFGKSVHLQKPKPDKKKfeaHFE 590
Cdd:cd14937 389 ELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYASTKKDINK---NFV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 591 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAipfgekKRKKGASFQtvaslHKENLNKL 670
Cdd:cd14937 464 IKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESL------GRKNLITFK-----YLKNLNNI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 671 MTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRIcREGFPNRLQYADFKQRYCILNPRTFPKSKFVSS 750
Cdd:cd14937 533 ISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDK 611
|
650 660
....*....|....*....|....*...
gi 119600132 751 RKAAEELLGSLEIDhtQYRFGITKVFFK 778
Cdd:cd14937 612 EKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
117-778 |
1.36e-95 |
|
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: 324.46 E-value: 1.36e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAY---KGKRRSEAPPHIFAVANNAFQDMLHNRENQSIL 193
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 194 FTGESGAGKTVNSKHIIQYFATiaamiESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGAR-GMLS 272
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTC-----RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERkKHLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 273 SVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGA----VTVESLDDAEELLATEQAM 348
Cdd:cd14878 156 GARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredvSTAERSLNREKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 349 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQT 428
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 429 IEQVTCAVGALSKSMYERMFKWLVARINRAL----DAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWH 504
Cdd:cd14878 316 IQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 505 MFVLEQEEYKKESIEWVSIGFGLDLQACIDLI-EKPMGILSILEEECMFPKATDLTFKTKL---FDNHFGKSVHLQKP-- 578
Cdd:cd14878 396 LFLQEQTECVQEGVTMETAYSPGNQTGVLDFFfQKPSGFLSLLDEESQMIWSVEPNLPKKLqslLESSNTNAVYSPMKdg 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 579 --KPDKKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTdsaipfgekkrkkgasf 656
Cdd:cd14878 476 ngNVALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLVT----------------- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 657 qtVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCI 736
Cdd:cd14878 539 --IASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKP 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 119600132 737 LnPRTFPKSKfvssRKAAEELLGSLEIDHTQ---YRFGITKVFFK 778
Cdd:cd14878 617 L-ADTLLGEK----KKQSAEERCRLVLQQCKlqgWQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
118-742 |
2.22e-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: 2.22e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKwlPVYQKEVMAAYKgKRRSEAPPHIFAVANNAFQDMLHNrENQSILFTGE 197
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 198 SGAGKTVNSKHIIQYfatiaaMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFgaRGMLSSVDID 277
Cdd:cd14898 78 SGSGKTENAKLVIKY------LVERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKITGAKFE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 278 IYLLEKSRVIFQQAGERNYHIFYQILSGQkelhDLLLvsanPSDFHFCSCGAVTVESLDD-AEELLATEQAMDILGFLPD 356
Cdd:cd14898 150 TYLLEKSRVTHHEKGERNFHIFYQFCASK----RLNI----KNDFIDTSSTAGNKESIVQlSEKYKMTCSAMKSLGIANF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 357 EKYGCYKLtgAIMHFGNMKFKQkprEEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAV 436
Cdd:cd14898 222 KSIEDCLL--GILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 437 GALSKSMYERMFKWLVARINRALDAKLSRQffIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKE 516
Cdd:cd14898 297 NSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 517 SIEWVSIGFgLDLQACIDLIEKPMGILSILEEECMFPKAT--DLTFKTKLFDNHFGKSvhlqkpkpdkkKFEAHFELVHY 594
Cdd:cd14898 375 GIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNGFINT-----------KARDKIKVSHY 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 595 AGVVPYNISGWLEKNKDllnetvvavfqkssnrllaslfenymsTDSAIPFGEKKRKKGASFQTVASLHKENLNKLMTNL 674
Cdd:cd14898 443 AGDVEYDLRDFLDKNRE---------------------------KGQLLIFKNLLINDEGSKEDLVKYFKDSMNKLLNSI 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119600132 675 KSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTF 742
Cdd:cd14898 496 NETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLF 563
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
132-778 |
9.33e-85 |
|
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: 295.02 E-value: 9.33e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 132 IYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGESGAGKTVNSKHIIQ 211
Cdd:cd14887 24 IYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQSILISGESGAGKTETSKHVLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 212 YFATIAAMIESRKKQGaLEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDIDIYLLEKSRVIFQQA 291
Cdd:cd14887 104 YLAAVSDRRHGADSQG-LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 292 GERNYHIFYQILSGQK--ELHDLLLVSANPsdfhfcscgavtvESLDdaeeLLATEQAMDILGFLPDEKYGCYKLTGAIM 369
Cdd:cd14887 183 DEFSFHIFYALCNAAVaaATQKSSAGEGDP-------------ESTD----LRRITAAMKTVGIGGGEQADIFKLLAAIL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 370 HFGNMKF--KQKPRE-------------EQLEADGTENADKAAFLMGINSSE--------LVKCLIHPRIKVGNEYV--- 423
Cdd:cd14887 246 HLGNVEFttDQEPETskkrkltsvsvgcEETAADRSHSSEVKCLSSGLKVTEasrkhlktVARLLGLPPGVEGEEMLrla 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 424 --------TRGQ-TIEQVTCAVGALSKSMYERMFKWLVARINRAL-------------DAKLSRQF-FIGILDITGFEIL 480
Cdd:cd14887 326 lvsrsvreTRSFfDLDGAAAARDAACKNLYSRAFDAVVARINAGLqrsakpsesdsdeDTPSTTGTqTIGILDLFGFEDL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 481 E---YNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKES--IEWVSIGFGLDLQACIDLIEKP---------------- 539
Cdd:cd14887 406 RnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCSAFPFSFPLASTLTSSPsstspfsptpsfrsss 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 540 --------MGILSILEEE-CMFPKATDLTFKTKLFDNHFGK----SVHLQKPKPDKKKFEAHFELVHYAGVVPYNISGWL 606
Cdd:cd14887 486 afatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKNITPALSRENLEFTVSHFACDVTYDARDFC 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 607 EKNKDLLNETVVAVFQKSSNRLLaslfENYMSTDSAIPFGEKKRKkgasfqTVASLHKENLNKLMTNLKSTAPHFVRCIN 686
Cdd:cd14887 566 RANREATSDELERLFLACSTYTR----LVGSKKNSGVRAISSRRS------TLSAQFASQLQQVLKALQETSCHFIRCVK 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 687 PNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFpkSKFVSSRKAAEELLGSLEIDHT 766
Cdd:cd14887 636 PNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMAL--REALTPKMFCKIVLMFLEINSN 713
|
730
....*....|..
gi 119600132 767 QYRFGITKVFFK 778
Cdd:cd14887 714 SYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
114-777 |
5.73e-83 |
|
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: 287.52 E-value: 5.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 114 LNEASVLHTLKRRYGQWMIYTY---SGLfcVTINPYKWLPVYQKEVMAAYK-------GKRRSEAPPHIFAVANNAFQDM 183
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 184 LHNRENQSILFTGESGAGKTVNSKHIIQYFATIAAmieSRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRM 263
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSS---HSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 264 HFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG-QKELHDLLLVSaNPSDF-----HFCSCGAVTVESlDD 337
Cdd:cd14879 156 QFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGaSPEERQHLGLD-DPSDYallasYGCHPLPLGPGS-DD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 338 AEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFkqkpreeQLEADGTENA---------DKAAFLMGINSSELV 408
Cdd:cd14879 234 AEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEF-------TYDHEGGEESavvkntdvlDIVAAFLGVSPEDLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 409 KCLIHpRIKvgneYVTRgqtiEQVTC---AVGA------LSKSMYERMFKWLVARINRALdAKLSRQF--FIGILDITGF 477
Cdd:cd14879 307 TSLTY-KTK----LVRK----ELCTVfldPEGAaaqrdeLARTLYSLLFAWVVETINQKL-CAPEDDFatFISLLDFPGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 478 EIL---EYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKE--SIEWVSIgfgLDLQACIDLI-EKPMGILSILEEEC- 550
Cdd:cd14879 377 QNRsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEgvSVPATSY---FDNSDCVRLLrGKPGGLLGILDDQTr 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 551 MFPKATDLTFKTKL---FDNHfgKSVHLQKPKPDKKKFeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVavfqkssnr 627
Cdd:cd14879 454 RMPKKTDEQMLEALrkrFGNH--SSFIAVGNFATRSGS-ASFTVNHYAGEVTYSVEGFLERNGDVLSPDFV--------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 628 llaSLFenymstdsaipfgekkrkKGASFqtvaslHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRC 707
Cdd:cd14879 522 ---NLL------------------RGATQ------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRS 574
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 708 NGVLEGTRICREGFPNRLQYADFKQRYcilnPRTFPKSKFVSSRKAAEELLGSLEIDhtqYRFGITKVFF 777
Cdd:cd14879 575 LGLPELAARLRVEYVVSLEHAEFCERY----KSTLRGSAAERIRQCARANGWWEGRD---YVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
117-725 |
7.32e-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: 264.85 E-value: 7.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEA-------PPHIFAVANNAFQDMLHNRE 188
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 189 NQSILFTGESGAGKTVNSKHIIQYFatiaAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGAR 268
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYF----HYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 269 ---------GMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLVS-------ANPSDFHFCSCGAV 330
Cdd:cd14884 157 entqknmfnGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlsDEDLARRNLVRncgvyglLNPDESHQKRSVKG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 331 TVESLDDAEELLATEQAMDILGF------LPDEKYGCYKLT------GAIMHFGNMKFKQkpreeqleadgtenadkAAF 398
Cdd:cd14884 237 TLRLGSDSLDPSEEEKAKDEKNFvallhgLHYIKYDERQINeffdiiAGILHLGNRAYKA-----------------AAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 399 LMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRAL------------DAKLSRQ 466
Cdd:cd14884 300 CLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdneDIYSINE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 467 FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIgfglDLQACIDLIEKPMGILSIL 546
Cdd:cd14884 380 AIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSD----VAPSYSDTLIFIAKIFRRL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 547 EEECMFP----KATDLTFKTKLFDNH----------FGK-SVHLQKPKPDKKKFEAH-FELVHYAGVVPYNISGWLEKNK 610
Cdd:cd14884 456 DDITKLKnqgqKKTDDHFFRYLLNNErqqqlegkvsYGFvLNHDADGTAKKQNIKKNiFFIRHYAGLVTYRINNWIDKNS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 611 DLLNETVVAVFQKSSNRLLASLFENymstdsaipfgekkrKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVN 690
Cdd:cd14884 536 DKIETSIETLISCSSNRFLREANNG---------------GNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAK 600
|
650 660 670
....*....|....*....|....*....|....*
gi 119600132 691 KIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRL 725
Cdd:cd14884 601 MLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKI 635
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
118-744 |
3.48e-73 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 258.12 E-value: 3.48e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKwlpvyqkEVMAA--YKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 195
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYR-------DVGNPltLTSTRSSPLAPQLLKVVQEAVRQQSETGYPQAIILS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 196 GESGAGKTVNSKHIIQYFATIAAmiesrkkqGALEDQIMQ----ANTILEAFGNAKTLRNDNSSRFGKFIRMHFgARGML 271
Cdd:cd14881 75 GTSGSGKTYASMLLLRQLFDVAG--------GGPETDAFKhlaaAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDGAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 272 SSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 349
Cdd:cd14881 146 YRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGlsQEERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKACLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 350 ILG--FLpdekyGCYKLTGAIMHFGNMKFKQKPREEQLEADGTEnADKAAFLMGINSSELVKCLIhprIKVGNeyvTRGQ 427
Cdd:cd14881 226 ILGipFL-----DVVRVLAAVLLLGNVQFIDGGGLEVDVKGETE-LKSVAALLGVSGAALFRGLT---TRTHN---ARGQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 428 TIEQVtCAVG-------ALSKSMYERMFKWLVARIN--RALDAKLSRQF---FIGILDITGFEILEYNSLEQLCINFTNE 495
Cdd:cd14881 294 LVKSV-CDANmsnmtrdALAKALYCRTVATIVRRANslKRLGSTLGTHAtdgFIGILDMFGFEDPKPSQLEHLCINLCAE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 496 KLQQFFNWHMFVLEQEEYKKESIEW-VSIGFgLDLQACIDLIEK-PMGILSILEEECMfPKATDLTFKTKLFDNHFGKSV 573
Cdd:cd14881 373 TMQHFYNTHIFKSSIESCRDEGIQCeVEVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPR 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 574 HLQKPKPDKKKfeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSnrllaslfenymstdsaIPFGekkrkkg 653
Cdd:cd14881 451 LFEAKPQDDRM----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN-----------------CNFG------- 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 654 asFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQR 733
Cdd:cd14881 503 --FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNAR 580
|
650
....*....|.
gi 119600132 734 YCILNPRTFPK 744
Cdd:cd14881 581 YRLLAPFRLLR 591
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
118-737 |
4.99e-70 |
|
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: 249.27 E-value: 4.99e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 197
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 198 SGAGKTVNSKHIIQYFATIAAMiesrkKQGALEdQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDID 277
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDG-----NRGATG-RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 278 IYLLEKSRVIFQQAGERNYHIFYQI---LSGQKELHDLLL------------VSANPSDFHFC-SCGAVTVESLDDAEEL 341
Cdd:cd14882 156 MYQLEKLRVSTTDGNQSNFHIFYYFydfIEAQNRLKEYNLkagrnyrylripPEVPPSKLKYRrDDPEGNVERYKEFEEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 342 LateQAMDilgFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEadGTENADKAAFLMGINSSELVKCLIHPRIKVGNE 421
Cdd:cd14882 236 L---KDLD---FNEEQLETVRKVLAAILNLGEIRFRQNGGYAELE--NTEIASRVAELLRLDEKKFMWALTNYCLIKGGS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 422 YVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINraldAKLS--RQFF-----IGILDITGFEILEYNSLEQLCINFTN 494
Cdd:cd14882 308 AERRKHTTEEARDARDVLASTLYSRLVDWIINRIN----MKMSfpRAVFgdkysISIHDMFGFECFHRNRLEQLMVNTLN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 495 EKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECmfpkatdltfKTKLFDNHFGKSVH 574
Cdd:cd14882 384 EQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDAS----------RSCQDQNYIMDRIK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 575 lQKPKPDKKKFEAH-FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMStdsaipfgEKKRKKG 653
Cdd:cd14882 454 -EKHSQFVKKHSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQV--------RNMRTLA 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 654 ASFQTvASLhkENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQR 733
Cdd:cd14882 525 ATFRA-TSL--ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRR 601
|
....
gi 119600132 734 YCIL 737
Cdd:cd14882 602 YQFL 605
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
118-742 |
3.20e-68 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 244.62 E-value: 3.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSeAPPHIFAVANNAFQDMLHNRENQSILFTGE 197
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPFLHSQELVRNYNQRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 198 SGAGKTVNSKHIIQYFATIAAmieSRKKQgaLEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDID 277
Cdd:cd14905 81 SGSGKSENTKIIIQYLLTTDL---SRSKY--LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 278 IYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCS-CGAVTVESLDDAEELLATEQAMDILGFlPD 356
Cdd:cd14905 156 SYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNqGGSISVESIDDNRVFDRLKMSFVFFDF-PS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 357 EKYG-CYKLTGAIMHFGNMKFKQKprEEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTieqvtca 435
Cdd:cd14905 235 EKIDlIFKTLSFIIILGNVTFFQK--NGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENRDS------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 436 vgaLSKSMYERMFKWLVARINRALDAKlSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKK 515
Cdd:cd14905 306 ---LARSLYSALFHWIIDFLNSKLKPT-QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 516 ESIEWVS-IGFGlDLQACIDLIEKpmgILSILEEECMFPKATDLTFKTKLfdNHFGKSVHLQKPKPDKkkfeahFELVHY 594
Cdd:cd14905 382 ERIPWMTpISFK-DNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--QNFLSRHHLFGKKPNK------FGIEHY 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 595 AGVVPYNISGWLEKNKDL-------------------------LNETVVAVFQ-----KSSNRLLASLFENYMSTDSAIP 644
Cdd:cd14905 450 FGQFYYDVRGFIIKNRDEilqrtnvlhknsitkylfsrdgvfnINATVAELNQmfdakNTAKKSPLSIVKVLLSCGSNNP 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 645 ------------------FGEKKRKKGASFQTVASLHKEnlnklmTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLR 706
Cdd:cd14905 530 nnvnnpnnnsgggggggnSGGGSGSGGSTYTTYSSTNKA------INNSNCDFHFIRCIKPNSKKTHLTFDVKSVNEQIK 603
|
650 660 670
....*....|....*....|....*....|....*...
gi 119600132 707 CNGVLEGTRICREGFPNRLQYADFKQRYCIL--NPRTF 742
Cdd:cd14905 604 SLCLLETTRIQRFGYTIHYNNKIFFDRFSFFfqNQRNF 641
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
117-737 |
1.28e-67 |
|
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: 241.70 E-value: 1.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 117 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYkgkrrseappHIFAVANNAFQDMLHNREN-QSILFT 195
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 196 GESGAGKTVNSKHIIQYFATIAAMIESRKKQGALEdqimqanTILEAFGNAKTLRNDNSSRFGKFIRMHFgARGMLSSVD 275
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAIE-------SVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 276 IDIYL-LEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFL 354
Cdd:cd14874 143 LKYTVpLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 355 PDEKYGCYKLTGAIMHFGNMKFKQKPR---EEQLEADGTENADK-AAFLMGINSSELVKCLIhPRIKVGNEYvtrgqTIE 430
Cdd:cd14874 223 DDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKwVAFLLEVDFDQLVNFLL-PKSEDGTTI-----DLN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 431 QVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFfIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQ 510
Cdd:cd14874 297 AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV-ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 511 EEYKKESIEwvsigfgLDLQ--ACID-------LIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPD 581
Cdd:cd14874 376 VDYAKDGIS-------VDYKvpNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 582 KKKFEAHfelvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMS-TDSAIPFGEKKRKKGAsfQTVA 660
Cdd:cd14874 449 RLEFGVR----HCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSnTSDMIVSQAQFILRGA--QEIA 522
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119600132 661 slhkENLNKLMTnlkstapHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRY-CIL 737
Cdd:cd14874 523 ----DKINGSHA-------HFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYrCLL 589
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
120-777 |
7.06e-67 |
|
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: 242.57 E-value: 7.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 120 LHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRR----------SEAPPHIFAVANNAFQDMLHNREN 189
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 190 QSILFTGESGAGKTVNSKHIIQYFATIAAMIESRK----KQGALE---DQIMQANTILEAFGNAKTLRNDNSSRFGKFIR 262
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPdsegASGVLHpigQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 263 MHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKE---LHDLLLVSANPSDFHFCSCGA--VTVESLD- 336
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdptLRDSLEMNKCVNEFVMLKQADplATNFALDa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 337 -DAEELLATEQAMDIlgfLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENA----------DKAAFLMGINSS 405
Cdd:cd14893 244 rDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTvsdaqscalkDPAQILLAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 406 ELVKCLIHPRIKV-------GNEYVTRGQ--TIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSR---------QF 467
Cdd:cd14893 321 EVEPVVLDNYFRTrqffskdGNKTVSSLKvvTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksnivinSQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 468 FIGILDITGFEILE--YNSLEQLCINFTNEKLQQFF-------NWHMFVLEQEEYKKESIEWVSIGFGLDLQACIDLIE- 537
Cdd:cd14893 401 GVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvqntlaiNFSFLEDESQQVENRLTVNSNVDITSEQEKCLQLFEd 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 538 KPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVhLQKPKPD----------KKKFEAHFELVHYAGVVPYNISGWLE 607
Cdd:cd14893 481 KPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGG-LSRPNMGadttneylapSKDWRLLFIVQHHCGKVTYNGKGLSS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 608 KNKDLLNETVVAVFQKSSNRLLASLFENYM---STDSAIPFGEKKRKKGASFQTVASLHKENLN--------------KL 670
Cdd:cd14893 560 KNMLSISSTCAAIMQSSKNAVLHAVGAAQMaaaSSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadAL 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 671 MTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYcilnprtfpkSKFVSS 750
Cdd:cd14893 640 LHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY----------KNVCGH 709
|
730 740 750
....*....|....*....|....*....|.
gi 119600132 751 RKAAEELLGSLE----IDHTQYRFGITKVFF 777
Cdd:cd14893 710 RGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
139-263 |
1.70e-52 |
|
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: 182.16 E-value: 1.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 139 FCVTINPYKWLPVY-QKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGESGAGKTVNSKHIIQYFATIA 217
Cdd:cd01363 1 VLVRVNPFKELPIYrDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 119600132 218 A----------MIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRM 263
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 ... |
118-776 |
5.37e-46 |
|
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: 178.88 E-value: 5.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 118 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSE-APPHIFAVANNAFQDMLHNRENQSILFTG 196
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 197 ESGAGKTVNSKHIIQYFATIAA------------------MIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFG 258
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKgsrrlptnlndqeednihNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 259 KFIRMHFGARgMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESLDDA 338
Cdd:cd14938 162 KFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 339 EELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQL-----------------------EADGTENADK 395
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRKKSLlmgknqcgqninyetilselensEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 396 ----AAFLMGINSSELVKCLIHPRIkVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFF--- 468
Cdd:cd14938 321 nlllACKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININtny 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 469 IGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGLDLQACID-LIEKPMGILSILE 547
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNlLVGPTEGSLFSLL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 548 EECMFPKATDLTFKTKLFDNHFGKSVHLQKpKPDKKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNR 627
Cdd:cd14938 480 ENVSTKTIFDKSNLHSSIIRKFSRNSKYIK-KDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSENE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 628 LLASL--FENYMSTDS--------AIPFGEK--KRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNK-IPG 694
Cdd:cd14938 559 YMRQFcmFYNYDNSGNiveekrrySIQSALKlfKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKrELC 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 695 ILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPrtfpkskfvSSRKAAEELLGSLEIDHTQYRFGITK 774
Cdd:cd14938 639 SFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 119600132 775 VF 776
Cdd:cd14938 710 IF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
869-1759 |
4.24e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 130.56 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 869 AQLQKAlEKSEFQREELKAKQVSL-TQEKNDLILQLQAEQETLANVEEQCEwlikskiQLEARVKELSERVEEEEEINSE 947
Cdd:TIGR02168 207 RQAEKA-ERYKELKAELRELELALlVLRLEELREELEELQEELKEAEEELE-------ELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 948 LTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEE 1027
Cdd:TIGR02168 279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1028 KLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELsqmnskve 1107
Cdd:TIGR02168 359 ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL-------- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1108 nEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGgsslAQLEITKKQETKFQKLH 1187
Cdd:TIGR02168 431 -EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ----ARLDSLERLQENLEGFS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1188 RDMEEATLhfettsaslkkrHADSLAELEGQVENLQQVKQKLEKDKS-DLQLEVDDLLtrVEQMTRAKANAEKLctlyee 1266
Cdd:TIGR02168 506 EGVKALLK------------NQSGLSGILGVLSELISVDEGYEAAIEaALGGRLQAVV--VENLNAAKKAIAFL------ 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1267 rlheATAKLDKVTQLANDLAAQkTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLeketksqsALAHALQ 1346
Cdd:TIGR02168 566 ----KQNELGRVTFLPLDSIKG-TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV--------LVVDDLD 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1347 KAQRdcdLLREQYEEEQEVKAELHRTL---------SKVNAEMVQWRMKYENNViQRTEDLEDAKKELAIRLQEAAEAMG 1417
Cdd:TIGR02168 633 NALE---LAKKLRPGYRIVTLDGDLVRpggvitggsAKTNSSILERRREIEELE-EKIEELEEKIAELEKALAELRKELE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1418 VANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLK 1497
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1498 NTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLEL 1577
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1578 LEAKAELERKLSEKDEEIENfrrkqqctIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQ 1657
Cdd:TIGR02168 869 EELESELEALLNERASLEEA--------LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1658 LQIQIKDL-QMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEqtergrrLSEEELLEATERINLFYTQNTSLL 1736
Cdd:TIGR02168 941 LQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNL-------AAIEEYEELKERYDFLTAQKEDLT 1013
|
890 900
....*....|....*....|...
gi 119600132 1737 SQKKKLEADVARMQKEAEEVVQE 1759
Cdd:TIGR02168 1014 EAKETLEEAIEEIDREARERFKD 1036
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1093-1932 |
2.35e-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: 128.25 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1093 RKKELElSQMNSKVENekglVAQLQKTVKELQTQIKDLKEKLE-AERTTRAKMERERADLTQDLADLNERLEEVggssLA 1171
Cdd:TIGR02168 173 RRKETE-RKLERTREN----LDRLEDILNELERQLKSLERQAEkAERYKELKAELRELELALLVLRLEELREEL----EE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1172 QLEITKKQETKFQKLHRDMEEATLHFETTSASLKKRHaDSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMT 1251
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELE-EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1252 RAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQL 1331
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1332 EKETKSQSALAHALQKAQRDCDLLREQYEEEQevKAELHRTLSKVNAEMVQWRMKYEnNVIQRTEDLEDAKKELAIRLQE 1411
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELE-RLEEALEELREELEEAEQALDA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1412 AAEAMGVANARNASLERARHQLQlelgdalsdlGKVRSAAARLDQKQLQSGkaladwkqkheesqalldasqkeVQALST 1491
Cdd:TIGR02168 480 AERELAQLQARLDSLERLQENLE----------GFSEGVKALLKNQSGLSG-----------------------ILGVLS 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1492 ELLKLKNTYEESIvgqETLRREnkNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKIL 1571
Cdd:TIGR02168 527 ELISVDEGYEAAI---EAALGG--RLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFL 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1572 HFQLELLEAKAELERKLS----------EKDEEIENFRR-KQQCTIDSLQSSL-----------DSEAKSRIEVTRLKKK 1629
Cdd:TIGR02168 602 GVAKDLVKFDPKLRKALSyllggvlvvdDLDNALELAKKlRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRREIEE 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1630 MEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTER 1709
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1710 GRRLSEEELLEATERInlfytqnTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIA 1789
Cdd:TIGR02168 762 EIEELEERLEEAEEEL-------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1790 HLERTRENMEQTITDLQKRLAEAE------QMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELT 1863
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAaeieelEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1864 YQAEEDKKNLSRMQTQMDKLQLKVQNYKQQV-EVAETQANQYLSKYKKQQHELNEVKERAEVAESQVNKL 1932
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
233-718 |
4.12e-24 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 110.60 E-value: 4.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 233 IMQANTILEAFGNAKTLRNDNSSRFGKF--IRMHFGARG---MLSSVDIDIYLLEKSRVIFQQA------GERNYHIFYQ 301
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERGresgdqNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 302 ILSG----------QKELH-DLLLVSA----NPSDFHFCscGAVTVESL--DDAEELLATEQAMDILGFLPDEKYGCYKL 364
Cdd:cd14894 329 MVAGvnafpfmrllAKELHlDGIDCSAltylGRSDHKLA--GFVSKEDTwkKDVERWQQVIDGLDELNVSPDEQKTIFKV 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 365 TGAIMHFGNMKFKQKPREEQL--EADGTENA-DKAAFLMGINSSE-LVKCLIHPRIKVGNEYVTRGQTIE--QVTCAVGA 438
Cdd:cd14894 407 LSAVLWLGNIELDYREVSGKLvmSSTGALNApQKVVELLELGSVEkLERMLMTKSVSLQSTSETFEVTLEkgQVNHVRDT 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 439 LSKSMYERMFKWLVARINRA--------------LDAKLSRQ---FFIGILDITGFEILEYNSLEQLCINFTNEKLQqff 501
Cdd:cd14894 487 LARLLYQLAFNYVVFVMNEAtkmsalstdgnkhqMDSNASAPeavSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY--- 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 502 nwhmfvleQEEYKKESIEWVSIGFGLDLQACIDLI---EKPMGILSILEEECMFPKATDLTF-----KTKLFDNHFGKSV 573
Cdd:cd14894 564 --------AREEQVIAVAYSSRPHLTARDSEKDVLfiyEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIYDRN 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 574 HLQKPKPDKKKFEAH-----------FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYM----- 637
Cdd:cd14894 636 SSRLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSqlgws 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 638 -STDSAIPFGEKKRKKGAsfQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRI 716
Cdd:cd14894 716 pNTNRSMLGSAESRLSGT--KSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEI 793
|
..
gi 119600132 717 CR 718
Cdd:cd14894 794 CR 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
961-1815 |
1.74e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 99.37 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 961 ELKKEIDDLE-TMLVKS----EKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAkvvqEAHQQTLDDLHMEEEKLSSLSKA 1035
Cdd:TIGR02169 215 ALLKEKREYEgYELLKEkealERQKEAIERQLASLEEELEKLTEEISELEKRL----EEIEQLLEELNKKIKDLGEEEQL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1036 NLKleQQVDELEGALEQerkarmncerelhkLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQ 1115
Cdd:TIGR02169 291 RVK--EKIGELEAEIAS--------------LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1116 LQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDM---EE 1192
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIagiEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1193 ATLHFETTsaslKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLltrveqmtrakanaeklctlyEERLHEAT 1272
Cdd:TIGR02169 435 KINELEEE----KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV---------------------EKELSKLQ 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1273 AKLDKvtqlandLAAQKTKLWSESGEFLRRLEEKEA-------LINQLSREKSNFTRQIEdlrgqleketksqSALAHAL 1345
Cdd:TIGR02169 490 RELAE-------AEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGSVGERYATAIE-------------VAAGNRL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1346 QKAQRDCDLLRE---QYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAI-------------RL 1409
Cdd:TIGR02169 550 NNVVVEDDAVAKeaiELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPafkyvfgdtlvveDI 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1410 QEAAEAMGvaNARNASLE--------------RARHQLQlelGDALSDLGKVRSAAARLDQKQlqsgKALADWKQKHEES 1475
Cdd:TIGR02169 630 EAARRLMG--KYRMVTLEgelfeksgamtggsRAPRGGI---LFSRSEPAELQRLRERLEGLK----RELSSLQSELRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1476 QALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLtnqvregtknltemekvkkliEEEKTEVQVT 1555
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL---------------------EQEIENVKSE 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1556 LEETEGALERNESKILHFQLELleakAELERKLS-EKDEEIENFRRKQQCTIDSLQSSLDSeaksrievtrlkkkMEEDL 1634
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEAL----NDLEARLShSRIPEIQAELSKLEEEVSRIEARLRE--------------IEQKL 821
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1635 NEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRS----LQEQ---T 1707
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKerdeLEAQlreL 901
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1708 ERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEE------VVQECQNAEEKAKKAAIEAANLSEEL 1781
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEelsledVQAELQRVEEEIRALEPVNMLAIQEY 981
|
890 900 910
....*....|....*....|....*....|....
gi 119600132 1782 KKKQDTIAHLERTRENMEQTITDLQKRLAEAEQM 1815
Cdd:TIGR02169 982 EEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
859-1756 |
2.72e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 98.60 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 859 EEVAGLKEECAQLQKALEKSEFQREELKAKQvSLTQEKNDLILQLQAEQETLanveEQCEWLIKSKIQLEARVKELSERv 938
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLD-LIIDEKRQQLERLRREREKA----ERYQALLKEKREYEGYELLKEKE- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 939 eeeeeinsELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISklnraakvvqeahqqt 1018
Cdd:TIGR02169 234 --------ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---------------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1019 lddlhmeeeklsslskanLKLEQQVDELEGALEQerkarmncerelhkLEGNLKLNRESMENLESSQRHLAEELRKKELE 1098
Cdd:TIGR02169 290 ------------------LRVKEKIGELEAEIAS--------------LERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1099 LSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKK 1178
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1179 QETKFQKLHRDM---EEATLHFETTsaslKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLltrveqmtraka 1255
Cdd:TIGR02169 418 LSEELADLNAAIagiEAKINELEEE----KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV------------ 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1256 naeklctlyEERLHEATAKLDKvtqlandLAAQKTKLWSESGEFLRRLEEKEA-------LINQLSREKSNFTRQIEDLR 1328
Cdd:TIGR02169 482 ---------EKELSKLQRELAE-------AEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGSVGERYATAIEVAA 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1329 GQ------LEKETKSQSALAHALQ-KAQRDCDL-LREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENN---VIQRT-- 1395
Cdd:TIGR02169 546 GNrlnnvvVEDDAVAKEAIELLKRrKAGRATFLpLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAfkyVFGDTlv 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1396 -EDLEDAKK--------ELAIRLQEAAEAM-----------GVANARNASLERARHQLQlELGDALSDL-GKVRSAAARL 1454
Cdd:TIGR02169 626 vEDIEAARRlmgkyrmvTLEGELFEKSGAMtggsraprggiLFSRSEPAELQRLRERLE-GLKRELSSLqSELRRIENRL 704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1455 DQKQlqsgKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKN 1534
Cdd:TIGR02169 705 DELS----QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA 780
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1535 LTEMEkvKKLIEEEKTEVQVTLEETEGALERNESKILHFQLElLEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLD 1614
Cdd:TIGR02169 781 LNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK-LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1615 SEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQ 1694
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119600132 1695 ----------SELEDLRSLQEQTERgrrlsEEELLEATERINLFYTQN-TSLLSQKKKLEADVARMQKEAEEV 1756
Cdd:TIGR02169 938 dpkgedeeipEEELSLEDVQAELQR-----VEEEIRALEPVNMLAIQEyEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
856-1597 |
9.57e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 93.58 E-value: 9.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 856 EVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQekndlilQLQAEQETLANVEEQCEWLIKSKIQLEARVKELS 935
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEE-------QLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 936 ERVEEEEEINSELtaRGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAkvvqEAH 1015
Cdd:TIGR02168 414 DRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL----AQL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1016 QQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQeRKARMNCERELHK-LEGNLklnRESMENLESsqrhlaeelRK 1094
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV-LSELISVDEGYEAaIEAAL---GGRLQAVVV---------EN 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1095 KELELSQMNSKVENEKGLVAQLqktvkeLQTQIKDlkEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLE 1174
Cdd:TIGR02168 555 LNAAKKAIAFLKQNELGRVTFL------PLDSIKG--TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVL 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1175 ITKKQETKFQKLHRDMEEATL-----------------HFETTSASLKKR-----HADSLAELEGQVENLQQVKQKLEKD 1232
Cdd:TIGR02168 627 VVDDLDNALELAKKLRPGYRIvtldgdlvrpggvitggSAKTNSSILERRreieeLEEKIEELEEKIAELEKALAELRKE 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1233 KSDLQLEVDDLLTRVEQMTRA-------KANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEE 1305
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQisalrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1306 KEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMvqwrm 1385
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI----- 861
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1386 kyennviqrtEDLEDAKKELAIRLQEAAEAMgvanarnASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKAL 1465
Cdd:TIGR02168 862 ----------EELEELIEELESELEALLNER-------ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1466 ADWKQKHEESQALLDASQKEVQAL-STELLKLKNTYEESIVGQETLRRENKNLQEEISNLtnqvreGTKNLTEMEKvkkl 1544
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL------GPVNLAAIEE---- 994
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 119600132 1545 IEEEKTEVQVTLEETEgalerneskilhfqlELLEAKAELERKLSEKDEEIEN 1597
Cdd:TIGR02168 995 YEELKERYDFLTAQKE---------------DLTEAKETLEEAIEEIDREARE 1032
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
855-1601 |
4.62e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 91.28 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 855 SEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEK----NDLILQLQAEQE----TLANVEEQCEWLIKSKIQ 926
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvKEKIGELEAEIAslerSIAEKERELEDAEERLAK 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 927 LEARVKELSERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNR 1006
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1007 AAKVVQEAHQQTLDDLHMEEEKLSSLskanlklEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQR 1086
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGI-------EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1087 HLAEELRKKELELSQ---------------------MNSKVENEKGLVAQLQKTVKELQTQI------------------ 1127
Cdd:TIGR02169 480 RVEKELSKLQRELAEaeaqaraseervrggraveevLKASIQGVHGTVAQLGSVGERYATAIevaagnrlnnvvveddav 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1128 -KDLKEKLEAERTTRA------KMERERADLTQ-----------DLADLNERLEE----VGGSSLA--QLEITKKQETKF 1183
Cdd:TIGR02169 560 aKEAIELLKRRKAGRAtflplnKMRDERRDLSIlsedgvigfavDLVEFDPKYEPafkyVFGDTLVveDIEAARRLMGKY 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1184 QKLHRDMEEATLHFETTSASLKKRHADSLA-ELEGQVENLQQVKQKLEKDKSDLQLEVDDLltrveqmtrakanaeklct 1262
Cdd:TIGR02169 640 RMVTLEGELFEKSGAMTGGSRAPRGGILFSrSEPAELQRLRERLEGLKRELSSLQSELRRI------------------- 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1263 lyEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALA 1342
Cdd:TIGR02169 701 --ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1343 HALQKAQRdcDLLREQYEEEQevkaelhRTLSKVNAEMVQWRmkyennviQRTEDLEDAKKELAIRLQEAAEAMGVANAR 1422
Cdd:TIGR02169 779 EALNDLEA--RLSHSRIPEIQ-------AELSKLEEEVSRIE--------ARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1423 NASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEE 1502
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1503 SIVGQETLRRENKnlqeEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQvTLEETEGALERNESKILHFQLELLEAKA 1582
Cdd:TIGR02169 922 LKAKLEALEEELS----EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIR-ALEPVNMLAIQEYEEVLKRLDELKEKRA 996
|
810
....*....|....*....
gi 119600132 1583 ELERKLSEKDEEIENFRRK 1601
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKK 1015
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
853-1417 |
8.08e-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: 8.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 853 KSSEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVK 932
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 933 ELSERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQ 1012
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1013 EAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEEL 1092
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1093 RKKELELSQMNSKVENEKGLVAQLQktvkELQTQIKDLKEKLEAERTTRAkMERERADLTQDLADLNERLEEVGGSSLAQ 1172
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYE----GFLEGVKAALLLAGLRGLAGA-VAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1173 LEITKKQETKFQKLHRDmEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVeqmTR 1252
Cdd:COG1196 555 DDEVAAAAIEYLKAAKA-GRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV---AA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1253 AKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKlwsESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLE 1332
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE---LLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1333 KETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEmvqwrmkyennVIQRTEDLEDAKKELAiRLQEA 1412
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE-----------ELPEPPDLEELERELE-RLERE 775
|
....*
gi 119600132 1413 AEAMG 1417
Cdd:COG1196 776 IEALG 780
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1207-1832 |
1.03e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.00 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1207 RHADSLAELEGQVENLQ-QVKQ-------KLEKDKSDLQL---EVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKL 1275
Cdd:COG1196 190 RLEDILGELERQLEPLErQAEKaeryrelKEELKELEAELlllKLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1276 DKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLL 1355
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1356 REQYEEEQEVKAELHRTLSKVNAEMVQWrmkyennviqrtedlEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQL 1435
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEA---------------EEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1436 ELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEEsIVGQETLRRENK 1515
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE-LLEELAEAAARL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1516 NLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERKLSEKDEEI 1595
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGR 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1596 ENFrrkqqctidslqssldsEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEAtkslGQLQIQIKDLQMQLDDSTQL 1675
Cdd:COG1196 574 ATF-----------------LPLDKIRARAALAAALARGAIGAAVDLVASDLREAD----ARYYVLGDTLLGRTLVAARL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1676 NSDLKEQVAVAERRNSLLQsELEDLRSLQEQTERGRRLSEEELLEATERInlfytqntsllSQKKKLEADVARMQKEAEE 1755
Cdd:COG1196 633 EAALRRAVTLAGRLREVTL-EGEGGSAGGSLTGGSRRELLAALLEAEAEL-----------EELAERLAEEELELEEALL 700
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119600132 1756 VVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQIQKLESRVR 1832
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
856-1466 |
1.37e-17 |
|
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: 89.73 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 856 EVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEwlikskiQLEARVKELS 935
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-------SLEAELEELE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 936 ERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRaakvvqEAH 1015
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL------KEL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1016 QQTLDDLHMEEEKLSslsKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKK 1095
Cdd:TIGR02168 439 QAELEELEEELEELQ---EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1096 E-------LELSQMNSKVENEKGLVAQLQKT-----VKELQTQIKD---LKE-----------------KLEAERTTRAK 1143
Cdd:TIGR02168 516 SglsgilgVLSELISVDEGYEAAIEAALGGRlqavvVENLNAAKKAiafLKQnelgrvtflpldsikgtEIQGNDREILK 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1144 MERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDMEEATL-----------------HFETTSASLKK 1206
Cdd:TIGR02168 596 NIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIvtldgdlvrpggvitggSAKTNSSILER 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1207 R-----HADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLC-------------------- 1261
Cdd:TIGR02168 676 RreieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLarleaeveqleeriaqlske 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1262 --------TLYEERLHEATAKLD-----------KVTQLANDLAAQKTKLWSESGEFLR---RLEEKEALINQLSREKSN 1319
Cdd:TIGR02168 756 lteleaeiEELEERLEEAEEELAeaeaeieeleaQIEQLKEELKALREALDELRAELTLlneEAANLRERLESLERRIAA 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1320 FTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQwRMKYENNVIQRTEDLE 1399
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE-LSEELRELESKRSELR 914
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119600132 1400 DAKKELAIRLQEAAEAMGVANARNASL-ERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALA 1466
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1142-1918 |
2.21e-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: 88.97 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1142 AKMERERADLTQDLADLNERLEEVG------GSSLAQLEITKKQETKFQKLHRDMEEATLhfeTTSASLKKRHADSLAEL 1215
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDliidekRQQLERLRREREKAERYQALLKEKREYEG---YELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1216 EGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMtrakanAEKLCTLYEERLHEATAKLDKVTqlandlaAQKTKLWSE 1295
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL------NKKIKDLGEEEQLRVKEKIGELE-------AEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1296 SGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSK 1375
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1376 VNAEMVQwrMKYENNVIQRTED-LEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQLELgdalsdlgkvrsaaARL 1454
Cdd:TIGR02169 390 YREKLEK--LKREINELKRELDrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI--------------KKQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1455 DQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKn 1534
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1535 lTEMEKVKKLIEEEKTEVQVTLEETEG--------ALERNESKILHFQLELLEAKAELERKLSEK------------DEE 1594
Cdd:TIGR02169 533 -VGERYATAIEVAAGNRLNNVVVEDDAvakeaielLKRRKAGRATFLPLNKMRDERRDLSILSEDgvigfavdlvefDPK 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1595 IEN-FRRKQQCTI--DSLQS-----------SLDSE--------------AKSRIEVTRLKK----KMEEDLNEMELQLS 1642
Cdd:TIGR02169 612 YEPaFKYVFGDTLvvEDIEAarrlmgkyrmvTLEGElfeksgamtggsraPRGGILFSRSEPaelqRLRERLEGLKRELS 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1643 CANRQVSEATKSLGQLQIQIKDLQMQLddstqlnSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEAT 1722
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQELSDASRKI-------GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1723 ERINLFYTQNTSLLSQKKKLEADVArmQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTI 1802
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1803 TDLQKRLAEAEQmALMGSRKQIQKLESRVrelegelegeirrsAEAQRGARRLERCIKELtyqaeedKKNLSRMQTQMDK 1882
Cdd:TIGR02169 843 IDLKEQIKSIEK-EIENLNGKKEELEEEL--------------EELEAALRDLESRLGDL-------KKERDELEAQLRE 900
|
810 820 830
....*....|....*....|....*....|....*.
gi 119600132 1883 LQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEV 1918
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1306-1945 |
4.26e-17 |
|
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: 88.19 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1306 KEALiNQLSREKSNFTRqIEDLRGQLEKETKSQSALAHALQKAQRdcdlLREQYEEEQ---------EVKAELHRTLSKV 1376
Cdd:TIGR02168 175 KETE-RKLERTRENLDR-LEDILNELERQLKSLERQAEKAERYKE----LKAELRELElallvlrleELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1377 NaEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQL---ELGDALSDLGKVRSAAAR 1453
Cdd:TIGR02168 249 K-EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIlreRLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1454 LDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTK 1533
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1534 NLTEMEK------------VKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRK 1601
Cdd:TIGR02168 408 RLERLEDrrerlqqeieelLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1602 QQcTIDSLQS---------------------------------SLDSEAKSRIEV------------------------- 1623
Cdd:TIGR02168 488 QA-RLDSLERlqenlegfsegvkallknqsglsgilgvlseliSVDEGYEAAIEAalggrlqavvvenlnaakkaiaflk 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1624 -----------------TRLKKKMEEDLNEMELQLSCANRQVSEATKS-------LGQLQIqIKDLQMQLDDSTQLNSDL 1679
Cdd:TIGR02168 567 qnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsylLGGVLV-VDDLDNALELAKKLRPGY 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1680 K------EQV--------AVAERRNSLL--QSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLE 1743
Cdd:TIGR02168 646 RivtldgDLVrpggvitgGSAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1744 ADVARMQKEAEEVVQECQNAEEKAKKAAIEAANL-------SEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQmA 1816
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELeaeieelEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-A 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1817 LMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEV 1896
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 119600132 1897 AETQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQE 1945
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1212-1945 |
6.42e-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: 87.43 E-value: 6.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1212 LAELEGQVENLQQVKQKLEKDKsDLQLEVDD-----LLTRVEQMTRAKANAEKlctlyeeRLHEATAKLDKVTQLANDLA 1286
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQ-ALLKEKREyegyeLLKEKEALERQKEAIER-------QLASLEEELEKLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1287 AqktklwsESGEFLRRLEEKEALINQLSREKSN-FTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEV 1365
Cdd:TIGR02169 265 K-------RLEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1366 KAELHRTLSKVNAEMVQWrmkyennvIQRTEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSDLG 1445
Cdd:TIGR02169 338 IEELEREIEEERKRRDKL--------TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1446 KVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELlklkntyEESIVGQETLRRENKNLQEEISNLT 1525
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL-------EQLAADLSKYEQELYDLKEEYDRVE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1526 NQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEEtegaLERNESKILHFQLELLEAKAELERKLsekdeEIENFRRKQQCT 1605
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASEERVRGGRAVEEV----LKASIQGVHGTVAQLGSVGERYATAI-----EVAAGNRLNNVV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1606 IDSlqsslDSEAKSRIEVTRLKK----------KMEE------------------DLNEMELQLSCANRQVSEATKSLGQ 1657
Cdd:TIGR02169 554 VED-----DAVAKEAIELLKRRKagratflplnKMRDerrdlsilsedgvigfavDLVEFDPKYEPAFKYVFGDTLVVED 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1658 LQIQiKDLQMQLDDSTqLNSDLKEQV------AVAERRNSLLQ-SELEDLRSLQEQTERGRRLSEEELLEATERINLFYt 1730
Cdd:TIGR02169 629 IEAA-RRLMGKYRMVT-LEGELFEKSgamtggSRAPRGGILFSrSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD- 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1731 qntSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLA 1810
Cdd:TIGR02169 706 ---ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1811 EAEQMALMGSRKQIQKLESRVRelegelegEIRRSAEAQrgARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNY 1890
Cdd:TIGR02169 783 DLEARLSHSRIPEIQAELSKLE--------EEVSRIEAR--LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 119600132 1891 KQQVEVAETQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQE 1945
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1135-1759 |
8.04e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.30 E-value: 8.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1135 EAERttraKMERERADLTQdladLNERLEEVGgSSLAQLEITKKQETKFQKL-----HRDMEEATLHFETTSASLKK--- 1206
Cdd:COG1196 176 EAER----KLEATEENLER----LEDILGELE-RQLEPLERQAEKAERYRELkeelkELEAELLLLKLRELEAELEElea 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1207 ---RHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLAN 1283
Cdd:COG1196 247 eleELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1284 DLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQ 1363
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1364 EVKAELHRTLSKVNAEMVQWRMKyENNVIQRTEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSD 1443
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEA-LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1444 LGKVRSAAARLDQKQLQSGKALADWKQKHEESQ------------------------ALLDASQKEVQALSTELLKLKNT 1499
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGlrglagavavligveaayeaaleaALAAALQNIVVEDDEVAAAAIEY 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1500 YEESIVGQETLRRENK-NLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELL 1578
Cdd:COG1196 566 LKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1579 EAKAELERKLSEKDEEIENFRRKQQctidslQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQL 1658
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRREL------LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1659 QIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQ-SELEDLRSLQEQTERGRR----------LSEEELLEATERINL 1727
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEElPEPPDLEELERELERLEReiealgpvnlLAIEEYEELEERYDF 799
|
650 660 670
....*....|....*....|....*....|..
gi 119600132 1728 FYTQNTSLLSQKKKLEADVARMQKEAEEVVQE 1759
Cdd:COG1196 800 LSEQREDLEEARETLEEAIEEIDRETRERFLE 831
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1074-1724 |
3.63e-16 |
|
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: 84.77 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1074 NRESMENLESSQRHLAEELRK----KELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERa 1149
Cdd:pfam05483 72 NSEGLSRLYSKLYKEAEKIKKwkvsIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEN- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1150 DLTQDLADLNERLEEVGGSSLAQLEITKKQETK-FQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQK 1228
Cdd:pfam05483 151 NATRHLCNLLKETCARSAEKTKKYEYEREETRQvYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1229 LEKDKSDLQLEVDDLLTrveQMTRAKANAEKLCTLYEErlheataKLDKVTQLandlaAQKTKLWSESgeflrrleekea 1308
Cdd:pfam05483 231 YKKEINDKEKQVSLLLI---QITEKENKMKDLTFLLEE-------SRDKANQL-----EEKTKLQDEN------------ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1309 lINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYE 1388
Cdd:pfam05483 284 -LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1389 N---NVIQRTEDLEDAKKELAIRLQEAAEAMgvanarnASLERARHQLQLElgdaLSDLGKVRSAAARLDQKQLQSGKAL 1465
Cdd:pfam05483 363 EllrTEQQRLEKNEDQLKIITMELQKKSSEL-------EEMTKFKNNKEVE----LEELKKILAEDEKLLDEKKQFEKIA 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1466 ADWKQKHEESQALLDASQKEVQALSTELLKLKNTyeesivgQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLI 1545
Cdd:pfam05483 432 EELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS-------EEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1546 EEEKTEVQVTLEETEGALERNESKilhfQLELLEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTR 1625
Cdd:pfam05483 505 TQEASDMTLELKKHQEDIINCKKQ----EERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEY 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1626 LKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQ-LDDSTQLNSdLKEQVAVAERRNSLLQSELEDLRSLQ 1704
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKgSAENKQLNA-YEIKVNKLELELASAKQKFEEIIDNY 659
|
650 660
....*....|....*....|
gi 119600132 1705 EQTERGRRLSEEELLEATER 1724
Cdd:pfam05483 660 QKEIEDKKISEEKLLEEVEK 679
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1306-1938 |
1.47e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1306 KEALiNQLSREKSNFTRqIEDLRGQLEK----------------------ETKSQSALAHALQKAQRDCDLLREQYEEEQ 1363
Cdd:COG1196 175 EEAE-RKLEATEENLER-LEDILGELERqleplerqaekaeryrelkeelKELEAELLLLKLRELEAELEELEAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1364 EVKAELHRTLSKVNAEMvqwrmkyennviqrtEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSD 1443
Cdd:COG1196 253 AELEELEAELAELEAEL---------------EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1444 LGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISN 1523
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1524 LTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRKQQ 1603
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1604 CTIDSLQSSLDSEAKsrievtrlkkkmEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQV 1683
Cdd:COG1196 478 ALAELLEELAEAAAR------------LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1684 AVAERRNSLLQSELEDLRSLQEQTERGR----RLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQE 1759
Cdd:COG1196 546 AALQNIVVEDDEVAAAAIEYLKAAKAGRatflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1760 CQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALmgSRKQIQKLESRVRELEGELE 1839
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE--LAERLAEEELELEEALLAEE 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1840 GEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQ-------- 1911
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREiealgpvn 783
|
650 660 670
....*....|....*....|....*....|
gi 119600132 1912 ---QHELNEVKERAEVAESQVNKLKiKARE 1938
Cdd:COG1196 784 llaIEEYEELEERYDFLSEQREDLE-EARE 812
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1473-1946 |
2.44e-15 |
|
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: 82.53 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1473 EESQALLDASQKEVQALSTELLKLKNTYEESIVGqetLRRENKNLQEEISNLTNQV--REGTKNLTEMEKVKKLIEEEKT 1550
Cdd:pfam01576 60 EEMRARLAARKQELEEILHELESRLEEEEERSQQ---LQNEKKKMQQHIQDLEEQLdeEEAARQKLQLEKVTTEAKIKKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1551 EVQVTLEETEGALERNESKILHfqlellEAKAELERKLSEKDEEIENF---RRKQQCTIDSLQSSLDSEAKSRIEVTRLK 1627
Cdd:pfam01576 137 EEDILLLEDQNSKLSKERKLLE------ERISEFTSNLAEEEEKAKSLsklKNKHEAMISDLEERLKKEEKGRQELEKAK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1628 KKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQT 1707
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1708 ERGRRLSEEELlEATeRINLFYTQNTSLLSQ--KKKLEADVARMQK--EAEEVVQECQnAEEKAKKAAIEAANLSEELKK 1783
Cdd:pfam01576 291 EKQRRDLGEEL-EAL-KTELEDTLDTTAAQQelRSKREQEVTELKKalEEETRSHEAQ-LQEMRQKHTQALEELTEQLEQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1784 KQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQiQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELT 1863
Cdd:pfam01576 368 AKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKR-KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVS 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1864 YQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEvAETQANQYLSKYKKQ--------QHELNEVKERAEVAESQVNKLKIK 1935
Cdd:pfam01576 447 SLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ-EETRQKLNLSTRLRQledernslQEQLEEEEEAKRNVERQLSTLQAQ 525
|
490
....*....|.
gi 119600132 1936 AREFGKKVQEE 1946
Cdd:pfam01576 526 LSDMKKKLEED 536
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
858-1762 |
5.19e-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: 81.25 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 858 GEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKnDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSER 937
Cdd:TIGR00606 199 GQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 938 VEEEEEINSELTargRKLEDECFELKKEIDDLETMlvkSEKEKRTTEHKVKNLTEEVEFLNEDISKLN--RAAKVVQEAH 1015
Cdd:TIGR00606 278 KKQMEKDNSELE---LKMEKVFQGTDEQLNDLYHN---HQRTVREKERELVDCQRELEKLNKERRLLNqeKTELLVEQGR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1016 QQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKK 1095
Cdd:TIGR00606 352 LQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEI 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1096 ELELSQMNSKVENEKglvAQLQKTVKELQTQIKDLKeklEAERTTRAKMERERAdLTQDLADLNERLEEvggsslAQLEI 1175
Cdd:TIGR00606 432 RDEKKGLGRTIELKK---EILEKKQEELKFVIKELQ---QLEGSSDRILELDQE-LRKAERELSKAEKN------SLTET 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1176 TKKQETKFQKLHRDMEEaTLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLL---TRVEQMTR 1252
Cdd:TIGR00606 499 LKKEVKSLQNEKADLDR-KLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLgyfPNKKQLED 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1253 AKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSEsgefLRRLEEKeaLINQLSREksNFTRQIEDLRGQLE 1332
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQ----LSSYEDK--LFDVCGSQ--DEESDLERLKEEIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1333 KETKSQSALAHALQKAqrdcDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEA 1412
Cdd:TIGR00606 650 KSSKQRAMLAGATAVY----SQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRR 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1413 AEAMGVANARNASLERarhqLQLELGDALSDLGKVRSAAARLdQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTE 1492
Cdd:TIGR00606 726 DEMLGLAPGRQSIIDL----KEKEIPELRNKLQKVNRDIQRL-KNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQME 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1493 LLKLKNTYEE------SIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQvTLEETEGALERN 1566
Cdd:TIGR00606 801 LKDVERKIAQqaaklqGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTN-ELKSEKLQIGTN 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1567 ESKILHFQLELLEAKAELE---RKLSEKDEEI---ENFRRKQQCTIDSLQSSLDSEAK-SRIEVTRLKKKM--------- 1630
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTEVQsliREIKDAKEQDsplETFLEKDQQEKEELISSKETSNKkAQDKVNDIKEKVknihgymkd 959
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1631 ---------EEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLR 1701
Cdd:TIGR00606 960 ienkiqdgkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQ 1039
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119600132 1702 SLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEvvQECQN 1762
Cdd:TIGR00606 1040 HLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE--PQFRD 1098
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
864-1560 |
7.00e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 80.93 E-value: 7.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 864 LKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIK-SKIQLEARVKELSERVEEEE 942
Cdd:pfam15921 108 LRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEdSNTQIEQLRKMMLSHEGVLQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 943 EINSELT----ARGRKLEDEcfelkkeiDDLETMLVKSEKEkrTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQT 1018
Cdd:pfam15921 188 EIRSILVdfeeASGKKIYEH--------DSMSTMHFRSLGS--AISKILRELDTEISYLKGRIFPVEDQLEALKSESQNK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1019 LDDLhmeeeklssLSKANLKLEQQVDELE----GALEQERKARmnceRELHKLEGNLKLNRESMENLESS-QRHLAEelr 1093
Cdd:pfam15921 258 IELL---------LQQHQDRIEQLISEHEveitGLTEKASSAR----SQANSIQSQLEIIQEQARNQNSMyMRQLSD--- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1094 kKELELSQMNSKVENEKGLvaqLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDL----ADLNERLEEvggss 1169
Cdd:pfam15921 322 -LESTVSQLRSELREAKRM---YEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLqkllADLHKREKE----- 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1170 laqLEITKKQETKF-----------QKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKS-DLQ 1237
Cdd:pfam15921 393 ---LSLEKEQNKRLwdrdtgnsitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSlTAQ 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1238 LEVDDLLTR--VEQMTRAKANAEK-------LCTLYEERLHEATAKLDKVTQLAN--DLAAQKTKLWSESGEFLRRLE-E 1305
Cdd:pfam15921 470 LESTKEMLRkvVEELTAKKMTLESsertvsdLTASLQEKERAIEATNAEITKLRSrvDLKLQELQHLKNEGDHLRNVQtE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1306 KEALINQLSREKsnftRQIEDLRGQLEKETK-----SQSALAHALQKAQRDCDLlREQYEEEQEVKA----------ELH 1370
Cdd:pfam15921 550 CEALKLQMAEKD----KVIEILRQQIENMTQlvgqhGRTAGAMQVEKAQLEKEI-NDRRLELQEFKIlkdkkdakirELE 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1371 RTLSKVNAEMVQW------RMKYENNVIQRTEDLEDAKKELAIRLQEAAEAMGV--ANARNAS--LERARHQLQLELGDA 1440
Cdd:pfam15921 625 ARVSDLELEKVKLvnagseRLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVlkRNFRNKSeeMETTTNKLKMQLKSA 704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1441 LSDLGKVRSAAARLD-------------QKQLQSGKALADWKQKHEE--SQALLDASQK------EVQALSTELLKLKnT 1499
Cdd:pfam15921 705 QSELEQTRNTLKSMEgsdghamkvamgmQKQITAKRGQIDALQSKIQflEEAMTNANKEkhflkeEKNKLSQELSTVA-T 783
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119600132 1500 YEESIVGQ-ETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEE--KTEVQVTLEETE 1560
Cdd:pfam15921 784 EKNKMAGElEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQEsvRLKLQHTLDVKE 847
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1001-1945 |
1.60e-14 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 79.71 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1001 ISKLNRAAKVVQEaHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKlnreSMEN 1080
Cdd:TIGR00606 185 IKALETLRQVRQT-QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLK----EIEH 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1081 LESSQRHLAEELR---KKELELSQMNSKVEnekglvaqlQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLAD 1157
Cdd:TIGR00606 260 NLSKIMKLDNEIKalkSRKKQMEKDNSELE---------LKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1158 LNERleevggsslAQLEITKKQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGqvenlqqvkqkLEKDkSDLQ 1237
Cdd:TIGR00606 331 LNKE---------RRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDG-----------FERG-PFSE 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1238 LEVDDLLTRV-EQMTRAKANAEKLCTLYEERLHEATAKLDKvtqlandLAAQKTKLWSESGEFLRRLEEKEALINQLSRE 1316
Cdd:TIGR00606 390 RQIKNFHTLViERQEDEAKTAAQLCADLQSKERLKQEQADE-------IRDEKKGLGRTIELKKEILEKKQEELKFVIKE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1317 KSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEeeQEVKAELHRTLSKVNAEMVQwrMKYENNVIQRTE 1396
Cdd:TIGR00606 463 LQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSL--QNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQME 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1397 DLEDAKKE-----LAIRLQEAAEAMGVAN--ARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWK 1469
Cdd:TIGR00606 539 MLTKDKMDkdeqiRKIKSRHSDELTSLLGyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKE 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1470 QKH-------------EESQALLDASQKEVQALSTELLKL--KNTYEESIVGQETLRREN------------KNLQEEIS 1522
Cdd:TIGR00606 619 EQLssyedklfdvcgsQDEESDLERLKEEIEKSSKQRAMLagATAVYSQFITQLTDENQSccpvcqrvfqteAELQEFIS 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1523 NLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILhfqlELLEAKAELERKLSEKDEEIEnfrrKQ 1602
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP----ELRNKLQKVNRDIQRLKNDIE----EQ 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1603 QCTIDSLQSSLDSEAKSRIEVTRLKK-KMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKE 1681
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERfQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1682 QVAVAERRNSLLQSELEDLRS--LQEQTERGRRLS-EEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQ 1758
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKSekLQIGTNLQRRQQfEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1759 ECQnaeekakkaaieaanlsEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQIQKLESRVRELEgel 1838
Cdd:TIGR00606 931 SKE-----------------TSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECE--- 990
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1839 egeiRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEV 1918
Cdd:TIGR00606 991 ----KHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLI 1066
|
970 980
....*....|....*....|....*..
gi 119600132 1919 KERAEVAESQVNKLKIKAREFGKKVQE 1945
Cdd:TIGR00606 1067 KRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
957-1456 |
2.54e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.93 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 957 DECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLnraakvvqeahqqtLDDLHMEEEKLSSLskan 1036
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL--------------LAEAGLDDADAEAV---- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1037 lklEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSqrhlAEELRKKELELsqmNSKVENEKGLVAQL 1116
Cdd:PRK02224 313 ---EARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER----AEELREEAAEL---ESELEEAREAVEDR 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1117 QKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVggsslaqleitkkqETKFQKLHRDMEEATLH 1196
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL--------------EATLRTARERVEEAEAL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1197 FE-----TTSASLKKR-HADSLAELEGQVEnlqqvkqKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYE----- 1265
Cdd:PRK02224 449 LEagkcpECGQPVEGSpHVETIEEDRERVE-------ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErredl 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1266 -ERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDL---RGQLEKETKSQSAL 1341
Cdd:PRK02224 522 eELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELkerIESLERIRTLLAAI 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1342 AHALQKAQRdcdlLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNviqRTEDLEDAKKELAIRLQEAAEAMgvana 1421
Cdd:PRK02224 602 ADAEDEIER----LREKREALAELNDERRERLAEKRERKRELEAEFDEA---RIEEAREDKERAEEYLEQVEEKL----- 669
|
490 500 510
....*....|....*....|....*....|....*
gi 119600132 1422 rnASLERARHQLQLELGDALSDLGKVRSAAARLDQ 1456
Cdd:PRK02224 670 --DELREERDDLQAEIGAVENELEELEELRERREA 702
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
951-1810 |
3.10e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.03 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 951 RGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQtlDDLHMEEEKLS 1030
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKA--EDARKAEEARK 1147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1031 SLSKANLKLEQQVDELEGAlEQERKARmncerELHKLEGNlklnRESMENLESSQRHLAEELRKKELElsqmnSKVENEK 1110
Cdd:PTZ00121 1148 AEDAKRVEIARKAEDARKA-EEARKAE-----DAKKAEAA----RKAEEVRKAEELRKAEDARKAEAA-----RKAEEER 1212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1111 GLVAQLQKTVKELQTQIKDLKE-KLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQlEITKKQETKFQKLHRD 1189
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKAEEaKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE-EARKADELKKAEEKKK 1291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1190 MEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLE--KDKSDLQLEVDDLLTRVEQMTRAKAN-AEKLCTLYEE 1266
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADaaKKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEAAEK 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1267 RLHEATAKLDKVTQLAN-----DLAAQKTKLWSESGEFLRRLEEKEALINQLsREKSNFTRQIEDLRGQLEKETKSQSAL 1341
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEekkkaDEAKKKAEEDKKKADELKKAAAAKKKADEA-KKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1342 AHALQKaqRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKElAIRLQEAAEAMGVANA 1421
Cdd:PTZ00121 1451 KKAEEA--KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK-ADEAKKAEEAKKADEA 1527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1422 RNAS----LERARHQLQLELGDALSDLGKVRSAAARldQKQLQSGKALAD---WKQKHEESQALLDASQKEVQALSTELL 1494
Cdd:PTZ00121 1528 KKAEeakkADEAKKAEEKKKADELKKAEELKKAEEK--KKAEEAKKAEEDknmALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1495 KLK----NTYEESIVGQETLRREnknlQEEISNLTNQVREGTKNLTEMEKVKKliEEEKTEVQVTLEETEGALERNESKI 1570
Cdd:PTZ00121 1606 KMKaeeaKKAEEAKIKAEELKKA----EEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAEEAKKAEEDKKKAEE 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1571 LHFQLELLEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDlnemelqlscaNRQVSE 1650
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED-----------KKKAEE 1748
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1651 ATKSLGQlqiQIKDLQMQLDDSTQLNSDLKEQVAVAERRnslLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYT 1730
Cdd:PTZ00121 1749 AKKDEEE---KKKIAHLKKEEEKKAEEIRKEKEAVIEEE---LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVIN 1822
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1731 QNTSLLSQKKKLEADVARMQK-EAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRL 1809
Cdd:PTZ00121 1823 DSKEMEDSAIKEVADSKNMQLeEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902
|
.
gi 119600132 1810 A 1810
Cdd:PTZ00121 1903 P 1903
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
988-1880 |
4.21e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 78.47 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 988 KNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKAnlklEQQVDELEGALEQERKARMNCERELHKL 1067
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLK----EQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1068 egnLKLNRESMENLEssqrhlaEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERE 1147
Cdd:pfam02463 232 ---LKLNEERIDLLQ-------ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1148 RADLTQDLADLNERLEEvggsslAQLEITKKQEtkfqklhrdmeeatlhfettsaslkkrhadSLAELEGQVENLQQVKQ 1227
Cdd:pfam02463 302 LLKLERRKVDDEEKLKE------SEKEKKKAEK------------------------------ELKKEKEEIEELEKELK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1228 KLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTklwSESGEFLRRLEEKE 1307
Cdd:pfam02463 346 ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ---LLLELARQLEDLLK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1308 ALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTL----SKVNAEMVQW 1383
Cdd:pfam02463 423 EEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELllsrQKLEERSQKE 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1384 RMKYENN------VIQRTEDLEDAKKELAIRLQEAAEAMGVANarNASLERARHQLQLELGDALSDLGKVRSAAARLDQK 1457
Cdd:pfam02463 503 SKARSGLkvllalIKDGVGGRIISAHGRLGDLGVAVENYKVAI--STAVIVEVSATADEVEERQKLVRALTELPLGARKL 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1458 QLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKN-----TYEESIVGQETLRRENKNLQEEISNLTNQVREGT 1532
Cdd:pfam02463 581 RLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRakvveGILKDTELTKLKESAKAKESGLRKGVSLEEGLAE 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1533 KNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSS 1612
Cdd:pfam02463 661 KSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKL 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1613 LDSEAKSRIEV---TRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERR 1689
Cdd:pfam02463 741 LKQKIDEEEEEeekSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEE 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1690 NSLLQSELEDLRSLQEQ-------TERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQN 1762
Cdd:pfam02463 821 QLLIEQEEKIKEEELEElalelkeEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKK 900
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1763 AEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQIQKLESRVRELEGELEGEI 1842
Cdd:pfam02463 901 ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAI 980
|
890 900 910
....*....|....*....|....*....|....*...
gi 119600132 1843 RRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQM 1880
Cdd:pfam02463 981 EEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQR 1018
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1042-1725 |
1.27e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1042 QVDELEGALEQERKARMNCERELHKLEGNLKlnreSMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVK 1121
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIK----RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1122 ELqtqiKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVggsslaqleitKKQETKFQKLHRDMEEAtlhfetts 1201
Cdd:PRK03918 232 EL----EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL-----------KKEIEELEEKVKELKEL-------- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1202 aslkKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEE------RLHEATAKL 1275
Cdd:PRK03918 289 ----KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekrleELEERHELY 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1276 DKVTQLANDLAAQKTKLWSESgeflrrLEEKEALINQLSREKSNFTRQIEDL---RGQLEKETKSQSALAHALQKAQRDC 1352
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLT------PEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAKGKC 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1353 DLLREQYEEEQ--EVKAELHRTLSKVNAEMvqwrmkyennvIQRTEDLEDAKKELairlqeaaeamgvanaRNASLERAR 1430
Cdd:PRK03918 439 PVCGRELTEEHrkELLEEYTAELKRIEKEL-----------KEIEEKERKLRKEL----------------RELEKVLKK 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1431 HQLQLELGDALSDLGKVRSAAARLDQKQLQsgkalADWKqKHEESQALLDASQKEVQALSTELLKLKNTYEESivgqETL 1510
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKYNLEELE-----KKAE-EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL----AEL 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1511 RRENKNLQEEISNLTNQVRE-GTKNLTEMEKVKKLIEEEKTEVqVTLEETEGALERNESKILHFQLELLEAKAELErkls 1589
Cdd:PRK03918 562 EKKLDELEEELAELLKELEElGFESVEELEERLKELEPFYNEY-LELKDAEKELEREEKELKKLEEELDKAFEELA---- 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1590 EKDEEIENFRRKqqctIDSLQSSLDSEAKSRIEVTRLKKKMEedLNEMELQLSCANRQVSEATKSLGQLQIQikdlqmql 1669
Cdd:PRK03918 637 ETEKRLEELRKE----LEELEKKYSEEEYEELREEYLELSRE--LAGLRAELEELEKRREEIKKTLEKLKEE-------- 702
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 119600132 1670 ddstqlnsdlKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERI 1725
Cdd:PRK03918 703 ----------LEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1216-1945 |
1.46e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1216 EGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMT--RAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKlw 1293
Cdd:PTZ00121 1057 EGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEAteEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-- 1134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1294 seSGEFLRRLEEKEALINQlsrEKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQ--RDCDLLREQYEE---EQEVKAE 1368
Cdd:PTZ00121 1135 --KAEDARKAEEARKAEDA---KRVEIARKAEDARKAEEARKAEDAKKAEAARKAEevRKAEELRKAEDArkaEAARKAE 1209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1369 LHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEaaEAMGVANARNASLERARHQLQLELGDALSDLGKVR 1448
Cdd:PTZ00121 1210 EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE--EIRKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1449 SAAARLDQKQLQSGKALADWKQKHEESQALlDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNlTNQV 1528
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA-AEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1529 REGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKIlhfqlELLEAKAELERKLSEKDEEIENFRRKQQCTIDS 1608
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA-----DELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1609 LQSSLDSEAKSRIEVTR----LKKKMEEDLNEMELQLSCAN-RQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLK--E 1681
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKkaeeAKKKAEEAKKADEAKKKAEEaKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaeE 1520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1682 QVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERinlfytqntSLLSQKKKLEADVARMQKEAEEVVQ-EC 1760
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEK---------KKAEEAKKAEEDKNMALRKAEEAKKaEE 1591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1761 QNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQIQKLESRVRELEGELEG 1840
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1841 EIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQylskYKKQQHELNEVKE 1920
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE----AKKEAEEDKKKAE 1747
|
730 740
....*....|....*....|....*
gi 119600132 1921 RAEVAESQVNKLKIKAREFGKKVQE 1945
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
865-1754 |
1.99e-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: 76.16 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 865 KEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQL-QAEQETLANVEEqcewliksKIQLEARVKelserveeeee 943
Cdd:pfam02463 221 LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEiEKEEEKLAQVLK--------ENKEEEKEK----------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 944 inSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDdlh 1023
Cdd:pfam02463 282 --KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE--- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1024 mEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMN 1103
Cdd:pfam02463 357 -EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1104 SKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKF 1183
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLAL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1184 QKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEV--DDLLTRVEQMTRAKANAEKLC 1261
Cdd:pfam02463 516 IKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTElpLGARKLRLLIPKLKLPLKSIA 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1262 TLYEERLHEATAKldkvtQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSAL 1341
Cdd:pfam02463 596 VLEIDPILNLAQL-----DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSE 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1342 AHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYEnnviQRTEDLEDAKKELAIRLQEaaeamgvaNA 1421
Cdd:pfam02463 671 LTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL----EAEELLADRVQEAQDKINE--------EL 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1422 RNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYE 1501
Cdd:pfam02463 739 KLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1502 ESIvgqetlrrENKNLQEEISNLTNQvrEGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAK 1581
Cdd:pfam02463 819 EEQ--------LLIEQEEKIKEEELE--ELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDEL 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1582 AELERKLSEKDEEIENFRRkqqctIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELqLSCANRQVSEATKSLGQLQIQ 1661
Cdd:pfam02463 889 ESKEEKEKEEKKELEEESQ-----KLNLLEEKENEIEERIKEEAEILLKYEEEPEELL-LEEADEKEKEENNKEEEEERN 962
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1662 IKDLQMQLDDSTQLNSDLKEQVAVAERRNsllqSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKK 1741
Cdd:pfam02463 963 KRLLLAKEELGKVNLMAIEEFEEKEERYN----KDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFF 1038
|
890
....*....|...
gi 119600132 1742 LEADVARMQKEAE 1754
Cdd:pfam02463 1039 YLELGGSAELRLE 1051
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1547-1862 |
2.71e-13 |
|
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: 75.86 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1547 EEKTEVQVTLEETEGALERNESKI--LHFQLELLEAKAELERKLSEKDEEIENFRrkqqctIDSLQSSLDSEAKSRIEVT 1624
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILneLERQLKSLERQAEKAERYKELKAELRELE------LALLVLRLEELREELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1625 RLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQ 1704
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1705 EQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKK 1784
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1785 QDTIAHLERTRENMEQTITDLQKRLAEAE----QMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIK 1860
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAElkelQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
..
gi 119600132 1861 EL 1862
Cdd:TIGR02168 486 QL 487
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1115-1873 |
4.30e-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: 75.15 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1115 QLQKTVKELQTQIKDLKEKLEAERTTRakmERERADLTQDLADLNERLEEVGGSSLAQLEItKKQETKFQKLHRDMEEAT 1194
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELH---EKQKFYLRQSVIDLQTKLQEMQMERDAMADI-RRRESQSQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1195 LHFETTSASLKKrhaDSLAELEGQVENLQQVKQKLEkdksDLQLEVDDLLTRVEQMTRAKA-NAEKLCTLYEERLHEATA 1273
Cdd:pfam15921 151 VHELEAAKCLKE---DMLEDSNTQIEQLRKMMLSHE----GVLQEIRSILVDFEEASGKKIyEHDSMSTMHFRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1274 KLdkVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNftrQIEDLRGQLEKET-----KSQSALAHAlQKA 1348
Cdd:pfam15921 224 KI--LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQD---RIEQLISEHEVEItglteKASSARSQA-NSI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1349 QRDCDLLREQYEEEQEVK----AELHRTLSKVNAEMVQWRMKYENNViqrtedlEDAKKELAIRLQEAAEAmgvaNARNA 1424
Cdd:pfam15921 298 QSQLEIIQEQARNQNSMYmrqlSDLESTVSQLRSELREAKRMYEDKI-------EELEKQLVLANSELTEA----RTERD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1425 SLERARHQLQLELGDALSDLGKvRSAAARLDQKQlqsGKALadWKQKHEESQAL------LDASQKEVQALSTELLKLKN 1498
Cdd:pfam15921 367 QFSQESGNLDDQLQKLLADLHK-REKELSLEKEQ---NKRL--WDRDTGNSITIdhlrreLDDRNMEVQRLEALLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1499 TYEESIVGQ-ETLRRENKNLqEEISNLTNQV---REGTKNLTEMEKVKKLIEE--EKT--EVQVTLEETEGALERNESKI 1570
Cdd:pfam15921 441 ECQGQMERQmAAIQGKNESL-EKVSSLTAQLestKEMLRKVVEELTAKKMTLEssERTvsDLTASLQEKERAIEATNAEI 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1571 L--------------HFQLE---LLEAKAE---LERKLSEKDEEIENFRRKqqctIDSLQSSLDSEAKSRIEVTRLKKKM 1630
Cdd:pfam15921 520 TklrsrvdlklqelqHLKNEgdhLRNVQTEceaLKLQMAEKDKVIEILRQQ----IENMTQLVGQHGRTAGAMQVEKAQL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1631 EEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSD-LKEQVAVAERRNSLL------QSELEDLRSL 1703
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSErLRAVKDIKQERDQLLnevktsRNELNSLSED 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1704 QEQTERGRRLSEEELLEATERINLFYTQNTSLLSQK----KKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSE 1779
Cdd:pfam15921 676 YEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTrntlKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEE 755
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1780 ELKKKQDTIAHLERTRENMEQTITDLQkrlAEAEQMA--LMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLER 1857
Cdd:pfam15921 756 AMTNANKEKHFLKEEKNKLSQELSTVA---TEKNKMAgeLEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQ 832
|
810
....*....|....*.
gi 119600132 1858 CIKELTYQAEEDKKNL 1873
Cdd:pfam15921 833 ESVRLKLQHTLDVKEL 848
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
847-1292 |
7.64e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 7.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 847 KIKPLVKSSEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLqaeqETLANVEEQCEWLIKSKIQ 926
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 927 LEARVKELSERVeeeeeinsELTARGRKLEDECFELKK-----EIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDI 1001
Cdd:PRK03918 350 LEKRLEELEERH--------ELYEEAKAKKEELERLKKrltglTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1002 SKLNRAAKVVQEAHQQ--TLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARmnceRELHKLEGNLKLNRESme 1079
Cdd:PRK03918 422 KELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLR----KELRELEKVLKKESEL-- 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1080 nleSSQRHLAEELRKKELELSQMN-SKVENEKGLVAQLQKTVKELQTQIKDLK---EKLEAERTTRAKMERERADLTQDL 1155
Cdd:PRK03918 496 ---IKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDELEEEL 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1156 ADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDMEEATLHFEttsaSLKKRHADSLAELEGQVENLQQVKQKLEKDKSD 1235
Cdd:PRK03918 573 AELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELE----REEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 119600132 1236 L-QLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKL 1292
Cdd:PRK03918 649 LeELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
954-1662 |
1.49e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 73.08 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 954 KLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAH--QQTLDDLHMEEEKLSS 1031
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1032 ----LSKANLKLEQQVDELEGALEQER---------------KARMNC-ERELHKLEGNLKLNRESMENLESSQRHLAEE 1091
Cdd:TIGR00618 275 qeavLEETQERINRARKAAPLAAHIKAvtqieqqaqrihtelQSKMRSrAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1092 LRKKELELSQMNSKVENEKGLvaQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERAdlTQDLADLNERLEEvggsslA 1171
Cdd:TIGR00618 355 IHIRDAHEVATSIREISCQQH--TLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQA--TIDTRTSAFRDLQ------G 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1172 QLEITKKQEtKFQKLHRDMEEATLHFETTSASLKKRHADSLAE-LEGQVENLQQVKQKLEKDKSdlqlevddllTRVEQM 1250
Cdd:TIGR00618 425 QLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQsLKEREQQLQTKEQIHLQETR----------KKAVVL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1251 TRAKANAEKLCTLYEERLHeatakldkvtqlandlAAQKTKLWSESGEFLRRLEEKEALINQLSREksnftrqIEDLRGQ 1330
Cdd:TIGR00618 494 ARLLELQEEPCPLCGSCIH----------------PNPARQDIDNPGPLTRRMQRGEQTYAQLETS-------EEDVYHQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1331 LEKETKSQSALAHALQKAQRDCDLLREQYeeeQEVKAELHRTLSKVNaEMVQWRMKYENNVIQRTEDL--EDAKKELAIR 1408
Cdd:TIGR00618 551 LTSERKQRASLKEQMQEIQQSFSILTQCD---NRSKEDIPNLQNITV-RLQDLTEKLSEAEDMLACEQhaLLRKLQPEQD 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1409 LQEAAEAMGVANARNASLERARHQLQLELgdaLSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQA-----LLDASQ 1483
Cdd:TIGR00618 627 LQDVRLHLQQCSQELALKLTALHALQLTL---TQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkeMLAQCQ 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1484 KEVQALSTELLKLKNTYEE----SIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEET 1559
Cdd:TIGR00618 704 TLLRELETHIEEYDREFNEienaSSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHL 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1560 EGALERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMEl 1639
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA- 862
|
730 740
....*....|....*....|....*.
gi 119600132 1640 QLSCANRQVSEATKSLG---QLQIQI 1662
Cdd:TIGR00618 863 QLTQEQAKIIQLSDKLNginQIKIQF 888
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
864-1515 |
1.52e-12 |
|
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: 72.83 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 864 LKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKskiqlEARVKELSERVEEEEE 943
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLK-----EDHEKIQHLEEEYKKE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 944 INSElTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLH 1023
Cdd:pfam05483 235 INDK-EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1024 MEEEKLSSLSKAnlkLEQQVDELEGALEQERKAR-------MNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKE 1096
Cdd:pfam05483 314 ALEEDLQIATKT---ICQLTEEKEAQMEELNKAKaahsfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1097 LELSQMNSKVENEKGLVAQLQKTVKElqtqikdlKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEIT 1176
Cdd:pfam05483 391 SELEEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAI 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1177 KKQETKFQKLHRDMEEatlhfETTSASLKKrhadslAELEGQVENLQQVKQKLEKDKSDLQLEvddLLTRVEQMTRAKAN 1256
Cdd:pfam05483 463 KTSEEHYLKEVEDLKT-----ELEKEKLKN------IELTAHCDKLLLENKELTQEASDMTLE---LKKHQEDIINCKKQ 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1257 AEKLctlyeerLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETK 1336
Cdd:pfam05483 529 EERM-------LKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKK 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1337 SQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEAAEAM 1416
Cdd:pfam05483 602 QIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAK 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1417 GVANARNASLERARHQLQLELGDALSDLGKVRSaaaRLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKL 1496
Cdd:pfam05483 682 AIADEAVKLQKEIDKRCQHKIAEMVALMEKHKH---QYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSL 758
|
650
....*....|....*....
gi 119600132 1497 KNTYEESIVGQETLRRENK 1515
Cdd:pfam05483 759 KKQLEIEKEEKEKLKMEAK 777
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
974-1607 |
1.62e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 974 VKSEKEKRTTEHKVKnlTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQE 1053
Cdd:PTZ00121 1289 KKKADEAKKAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1054 RKARMNCERELHKLEGNLKLNRESMENLESSQRhlAEELRKK--ELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLK 1131
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK--AEEDKKKadELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1132 EKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLH--RDMEEATLHFETTSASLKKRHA 1209
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADeaKKAAEAKKKADEAKKAEEAKKA 1524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1210 DSL--AELEGQVENLQQV--KQKLEKDKSDLQLEVDDLLTRVEQMTRAKAN-------AEKLCTLYEERLHEATaKLDKV 1278
Cdd:PTZ00121 1525 DEAkkAEEAKKADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAKKAEEDknmalrkAEEAKKAEEARIEEVM-KLYEE 1603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1279 TQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREq 1358
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK- 1682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1359 yEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEAA-----EAMGVANARNASLERAR-HQ 1432
Cdd:PTZ00121 1683 -AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKkeaeeDKKKAEEAKKDEEEKKKiAH 1761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1433 LQLELGDALSDLGKVRSAAAR--LDQK----QLQSGKALADWKQKHE--------------ESQALLDASQKEVQALSTE 1492
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEeeLDEEdekrRMEVDKKIKDIFDNFAniieggkegnlvinDSKEMEDSAIKEVADSKNM 1841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1493 LLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEktevqVTLEETEGALERNESKILH 1572
Cdd:PTZ00121 1842 QLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDD-----IEREIPNNNMAGKNNDIID 1916
|
650 660 670
....*....|....*....|....*....|....*
gi 119600132 1573 FQLELLEAKaelERKLSEKDEEIENFRRKQQCTID 1607
Cdd:PTZ00121 1917 DKLDKDEYI---KRDAEETREEIIKISKKDMCIND 1948
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1037-1595 |
1.62e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1037 LKLEQQVDELEGALEQERKARmncERELHKLEGNLKLNRESMENLESSQRHL---AEELRKKELELSQMNSKVENEKGLV 1113
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEV---LREINEISSELPELREELEKLEKEVKELeelKEEIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1114 AQLQKTVKELQTQIKDLKEK--------------------LEAERTTRAKMERERADLTQDLADLNERLEEvGGSSLAQL 1173
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKvkelkelkekaeeyiklsefYEEYLDELREIEKRLSRLEEEINGIEERIKE-LEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1174 EITKKQETKFQKLHRDMEEATLHFETTSA------SLKKRHAD-SLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTR 1246
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEAKAkkeeleRLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1247 VEQMTRAKA---NAEKLCTLYEERLHEATAK--LDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNft 1321
Cdd:PRK03918 421 IKELKKAIEelkKAKGKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL-- 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1322 RQIEDLRGQLEKETKSqsalaHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNaemvqwrmkyennviqRTEDLEDA 1401
Cdd:PRK03918 499 KELAEQLKELEEKLKK-----YNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE----------------KLEELKKK 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1402 KKELAIRLQEAAEAMGVANAR-----NASLERARHQLQlELGDALSDLGKVRSAAARLDQKQlqsgKALADWKQKHEESQ 1476
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKEleelgFESVEELEERLK-ELEPFYNEYLELKDAEKELEREE----KELKKLEEELDKAF 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1477 ALLDASQKEVQALSTELLKLKNTYEESivGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTL 1556
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710
|
570 580 590
....*....|....*....|....*....|....*....
gi 119600132 1557 EETEgALERNESKILHFQLELLEAKAELERKLSEKDEEI 1595
Cdd:PRK03918 711 KELE-KLEKALERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
984-1597 |
1.88e-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: 72.75 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 984 EHKVKNLTEEVEFLNEDISKLNRAAKVVQeahqqtlDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERE 1063
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLD-------KNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1064 LHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAK 1143
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1144 MERERADLTQDLADLNERL------EEVGGSSLAQLEITKKQ----ETKFQKLHRDMEEATLHFETTSASLK------KR 1207
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLLsnlkkkIQKNKSLESQISELKKQnnqlKDNIEKKQQEINEKTTEISNTQTQLNqlkdeqNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1208 HADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAK-----ANAEKLCTLYEERLHEATAKLDKVTQLA 1282
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKElkselKNQEKKLEEIQNQISQNNKIISQLNEQI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1283 NDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKS-------NFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLL 1355
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQsykqeikNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1356 REQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTE-----------------DLEDAKKELAIRLQEAAEamgv 1418
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESletqlkvlsrsinkikqNLEQKQKELKSKEKELKK---- 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1419 ANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKqlqsgkaLADWKQKHEESQALLDASQ--KEVQALSTELLKL 1496
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK-------ISDLEDELNKDDFELKKENleKEIDEKNKEIEEL 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1497 KNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLE 1576
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
650 660
....*....|....*....|.
gi 119600132 1577 LLEAKAelerKLSEKDEEIEN 1597
Cdd:TIGR04523 654 IKEIRN----KWPEIIKKIKE 670
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1220-1920 |
4.59e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 71.54 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1220 ENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLaNDLAAQKTKLWSESGEF 1299
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1300 LRRLEEKEALINQLS--REKSNFTRQIEDLrgqlekeTKSQSALAHALQKAQRDCDLLREQyeEEQEVKAELHRTLSKVN 1377
Cdd:TIGR00618 266 RARIEELRAQEAVLEetQERINRARKAAPL-------AAHIKAVTQIEQQAQRIHTELQSK--MRSRAKLLMKRAAHVKQ 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1378 AEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEAAEAMgvanarnaSLERARHQLQLELGdalSDLGKVRSAAARLDQK 1457
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQH--------TLTQHIHTLQQQKT---TLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1458 QLQSGKALADWKQKHEESQALLDA-SQKEVQALSTELLKL--KNTYEESIVGQETLRRENKNLQEEISNLTNqVREGTKN 1534
Cdd:TIGR00618 406 QREQATIDTRTSAFRDLQGQLAHAkKQQELQQRYAELCAAaiTCTAQCEKLEKIHLQESAQSLKEREQQLQT-KEQIHLQ 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1535 LTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQ------LELLEAKAELERKLSEKDEEIENFRRKQQCTIDS 1608
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpltrrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1609 LQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAER 1688
Cdd:TIGR00618 565 MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1689 RNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERInLFYTQN--TSLLSQKKKLEADVARMQKEAEEVVQECQNAEEK 1766
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALSIRVLPKELLASRQLA-LQKMQSekEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEI 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1767 AKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQ---IQKLESRVRELEGELEGEIR 1843
Cdd:TIGR00618 724 ENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELshlAAEIQFFNRLREEDTHLLKT 803
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119600132 1844 RSAEAQRGARRLErciKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEVKE 1920
Cdd:TIGR00618 804 LEAEIGQEIPSDE---DILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1301-1919 |
5.11e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 71.30 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1301 RRLEEKealiNQLSREKSNFTRQ-IEDLRGQLEKETKSQSALAhalqkaqrdcDLLREQYEEEQEVKAELHRTLSKVNAE 1379
Cdd:pfam15921 92 RRLNES----NELHEKQKFYLRQsVIDLQTKLQEMQMERDAMA----------DIRRRESQSQEDLRNQLQNTVHELEAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1380 --MVQWRMKYENNVIQRTEDL----EDAKKELAIRLQEAAEAMG--------VANARNASLERARHQLQLELGDALSDL- 1444
Cdd:pfam15921 158 kcLKEDMLEDSNTQIEQLRKMmlshEGVLQEIRSILVDFEEASGkkiyehdsMSTMHFRSLGSAISKILRELDTEISYLk 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1445 GKVRSAAARLDQKQLQSGKALADWKQKHEES-QALLDASQKEVQALsTELLKLKNTYEESI-----VGQETLRRENKNLQ 1518
Cdd:pfam15921 238 GRIFPVEDQLEALKSESQNKIELLLQQHQDRiEQLISEHEVEITGL-TEKASSARSQANSIqsqleIIQEQARNQNSMYM 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1519 EEISNLTNQVREGTKNLTEMEKV--KKLIEEEKTEVQVTLEETEGALERN----ESKILHFQLE-LLEAKAELERKLS-- 1589
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMyeDKIEELEKQLVLANSELTEARTERDqfsqESGNLDDQLQkLLADLHKREKELSle 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1590 -EKDEEIENFRRKQQCTIDSLQSSLDSEaksRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQlqiqIKDLQMQ 1668
Cdd:pfam15921 397 kEQNKRLWDRDTGNSITIDHLRRELDDR---NMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEK----VSSLTAQ 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1669 LDDSTQLNSDLKEQVAVaeRRNSLLQSE--LEDLRSLQEQTERGRRLSEEELLEATERINLFYTQntslLSQKKKLEADV 1746
Cdd:pfam15921 470 LESTKEMLRKVVEELTA--KKMTLESSErtVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQE----LQHLKNEGDHL 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1747 ARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDlqkRLAEAEQMALMGSRK--QI 1824
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIND---RRLELQEFKILKDKKdaKI 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1825 QKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQlkvQNYKQQVEVAETQANQY 1904
Cdd:pfam15921 621 RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK---RNFRNKSEEMETTTNKL 697
|
650
....*....|....*
gi 119600132 1905 LSKYKKQQHELNEVK 1919
Cdd:pfam15921 698 KMQLKSAQSELEQTR 712
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
870-1292 |
7.23e-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: 70.82 E-value: 7.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 870 QLQKALEKsefQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSERVEEEEEINSELT 949
Cdd:TIGR04523 211 QKNKSLES---QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 950 ARGRKLEDECFELKKE-----IDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHM 1024
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1025 EEEKLSSLSKAN-------LKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKEL 1097
Cdd:TIGR04523 368 KQNEIEKLKKENqsykqeiKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1098 ELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGG------SSLA 1171
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKkisslkEKIE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1172 QLEITKKQ-ETKFQKLHRDMEEatLHFETTSASLKKrhadSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQM 1250
Cdd:TIGR04523 528 KLESEKKEkESKISDLEDELNK--DDFELKKENLEK----EIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 119600132 1251 TRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKL 1292
Cdd:TIGR04523 602 IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1674-1946 |
1.13e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1674 QLNSdLKEQVAVAER-----------RNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKL 1742
Cdd:COG1196 201 QLEP-LERQAEKAERyrelkeelkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1743 EADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQmALMGSRK 1822
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE-ELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1823 QIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQAN 1902
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 119600132 1903 QYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQEE 1946
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1075-1640 |
2.95e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1075 RESMENLESSQRHLAEELRKKELeLSQMNSKVENEKGLVAQLQK--------TVKELQTQIKDLKEKLEAERTTRAKMER 1146
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERLAEleylraalRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1147 ERADLTQDLADLNERLEEV-------GGSSLAQLE--------ITKKQETKFQKLHRDMEEATLHFETTS---ASLKKRH 1208
Cdd:COG4913 310 ELERLEARLDALREELDELeaqirgnGGDRLEQLEreierlerELEERERRRARLEALLAALGLPLPASAeefAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1209 ADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANaeklctlYEERLHEATAKLDKVTQLAND---- 1284
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALRDALAEALGLDEAelpf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1285 ---------------------LAAQKTKL------WSESGEFLRRLEEKEAL-INQLSREKSNFTRQIEDLRGQLEK-ET 1335
Cdd:COG4913 463 vgelievrpeeerwrgaiervLGGFALTLlvppehYAAALRWVNRLHLRGRLvYERVRTGLPDPERPRLDPDSLAGKlDF 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1336 KSQSALAHALQKAQRDCDLLREQYEEEqevkaeLHRT--------LSKVNAEMVQ---WRMKYENNVIQRteDLEDAKKE 1404
Cdd:COG4913 543 KPHPFRAWLEAELGRRFDYVCVDSPEE------LRRHpraitragQVKGNGTRHEkddRRRIRSRYVLGF--DNRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1405 LAIRLQEAAEAMGVANARNASLERARHQLQlELGDALSDLGKVRSaaARLDQKQLQsgKALADWKQKHEEsqalLDASQK 1484
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSW--DEIDVASAE--REIAELEAELER----LDASSD 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1485 EVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVtLEETEGALE 1564
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF-AAALGDAVE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1565 RNESKILHFQLELLEAKAE-LERKLSEKdeeIENFRRKQQCTIDSLQSSLDSEAK-----SRIEVTRL---KKKMEEDLN 1635
Cdd:COG4913 765 RELRENLEERIDALRARLNrAEEELERA---MRAFNREWPAETADLDADLESLPEylallDRLEEDGLpeyEERFKELLN 841
|
....*
gi 119600132 1636 EMELQ 1640
Cdd:COG4913 842 ENSIE 846
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
49-94 |
3.43e-11 |
|
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: 59.75 E-value: 3.43e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 119600132 49 DGKKKCWIPDGENAYIEAEVKgSEDDGTVIVETADGESLSIKEDKI 94
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIK-EEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
911-1551 |
4.67e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 911 ANVEEQCEWLIKSKIQLEARVKELSERVEEEEEINSELTARGRKLEdecfELKKEIDDLETMLVKSEKEKRTTEHKVKNL 990
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 991 TEEVEFLNEDISKLNRAAKVVQEahqqtLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKarmNCERELHKLEGN 1070
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKELKE-----LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN---GIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1071 LKLNRESMENLESSQRHLaEELRKKELELSQMNSKVENEKGLVAQLQ-KTVKELQTQIKDLKEKLEAERTTRAKMERERA 1149
Cdd:PRK03918 337 EERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1150 DLTQDLADLNERLEEVggsslaqleitKKQETKFQKLHRDMEeatlhfETTSASLKKRHADSLAELEGQVENLQQVKQKL 1229
Cdd:PRK03918 416 ELKKEIKELKKAIEEL-----------KKAKGKCPVCGRELT------EEHRKELLEEYTAELKRIEKELKEIEEKERKL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1230 EKDKSdlqlEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEAL 1309
Cdd:PRK03918 479 RKELR----ELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1310 INQLsREKSNFTRQIEDLRGQLEKEtksqsalahalqkaqrdcdLLREQYEEEQEVKAELhRTLSKVNAEMVQWRmkyen 1389
Cdd:PRK03918 555 KKKL-AELEKKLDELEEELAELLKE-------------------LEELGFESVEELEERL-KELEPFYNEYLELK----- 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1390 NVIQRTEDLEDAKKELAIRLQEAAEAMGVANARnasLERARHQLQlELGDALSDlgkvrSAAARLDQKQLQSGKALADWK 1469
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKR---LEELRKELE-ELEKKYSE-----EEYEELREEYLELSRELAGLR 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1470 QKHEESQALLDASQKEVQALSTELLKLKNtYEESIVGQETLRRENKNLQEEISNLTNQVREGTknLTEMEKVKKLIEEEK 1549
Cdd:PRK03918 680 AELEELEKRREEIKKTLEKLKEELEEREK-AKKELEKLEKALERVEELREKVKKYKALLKERA--LSKVGEIASEIFEEL 756
|
..
gi 119600132 1550 TE 1551
Cdd:PRK03918 757 TE 758
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1021-1761 |
6.11e-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: 68.07 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1021 DLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKArmNCERELHKLEGNLKLNRESMENLeSSQRHLAEELRKKELELS 1100
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQ--VLEKELKHLREALQQTQQSHAYL-TQKREAQEEQLKKQQLLK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1101 QMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTrakmereradltqdladlnerleevggsslaqlEITKKQE 1180
Cdd:TIGR00618 264 QLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVT---------------------------------QIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1181 TKFQKLHRDMEEATLHFETTSASLKKRhadslAELEGQVENLQQVKQKLEKdksdLQLEVDDLLTRVEQMTRAKANaekl 1260
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKRAAHVKQQ-----SSIEEQRRLLQTLHSQEIH----IRDAHEVATSIREISCQQHTL---- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1261 ctlyEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQ---LEKETKS 1337
Cdd:TIGR00618 378 ----TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCaaaITCTAQC 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1338 QSALAHALQKAQRDcdlLREQYEEEQEVKaelhrTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEAAEAmG 1417
Cdd:TIGR00618 454 EKLEKIHLQESAQS---LKEREQQLQTKE-----QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNP-G 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1418 VANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLK 1497
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1498 ntyEESIVGQETLRRENKNLQEEISNLTNQVREGTKnltEMEKVKKLIEEEKTEVQVTLEETEGALERneskILHFQLEL 1577
Cdd:TIGR00618 605 ---EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQC---SQELALKLTALHALQLTLTQERVREHALS----IRVLPKEL 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1578 LEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLG- 1656
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARt 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1657 QLQIQIKDLQMQLDDST---QLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNT 1733
Cdd:TIGR00618 755 VLKARTEAHFNNNEEVTaalQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFL 834
|
730 740
....*....|....*....|....*...
gi 119600132 1734 SLLSQKKKLEADVARMQKEAEEVVQECQ 1761
Cdd:TIGR00618 835 SRLEEKSATLGEITHQLLKYEECSKQLA 862
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
946-1257 |
6.71e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 946 SELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHME 1025
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1026 EEKLSSLSKANLKLE-----QQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELS 1100
Cdd:TIGR02169 771 EEDLHKLEEALNDLEarlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1101 QMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLN---ERLEEVGGSSLAQLEITK 1177
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiEKKRKRLSELKAKLEALE 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1178 KQETKFQKLHRDMEE---ATLHFETTSASLKKRHADSLA----------ELEGQVENLQQVKQKLEKdksdLQLEVDDLL 1244
Cdd:TIGR02169 931 EELSEIEDPKGEDEEipeEELSLEDVQAELQRVEEEIRAlepvnmlaiqEYEEVLKRLDELKEKRAK----LEEERKAIL 1006
|
330
....*....|...
gi 119600132 1245 TRVEQMTRAKANA 1257
Cdd:TIGR02169 1007 ERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1618-1933 |
6.79e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1618 KSRIEVTRLK-KKMEEDLN-------EMELQLSCANRQVSEATKSLgQLQIQIKDLQMQLddstQLNSD--LKEQVAVAE 1687
Cdd:COG1196 171 KERKEEAERKlEATEENLErledilgELERQLEPLERQAEKAERYR-ELKEELKELEAEL----LLLKLreLEAELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1688 RRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKA 1767
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1768 KKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQIQKLESRVRELEGELEGEIRRSAE 1847
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1848 AQRGARRLERcIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEVKERAEVAES 1927
Cdd:COG1196 406 EEAEEALLER-LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
....*.
gi 119600132 1928 QVNKLK 1933
Cdd:COG1196 485 ELAEAA 490
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
864-1135 |
1.60e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.20 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 864 LKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSERVEEEEE 943
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 944 INSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLH 1023
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1024 MEEEKLSSLSKANLKLEQQVDELEGALEQ--ERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQ 1101
Cdd:TIGR04523 521 SLKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 119600132 1102 MNSKVENEKGLVAQLQKTV-------KELQTQIKDLKEKLE 1135
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELekakkenEKLSSIIKNIKSKKN 641
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1510-1945 |
2.64e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.43 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1510 LRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELE---- 1585
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnn 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1586 --------------RKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEA 1651
Cdd:TIGR04523 303 qkeqdwnkelkselKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1652 TKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQ 1731
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1732 NTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAE 1811
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1812 AEQMAL-MGSRKQIQKLESRVRelegELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRmqtQMDKLQLKVQNY 1890
Cdd:TIGR04523 543 LEDELNkDDFELKKENLEKEID----EKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK---EIEEKEKKISSL 615
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 119600132 1891 KQQVEVAETQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQE 1945
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKE 670
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1579-1820 |
4.66e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1579 EAKAELERKLSEKDEEIENfrrkqqctidsLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQL 1658
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAE-----------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1659 QIQIKDLQMQLDdstQLNSDLKEQVAVAERRNSllQSELEDLRSLQE--QTERGRRLSEEELLEATERINLFYTQNTSLL 1736
Cdd:COG4942 89 EKEIAELRAELE---AQKEELAELLRALYRLGR--QPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1737 SQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMA 1816
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
....
gi 119600132 1817 LMGS 1820
Cdd:COG4942 244 PAAG 247
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1456-1933 |
4.95e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 65.14 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1456 QKQLQSGKALADwKQKHEESQALLDAsQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNL 1535
Cdd:pfam15921 91 QRRLNESNELHE-KQKFYLRQSVIDL-QTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1536 -TEMEKVKKL------IEEEKTEVQVTLEETEGA--LERNESKILHFQlellEAKAELERKLSEKDEEIENFRRKQQCTI 1606
Cdd:pfam15921 169 nTQIEQLRKMmlshegVLQEIRSILVDFEEASGKkiYEHDSMSTMHFR----SLGSAISKILRELDTEISYLKGRIFPVE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1607 DSLQSsLDSEAKSRIEV--TRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDStqlNSDLKEQVA 1684
Cdd:pfam15921 245 DQLEA-LKSESQNKIELllQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ---NSMYMRQLS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1685 VAERRNSLLQSELEDLRSLQE----QTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEevVQEC 1760
Cdd:pfam15921 321 DLESTVSQLRSELREAKRMYEdkieELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS--LEKE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1761 QNAeekakkaaieaaNLSEELKKKQDTIAHLERTRE--NMEqtitdlqkrlaeaeqmalmgsrkqIQKLESRVRELEGEL 1838
Cdd:pfam15921 399 QNK------------RLWDRDTGNSITIDHLRRELDdrNME------------------------VQRLEALLKAMKSEC 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1839 EGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEV 1918
Cdd:pfam15921 443 QGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKL 522
|
490
....*....|....*
gi 119600132 1919 KERAEVAESQVNKLK 1933
Cdd:pfam15921 523 RSRVDLKLQELQHLK 537
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
883-1569 |
6.56e-10 |
|
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: 64.47 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 883 EELKAKQVSLTQEKNDLILQLQAEQETLANVEEQcewlIKSKIQLEARVKELSER-VEEEEEINSELTARGRKLEDECFE 961
Cdd:pfam12128 216 SRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQE----FNTLESAELRLSHLHFGyKSDETLIASRQEERQETSAELNQL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 962 LKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQ 1041
Cdd:pfam12128 292 LRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1042 QVDELEGALEQERKARmnCERELHKLEGNLKLNRES-----------MENLESSQRH-LAEELRKKELELSQMNSKVENE 1109
Cdd:pfam12128 372 DVTAKYNRRRSKIKEQ--NNRDIAGIKDKLAKIREArdrqlavaeddLQALESELREqLEAGKLEFNEEEYRLKSRLGEL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1110 KGLVAQLQKTvKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEvGGSSLAQLEI-TKKQETKFQKLHR 1188
Cdd:pfam12128 450 KLRLNQATAT-PELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQ-ASEALRQASRrLEERQSALDELEL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1189 DMEEAT---LHFETTSASLKKRHADSLAELE----------------GQVENLQQVKQKLEK-DKSDLQLEVDDLLTRVE 1248
Cdd:pfam12128 528 QLFPQAgtlLHFLRKEAPDWEQSIGKVISPEllhrtdldpevwdgsvGGELNLYGVKLDLKRiDVPEWAASEEELRERLD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1249 QMTRAKANAEKLCTLYEERLHEATAKLDKVtQLANDLAAQKTKlwsESGEFLRRL-EEKEALINQLSREKSNFTRQIEDL 1327
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELEKA-SREETFARTALK---NARLDLRRLfDEKQSEKDKKNKALAERKDSANER 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1328 RGQLEKETKsQSALAHALQKAQRDcDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLE-DAKKELA 1406
Cdd:pfam12128 684 LNSLEAQLK-QLDKKHQAWLEEQK-EQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALEtWYKRDLA 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1407 irlqeaaeAMGVANARNASLERARHqlqlELGDALSDLGKVRSAAARLDQKQLQSgkaladWKQKHEESQALLDASQKEV 1486
Cdd:pfam12128 762 --------SLGVDPDVIAKLKREIR----TLERKIERIAVRRQEVLRYFDWYQET------WLQRRPRLATQLSNIERAI 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1487 QALSTELLKLkntyeesivgQETLRRENKNLQEEISNLTNQVREGTKNLT----EMEKVKKLIEEEKTE-VQVTLEETEG 1561
Cdd:pfam12128 824 SELQQQLARL----------IADTKLRRAKLEMERKASEKQQVRLSENLRglrcEMSKLATLKEDANSEqAQGSIGERLA 893
|
....*...
gi 119600132 1562 ALERNESK 1569
Cdd:pfam12128 894 QLEDLKLK 901
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1026-1502 |
7.65e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 7.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1026 EEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNSK 1105
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1106 VENEkglvaQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQK 1185
Cdd:COG4717 132 QELE-----ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1186 LHRDMEEAtlhfettsaslkkrhadsLAELEGQVENLQQVKQKLEKDKSDLQLEvdDLLTRVEQMTRAKANAEKLCTLYE 1265
Cdd:COG4717 207 RLAELEEE------------------LEEAQEELEELEEELEQLENELEAAALE--ERLKEARLLLLIAAALLALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1266 ERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHAL 1345
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1346 QKAQRDCDLLREQYEE--EQEVKAELHRTLSKVNAEMV-QWRMKYENnvIQRTEDLEDAKKELAIRLQEAAEAMGVANAR 1422
Cdd:COG4717 347 EELQELLREAEELEEElqLEELEQEIAALLAEAGVEDEeELRAALEQ--AEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1423 N--ASLERARHQLQLELGDALSDLGKVRSAAARLDQ--KQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKN 1498
Cdd:COG4717 425 LdeEELEEELEELEEELEELEEELEELREELAELEAelEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
....
gi 119600132 1499 TYEE 1502
Cdd:COG4717 505 AREE 508
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
855-1266 |
8.33e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 855 SEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAeqetlanVEEQCEWLIKSKIQLEARVKel 934
Cdd:PRK02224 289 EELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA-------HNEEAESLREDADDLEERAE-- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 935 sERVEEEEEINSELTARGRKLED---ECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDI----SKLNRA 1007
Cdd:PRK02224 360 -ELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREaeleATLRTA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1008 AKVVQEA--------------------HQQTLDDlhmEEEKLSSLSKANLKLEQQVDELEGALEQERKARmNCERELHKL 1067
Cdd:PRK02224 439 RERVEEAealleagkcpecgqpvegspHVETIEE---DRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1068 EGNLKLNRESMENLESS---QRHLAEELRKKELEL-SQMNSKVE--NEKGLVAQ-LQKTVKELQTQIKDLKEKLEAERTT 1140
Cdd:PRK02224 515 EERREDLEELIAERRETieeKRERAEELRERAAELeAEAEEKREaaAEAEEEAEeAREEVAELNSKLAELKERIESLERI 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1141 RAKMErERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDMEEATLhfeTTSASLKKRHADSLAELEGQVE 1220
Cdd:PRK02224 595 RTLLA-AIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARI---EEAREDKERAEEYLEQVEEKLD 670
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 119600132 1221 NLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEE 1266
Cdd:PRK02224 671 ELREERDDLQAEIGAVENELEELEELRERREALENRVEALEALYDE 716
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1112-1504 |
8.35e-10 |
|
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: 64.20 E-value: 8.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1112 LVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQEtkfqklhrDME 1191
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQE--------DLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1192 EATLHFETTSASLKKRHaDSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRV---EQMTRAKANAEKLCTL----- 1263
Cdd:COG3096 358 ELTERLEEQEEVVEEAA-EQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiqyQQAVQALEKARALCGLpdltp 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1264 --YEERLHEATAKLDKVTQLANDLaAQKTKLWSES-GEFLRRLEEKEALINQLSREKSNFTRQiedlrgQLEKETKSQSA 1340
Cdd:COG3096 437 enAEDYLAAFRAKEQQATEEVLEL-EQKLSVADAArRQFEKAYELVCKIAGEVERSQAWQTAR------ELLRRYRSQQA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1341 LAHALQKAQRDCDLLREQYEEEQEVKAELHRtLSKvnaemvqwRMKYEnnvIQRTEDLEDAKKELAIRLQEAAEAMGVAN 1420
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQQQNAERLLEE-FCQ--------RIGQQ---LDAAEELEELLAELEAQLEELEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1421 ARNASLERARHQLQLELGdALSDLGKV-RSAAARLDQKQLQSGKALADWKQKHEESQALLDAsQKEVQALSTELLKLKNT 1499
Cdd:COG3096 578 EQRSELRQQLEQLRARIK-ELAARAPAwLAAQDALERLREQSGEALADSQEVTAAMQQLLER-EREATVERDELAARKQA 655
|
....*
gi 119600132 1500 YEESI 1504
Cdd:COG3096 656 LESQI 660
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
853-1259 |
1.16e-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: 63.50 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 853 KSSEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQ------EKNDLILQLQAEQETLANVEEQcEWLIKSKIQ 926
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkkikELEKQLNQLKSEISDLNNQKEQ-DWNKELKSE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 927 LEARVKELSERVEEEEEINSELTargrKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNR 1006
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIIS----QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1007 AAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLE---GNLKLNRESMEN--- 1080
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEliiKNLDNTRESLETqlk 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1081 -LESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLN 1159
Cdd:TIGR04523 472 vLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1160 ERLeevggsslaqleitKKQETKFQKLHRDMEEATLHFETTSaslkkrhadslaeLEGQVENLQQVKQKLEKDKSDLQLE 1239
Cdd:TIGR04523 552 FEL--------------KKENLEKEIDEKNKEIEELKQTQKS-------------LKKKQEEKQELIDQKEKEKKDLIKE 604
|
410 420
....*....|....*....|
gi 119600132 1240 VDDLLTRVEQMTRAKANAEK 1259
Cdd:TIGR04523 605 IEEKEKKISSLEKELEKAKK 624
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1089-1302 |
1.45e-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: 62.09 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1089 AEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGS 1168
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1169 SLAQLEITKKQETKFQKLHR-DMEEATLHFETTSASLKKRH---------ADSLAELEGQVENLQQVKQKLEKDKSDLQL 1238
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRqPPLALLLSPEDFLDAVRRLQylkylaparREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119600132 1239 EVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRR 1302
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
859-1338 |
2.19e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 859 EEVAGLKEECAQLQKALEKSEFQREELK-------AKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARV 931
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAeevrdlrERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 932 KELSERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNE---DISKLNRAA 1008
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgDAPVDLGNA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1009 KVVQEAHQQTLDDLHME----EEKLSSLSKANLKLEQQVDE---------LEG-----ALEQERKARMNCERELHKLEgn 1070
Cdd:PRK02224 411 EDFLEELREERDELREReaelEATLRTARERVEEAEALLEAgkcpecgqpVEGsphveTIEEDRERVEELEAELEDLE-- 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1071 lkLNRESMEN-LESsqrhlAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDL---KEKLEAE----RTTRA 1142
Cdd:PRK02224 489 --EEVEEVEErLER-----AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELrerAAELEAEaeekREAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1143 KMERERADLTQDLADLNERLEEVgGSSLAQLEITKKQETKFQKLHRDMEEatlhfettsasLKKRHADsLAELEGQVEnl 1222
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAEL-KERIESLERIRTLLAAIADAEDEIER-----------LREKREA-LAELNDERR-- 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1223 QQVKQKLEKdKSDLQLEVDDllTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKvtqLANDLAAQKTKLwsESGEFLRr 1302
Cdd:PRK02224 627 ERLAEKRER-KRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDD---LQAEIGAVENEL--EELEELR- 697
|
490 500 510
....*....|....*....|....*....|....*...
gi 119600132 1303 lEEKEALINQLSREKS--NFTRQIEDLRGQLEKETKSQ 1338
Cdd:PRK02224 698 -ERREALENRVEALEAlyDEAEELESMYGDLRAELRQR 734
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1511-1868 |
3.01e-09 |
|
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: 62.06 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1511 RRENKNLQEEISNLTNQ--VREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERKL 1588
Cdd:pfam17380 239 RKESFNLAEDVTTMTPEytVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1589 SEKdEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRL--KKKMEEDLNEMELQLSCanrqvsEATKSLGQLQIQIKDLQ 1666
Cdd:pfam17380 319 EEA-EKARQAEMDRQAAIYAEQERMAMERERELERIRQeeRKRELERIRQEEIAMEI------SRMRELERLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1667 MQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQT-ERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEAD 1745
Cdd:pfam17380 392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1746 VARMQKEAEEVVQECQNAEEKAKKAaieaanLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQ--MALMGSRKQ 1823
Cdd:pfam17380 472 RKRKKLELEKEKRDRKRAEEQRRKI------LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERrrEAEEERRKQ 545
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 119600132 1824 IQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEE 1868
Cdd:pfam17380 546 QEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
859-1404 |
3.06e-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: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 859 EEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSERV 938
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 939 EEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKV----------KNLTEEVEFLNEDISKLNRAA 1008
Cdd:TIGR04523 155 EKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlkkkiqknKSLESQISELKKQNNQLKDNI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1009 KVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLK-LNRESMEN----LES 1083
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdLNNQKEQDwnkeLKS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1084 SQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLE 1163
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1164 EVGGSSLAQLEITKKQETKFQKLHRDMEEatlhfettsasLKKRHADslaeLEGQVENLQQVKQKLEKDKSDLQLEVDDL 1243
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKEL-----------LEKEIER----LKETIIKNNSEIKDLTNQDSVKELIIKNL 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1244 LTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQ 1323
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1324 IEDLRGQLEK--ETKSQSALAHALQKAQRDCDLLREQYEE---EQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDL 1398
Cdd:TIGR04523 540 ISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSlkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL 619
|
....*.
gi 119600132 1399 EDAKKE 1404
Cdd:TIGR04523 620 EKAKKE 625
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
961-1601 |
1.59e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 961 ELKKEIDDLETMlvksEKEKRTTEHKVKNLTEEVEfLNEDISKLnRAAKVVQEAHQQTLDDLHmEEEKLSSLSKANLKLE 1040
Cdd:COG4913 229 ALVEHFDDLERA----HEALEDAREQIELLEPIRE-LAERYAAA-RERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1041 QQVDELEGALEQERKARMNCERELHKLEGNL-KLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKT 1119
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1120 VKELQTQIKDLKEKLEAERttrAKMERERADLTQDLADLNERLEEVggssLAQLEITKKQET----KFQKLHRDMEEATl 1195
Cdd:COG4913 382 FAALRAEAAALLEALEEEL---EALEEALAEAEAALRDLRRELREL----EAEIASLERRKSnipaRLLALRDALAEAL- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1196 hfettsaSLKKRHADSLAEL----------EGQVE---------------NLQQVKQKLE--KDKSDLQLEVDDLLTRVE 1248
Cdd:COG4913 454 -------GLDEAELPFVGELievrpeeerwRGAIErvlggfaltllvppeHYAAALRWVNrlHLRGRLVYERVRTGLPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1249 QMTRAKAN--AEKLctlyEERLHEATA-------------KLDKVTQLAN-DLAAQKTKLWSESGEF------------- 1299
Cdd:COG4913 527 ERPRLDPDslAGKL----DFKPHPFRAwleaelgrrfdyvCVDSPEELRRhPRAITRAGQVKGNGTRhekddrrrirsry 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1300 ------LRRLEEKEALINQLSREKSNFTRQIEDLRGQLEketksqsalahALQKAQRDCDLLREQYEEEQEVkAELHRTL 1373
Cdd:COG4913 603 vlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELD-----------ALQERREALQRLAEYSWDEIDV-ASAEREI 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1374 SKVNAEMvqwrmkyennviqrtEDLEDAKKELairlqeaaeamgvanarnASLERARHQLQLELGDALSDLGKVRSAAAR 1453
Cdd:COG4913 671 AELEAEL---------------ERLDASSDDL------------------AALEEQLEELEAELEELEEELDELKGEIGR 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1454 LDQKqlqsgkaLADWKQKHEESQALLDASQKEVQALSTELLklkNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTK 1533
Cdd:COG4913 718 LEKE-------LEQAEEELDELQDRLEAAEDLARLELRALL---EERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119600132 1534 NLTE-MEKVKKLIEEEKTEVQVTLEETEGALERneskilHFQLE---LLEAKAELERKLSE-KDEEIENFRRK 1601
Cdd:COG4913 788 ELERaMRAFNREWPAETADLDADLESLPEYLAL------LDRLEedgLPEYEERFKELLNEnSIEFVADLLSK 854
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1246-1933 |
1.82e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1246 RVEQMTRAKA--NAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSES--GEFLRRLEEkealinqlSREKSNFT 1321
Cdd:PTZ00121 1171 KAEDAKKAEAarKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAkkAEAVKKAEE--------AKKDAEEA 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1322 RQIEDLRGQLEKETKSQSALAH-----ALQKAQ--RDCDLLREQyeEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQR 1394
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHfarrqAAIKAEeaRKADELKKA--EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1395 TEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSDLGKVRSAaarldQKQLQSGKALADWKQKHEE 1474
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA-----KKKADAAKKKAEEKKKADE 1395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1475 SQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTevqv 1554
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK---- 1471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1555 TLEETEGALERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRKQQC-TIDSLQSSLDSEAKSRIEVTRLKKKMEED 1633
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAkKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1634 LNEMELQLSCANRQVSEATK-------SLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQE- 1705
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKaeedknmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEe 1631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1706 --QTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADvarmQKEAEEVVQEcqnaEEKAKKAAIEAANLSEELKK 1783
Cdd:PTZ00121 1632 kkKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED----KKKAEEAKKA----EEDEKKAAEALKKEAEEAKK 1703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1784 KQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLErciKELT 1863
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE---KEAV 1780
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1864 YQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEvAETQANQYLSKYKkqQHELNEVKERAEVAESQVNKLK 1933
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKIKDIFDNFANIIE-GGKEGNLVINDSK--EMEDSAIKEVADSKNMQLEEAD 1847
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1545-1923 |
2.07e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1545 IEEEKTEVQVTLEETEGALERNESKILHFQLelleakAELERKLSEKDEEIENF---RRKQQCTIDSLQSSLDSEAKSRI 1621
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDLHERL------NGLESELAELDEEIERYeeqREQARETRDEADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1622 EVTRLK---KKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDL--QMQLDDStqlnsdlkEQVAVAERRnsllqse 1696
Cdd:PRK02224 252 ELETLEaeiEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDA--------DAEAVEARR------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1697 lEDLRSLQEQTErgrrlseEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAAN 1776
Cdd:PRK02224 317 -EELEDRDEELR-------DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1777 LSEELKKKQDTIA-----------HLERTREN----------MEQTITDLQKRLAEAEQM-------------------- 1815
Cdd:PRK02224 389 LEEEIEELRERFGdapvdlgnaedFLEELREErdelrereaeLEATLRTARERVEEAEALleagkcpecgqpvegsphve 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1816 ALMGSRKQIQKLESR---VRELEGELEGEIRRSAEAQRGARRLERC----------IKELTYQAEEDKKNLSRMQTQMDK 1882
Cdd:PRK02224 469 TIEEDRERVEELEAEledLEEEVEEVEERLERAEDLVEAEDRIERLeerredleelIAERRETIEEKRERAEELRERAAE 548
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 119600132 1883 LQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEVKERAE 1923
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1007-1235 |
2.57e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1007 AAKVVQEAHQQTLDDLhmeEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQR 1086
Cdd:COG4942 17 AQADAAAEAEAELEQL---QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1087 HLAEELRKKELELS------QMNSKVENEKGLVAQ------------LQKTVKELQTQIKDLKEKLEAERTTRAKMERER 1148
Cdd:COG4942 94 ELRAELEAQKEELAellralYRLGRQPPLALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1149 ADLTQDLADLNERLEEvggssLAQLEitKKQETKFQKLHRDmeeatlhfettsaslKKRHADSLAELEGQVENLQQVKQK 1228
Cdd:COG4942 174 AELEALLAELEEERAA-----LEALK--AERQKLLARLEKE---------------LAELAAELAELQQEAEELEALIAR 231
|
....*..
gi 119600132 1229 LEKDKSD 1235
Cdd:COG4942 232 LEAEAAA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1186-1827 |
3.17e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1186 LHRDMEEAtlhfettsaslkKRHADSLAELEGQVENLQQVKQKLEkdksdlqlEVDDLLTRVEQMTRAKANAeklctLYE 1265
Cdd:COG4913 240 AHEALEDA------------REQIELLEPIRELAERYAAARERLA--------ELEYLRAALRLWFAQRRLE-----LLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1266 ERLHEATAKLDKVTQLANDLAAQKTKLwsesgeflrrLEEKEALINQLSrekSNFTRQIEDLRGQLEKETKSQSALAHAL 1345
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDAL----------REELDELEAQIR---GNGGDRLEQLEREIERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1346 QKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEAAEAMGVANARNAS 1425
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1426 LERARHQLQLELGDALSDL---------------------GKVRSAAARL--DQKQLqsgKALADW----KQKH------ 1472
Cdd:COG4913 442 LLALRDALAEALGLDEAELpfvgelievrpeeerwrgaieRVLGGFALTLlvPPEHY---AAALRWvnrlHLRGrlvyer 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1473 -EESQALLDASQKEVQALSTELLKLKNTYE---ESIVGQ----------ETLRRENKNLQEE--IS--------NLTNQV 1528
Cdd:COG4913 519 vRTGLPDPERPRLDPDSLAGKLDFKPHPFRawlEAELGRrfdyvcvdspEELRRHPRAITRAgqVKgngtrhekDDRRRI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1529 RE----GTKNLtemEKVKKLiEEEKTEVQVTLEETEGALERNESkilhfQLELLEAKAELERKLSEKDEEIENFRRKQQc 1604
Cdd:COG4913 599 RSryvlGFDNR---AKLAAL-EAELAELEEELAEAEERLEALEA-----ELDALQERREALQRLAEYSWDEIDVASAER- 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1605 TIDSLQSSLDSEAKSRIEVTRLKKKMEE---DLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDD-----STQLN 1676
Cdd:COG4913 669 EIAELEAELERLDASSDDLAALEEQLEEleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedlaRLELR 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1677 SDLKEQVAVAERRNSlLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSqkkkleADVArmqkEAEEV 1756
Cdd:COG4913 749 ALLEERFAAALGDAV-ERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLD------ADLE----SLPEY 817
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119600132 1757 VQECQNAEekakkaaieaanlSEELKKKQDTIAhlERTRENMEQTITDLQKRLAEAEQMAlmgsRKQIQKL 1827
Cdd:COG4913 818 LALLDRLE-------------EDGLPEYEERFK--ELLNENSIEFVADLLSKLRRAIREI----KERIDPL 869
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1266-1895 |
3.38e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1266 ERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKetksqsalahaL 1345
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK-----------L 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1346 QKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRmKYENNVIQRTEDLEDAKKELAiRLQEAAEAMGVANARNAS 1425
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE-ERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1426 LERARHQLQLELGD----------ALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLdASQKEVQALSTELL- 1494
Cdd:PRK03918 305 YLDELREIEKRLSRleeeingieeRIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTg 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1495 ----KLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVqvTLEETEGALERNESKI 1570
Cdd:PRK03918 384 ltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL--TEEHRKELLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1571 LHFQLELLEAKaELERKLSEKDEEIENFRRKQqctidslqssldSEAKSRIEVTRLKKKMEEDLNEMELQ-LSCANRQVS 1649
Cdd:PRK03918 462 KRIEKELKEIE-EKERKLRKELRELEKVLKKE------------SELIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1650 EATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEqvavAERRNSLLQSELEDLrsLQEQTERGRRlSEEELLEATERINLFY 1729
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELAEL--LKELEELGFE-SVEELEERLKELEPFY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1730 TQNTSLLSQKKKLEADVARMQKEAEEvvqecqnaeekakkaaieaanlseelkkkqdtiahLERTRENMEQTITDLQKRL 1809
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEEE-----------------------------------LDKAFEELAETEKRLEELR 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1810 AEAEQMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKK------NLSRMQTQMDKL 1883
Cdd:PRK03918 647 KELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKakkeleKLEKALERVEEL 726
|
650
....*....|..
gi 119600132 1884 QLKVQNYKQQVE 1895
Cdd:PRK03918 727 REKVKKYKALLK 738
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
853-1223 |
3.64e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 853 KSSEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVK 932
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 933 ELSERVEEeeeiNSELTARGRKLE-----------DECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDI 1001
Cdd:PRK02224 437 TARERVEE----AEALLEAGKCPEcgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1002 SKLNRAAKVVQ--EAHQQTLDDlhmEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESME 1079
Cdd:PRK02224 513 RLEERREDLEEliAERRETIEE---KRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1080 NLESSqRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERA-----DLTQD 1154
Cdd:PRK02224 590 SLERI-RTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAeeyleQVEEK 668
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119600132 1155 LADLNER----LEEVGG--SSLAQLEITKKQETKFQKLHRDMEeaTLHFETTsaSLKKRHADSLAELEGQ-VENLQ 1223
Cdd:PRK02224 669 LDELREErddlQAEIGAveNELEELEELRERREALENRVEALE--ALYDEAE--ELESMYGDLRAELRQRnVETLE 740
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1091-1298 |
5.25e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1091 ELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEE------ 1164
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1165 VGGSSLAQLE--------------------ITKKQETKFQKLHRDMEEAtlhfettsASLKKRHADSLAELEGQVENLQQ 1224
Cdd:COG3883 97 RSGGSVSYLDvllgsesfsdfldrlsalskIADADADLLEELKADKAEL--------EAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119600132 1225 VKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGE 1298
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
986-1193 |
7.06e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 986 KVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELH 1065
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1066 KLEGNL--------KLNRESMENLESSQRHLAEELRKKELelsqMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAE 1137
Cdd:COG4942 101 AQKEELaellralyRLGRQPPLALLLSPEDFLDAVRRLQY----LKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 119600132 1138 RTTRAKMERERADLTQDLADLNERLEEVGG---SSLAQLEITKKQETKFQKLHRDMEEA 1193
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKelaELAAELAELQQEAEELEALIARLEAE 235
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
859-1285 |
7.78e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 7.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 859 EEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDL--ILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSE 936
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 937 RVEEEEEINSELTARGRKLEDEC----FELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQ 1012
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1013 EAHQ-----------------QTLDDLHMEEEK----------------LSSLSKANLKLEQQVDELEGALEQERKARMN 1059
Cdd:COG4717 241 LEERlkearlllliaaallalLGLGGSLLSLILtiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1060 CERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQmnskvenekglvAQLQKTVKELQTQIKDLKEKLEAERT 1139
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE------------LQLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1140 TRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQ--ETKFQKLHRDMEEAtlhfettsASLKKRHADSLAELEG 1217
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEEL--------EEELEELREELAELEA 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119600132 1218 QVENLQQvkqklEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEAT-AKLDKVTQLANDL 1285
Cdd:COG4717 461 ELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYReERLPPVLERASEY 524
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1627-1854 |
9.51e-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: 56.31 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1627 KKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLR-SLQE 1705
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRaELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1706 QTER-GRRLSEEELLEATERINLFYTQNTSLLSQK--KKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELK 1782
Cdd:COG4942 102 QKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119600132 1783 KKQDTIAHLERTRENMEQTITDLQKRLAEAEQmALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARR 1854
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAA-ELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
865-1516 |
1.31e-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: 56.90 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 865 KEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQcEWLIKSKIQLEARVKELSERVEEEEEI 944
Cdd:TIGR00618 292 AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-RRLLQTLHSQEIHIRDAHEVATSIREI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 945 NS---ELTARGRKLEDEcfelkKEIDDLETMLVKSEKEKRTTE-HKVKNLTEEVEFLNEDISKLN-------RAAKVVQE 1013
Cdd:TIGR00618 371 SCqqhTLTQHIHTLQQQ-----KTTLTQKLQSLCKELDILQREqATIDTRTSAFRDLQGQLAHAKkqqelqqRYAELCAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1014 AHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQerkarmncERELHKLEGNLKlnresmENLESSQRHLAEELR 1093
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ--------ETRKKAVVLARL------LELQEEPCPLCGSCI 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1094 KKELELSQMNSKVENEKgLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGgsslAQL 1173
Cdd:TIGR00618 512 HPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK----EDI 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1174 EITKKQETKFQKL--HRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEvddlLTRVEQMT 1251
Cdd:TIGR00618 587 PNLQNITVRLQDLteKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT----LTQERVRE 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1252 RAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLwsesgEFLRRLEEKEALINQLSREKSNFTR-QIEDLRGQ 1330
Cdd:TIGR00618 663 HALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQ-----TLLRELETHIEEYDREFNEIENASSsLGSDLAAR 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1331 LEketksqsALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQ 1410
Cdd:TIGR00618 738 ED-------ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQ 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1411 EAAEAMGVANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALS 1490
Cdd:TIGR00618 811 EIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDG 890
|
650 660 670
....*....|....*....|....*....|....*...
gi 119600132 1491 TELLK------------LKNTYEESIVGQETLRRENKN 1516
Cdd:TIGR00618 891 DALIKflheitlyanvrLANQSEGRFHGRYADSHVNAR 928
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1039-1278 |
1.59e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1039 LEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRH--LAEELRKKELELSQmnskVENEKGLVAQL 1116
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELER----LDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1117 QKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSS-----------LAQLEITKKQETKFQK 1185
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelralleerFAAALGDAVERELREN 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1186 LHRDMEEATLHFETTSASL-------KKRHADSLAELEGQVENLQQVKQKLEkdksdlQLEVDDLLTRVEQMTRAKANAE 1258
Cdd:COG4913 771 LEERIDALRARLNRAEEELeramrafNREWPAETADLDADLESLPEYLALLD------RLEEDGLPEYEERFKELLNENS 844
|
250 260
....*....|....*....|....*
gi 119600132 1259 K-----LCTLYEERLHEATAKLDKV 1278
Cdd:COG4913 845 IefvadLLSKLRRAIREIKERIDPL 869
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
853-1242 |
1.64e-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: 56.61 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 853 KSSEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVK 932
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 933 ELSERveeeeeinsELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISklnraakvvq 1012
Cdd:TIGR02169 790 HSRIP---------EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK---------- 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1013 eahqqtlddlhMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEgnlklnrESMENLESSQRHLAEEL 1092
Cdd:TIGR02169 851 -----------SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE-------AQLRELERKIEELEAQI 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1093 RKKELELSQMNSKVENEKGLVAQLQKTVKELQtqiKDLKEKLEAErttraKMERERADLTQDLadlnERLEEVGGSSLAQ 1172
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEIEDPKGEDE---EIPEEELSLE-----DVQAELQRVEEEI----RALEPVNMLAIQE 980
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119600132 1173 LEITKKQETKFQ-KLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDD 1242
Cdd:TIGR02169 981 YEEVLKRLDELKeKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELSGGTGELILENPD 1051
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1061-1259 |
1.87e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1061 ERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTT 1140
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1141 RAKM--------ERERADL---TQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDMEEATLHFETTSAsLKKRHA 1209
Cdd:COG4942 106 LAELlralyrlgRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA-LLAELE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 119600132 1210 DSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEK 1259
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1318-1724 |
2.19e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.50 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1318 SNFTRQIEDLRGQLEKETKSQSALAHA---LQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEM--VQWRMKYENNVI 1392
Cdd:PRK04863 272 ADYMRHANERRVHLEEALELRRELYTSrrqLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlVQTALRQQEKIE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1393 QRTEDLEdakkELAIRLQEAAEAMGVANARNASLERarhqlqlelgdalsdlgkvRSAAARLDQKQLQSGkaLADWKQKH 1472
Cdd:PRK04863 352 RYQADLE----ELEERLEEQNEVVEEADEQQEENEA-------------------RAEAAEEEVDELKSQ--LADYQQAL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1473 EESQALLDASQKEVQAL--STELLKLKNTYEESIVG-QETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLI---- 1545
Cdd:PRK04863 407 DVQQTRAIQYQQAVQALerAKQLCGLPDLTADNAEDwLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVrkia 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1546 -EEEKTEVQVTLEETEGALErnESKILHFQLELLEAK-AELERKLSEKDEEIENFRRKQQctidSLQSSLDSEAksriEV 1623
Cdd:PRK04863 487 gEVSRSEAWDVARELLRRLR--EQRHLAEQLQQLRMRlSELEQRLRQQQRAERLLAEFCK----RLGKNLDDED----EL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1624 TRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQ------MQLDDS-TQLNSDLKEQVAVAERRNSLLQSE 1696
Cdd:PRK04863 557 EQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAarapawLAAQDAlARLREQSGEEFEDSQDVTEYMQQL 636
|
410 420
....*....|....*....|....*...
gi 119600132 1697 LEDLRSLQEQTERGRRlSEEELLEATER 1724
Cdd:PRK04863 637 LERERELTVERDELAA-RKQALDEEIER 663
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
980-1195 |
2.22e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 980 KRTTEHKVKNLTEEVEFLNEdisKLNRAAKVVQEAhQQTLDDLhMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMN 1059
Cdd:COG3206 163 EQNLELRREEARKALEFLEE---QLPELRKELEEA-EAALEEF-RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1060 CERELHKLEGNLKLNRESMENLESSQ--RHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAE 1137
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119600132 1138 -RTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETK---FQKLHRDMEEATL 1195
Cdd:COG3206 318 lEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVArelYESLLQRLEEARL 379
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1082-1250 |
2.69e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.78 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1082 ESSQRHLaEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNER 1161
Cdd:COG1579 3 PEDLRAL-LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1162 LEEVggSSLAQLEITKKQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVD 1241
Cdd:COG1579 82 LGNV--RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
....*....
gi 119600132 1242 DLLTRVEQM 1250
Cdd:COG1579 160 ELEAEREEL 168
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1327-1727 |
4.02e-07 |
|
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: 55.34 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1327 LRGQLEKETKSQSALAhaLQKAQRDCdllREQYEEEQEVKAELHRTLSKVNA----------------EMVQWRMKYENN 1390
Cdd:COG3096 274 MRHANERRELSERALE--LRRELFGA---RRQLAEEQYRLVEMARELEELSAresdleqdyqaasdhlNLVQTALRQQEK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1391 VIQRTEDLEdakkELAIRLQEAAEAmgvanARNASLERARHQLQLElgdalsdlgkvrsaAARLDQKQLQSGkaLADWKQ 1470
Cdd:COG3096 349 IERYQEDLE----ELTERLEEQEEV-----VEEAAEQLAEAEARLE--------------AAEEEVDSLKSQ--LADYQQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1471 KHEESQALLDASQKEVQAL--STELLKLKNTYEESIVG-QETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEE 1547
Cdd:COG3096 404 ALDVQQTRAIQYQQAVQALekARALCGLPDLTPENAEDyLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1548 EKTEVqvtleETEGALER--------NESKILHFQLELLEAK-AELERKLSEKdeeiENFRRKQQctidSLQSSLDSEAK 1618
Cdd:COG3096 484 IAGEV-----ERSQAWQTarellrryRSQQALAQRLQQLRAQlAELEQRLRQQ----QNAERLLE----EFCQRIGQQLD 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1619 SRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQ----LDDSTQLNSdLKEQVAVAerrnsllq 1694
Cdd:COG3096 551 AAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawLAAQDALER-LREQSGEA-------- 621
|
410 420 430
....*....|....*....|....*....|....*....
gi 119600132 1695 seLEDLRSLQE------QTERGRRLSEEELLEATERINL 1727
Cdd:COG3096 622 --LADSQEVTAamqqllEREREATVERDELAARKQALES 658
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
954-1545 |
4.27e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.29 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 954 KLEDECFELKKEIDDLE---TMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEE--- 1027
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRaeiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSaln 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1028 KLSSLSKANLKLEQQVDELEGALEQErkarmncERELHKLEGnlkLNRESMENLESSQRHLAEELRKKELELSQMNSKVE 1107
Cdd:PRK01156 243 ELSSLEDMKNRYESEIKTAESDLSME-------LEKNNYYKE---LEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1108 NEKGLVAQLQKtvkeLQTQIKDLKEkLEAERTTRAKMERERADLTQDLADLNERlEEVGGSSLAQLEITKKQETKFQKLH 1187
Cdd:PRK01156 313 ILSNIDAEINK----YHAIIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELEGY-EMDYNSYLKSIESLKKKIEEYSKNI 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1188 RDM----EEATLHFETTSASLKKRHAD---SLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTR----VEQMTRAKAN 1256
Cdd:PRK01156 387 ERMsafiSEILKIQEIDPDAIKKELNEinvKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpVCGTTLGEEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1257 AEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSesgeFLRRLEEKEAlinqlsREKSNFTRQIEDLRGQLEKETK 1336
Cdd:PRK01156 467 SNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKK----RKEYLESEEI------NKSINEYNKIESARADLEDIKI 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1337 SQSALAHALQKAQR--------DCDLLREQYEEEQEVKAELhrtlSKVNAEMVQWRmkyENNVIQRTEDLEDAKKELAIR 1408
Cdd:PRK01156 537 KINELKDKHDKYEEiknrykslKLEDLDSKRTSWLNALAVI----SLIDIETNRSR---SNEIKKQLNDLESRLQEIEIG 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1409 LQEaaeamgVANARNASLERARHQLQLeLGDALSDLGKVRSAAARLdQKQLQSGKALADWKQKHEESQALLDASQKEVQa 1488
Cdd:PRK01156 610 FPD------DKSYIDKSIREIENEANN-LNNKYNEIQENKILIEKL-RGKIDNYKKQIAEIDSIIPDLKEITSRINDIE- 680
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 119600132 1489 lsTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLI 1545
Cdd:PRK01156 681 --DNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1261-1946 |
4.30e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1261 CTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEalINQLSREKSNFTR-----QIEDLRG------ 1329
Cdd:PTZ00121 1000 CVIDKENHFSFTALTANTIDFNQNFNIEKIEELTEYGNNDDVLKEKD--IIDEDIDGNHEGKaeakaHVGQDEGlkpsyk 1077
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1330 ----QLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVqwRMKYENNVIQRTEDLEDAKK-E 1404
Cdd:PTZ00121 1078 dfdfDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEA--RKAEDARKAEEARKAEDAKRvE 1155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1405 LAIRLQEAAEAMGVANARNAS-LERARHQLQLELGDALSDLGKVRSA-AARLDQKQLQSGKAL-ADWKQKHEESQALLDA 1481
Cdd:PTZ00121 1156 IARKAEDARKAEEARKAEDAKkAEAARKAEEVRKAEELRKAEDARKAeAARKAEEERKAEEARkAEDAKKAEAVKKAEEA 1235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1482 SQKEVQALSTEllKLKNTYE----ESIVGQETLRRENKNLQEEisnltnqvREGTKNLTEMEKVKKLIEEEKTEVQVTLE 1557
Cdd:PTZ00121 1236 KKDAEEAKKAE--EERNNEEirkfEEARMAHFARRQAAIKAEE--------ARKADELKKAEEKKKADEAKKAEEKKKAD 1305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1558 ETEG-ALERNESKILHFQLELLEAKAE-LERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLN 1635
Cdd:PTZ00121 1306 EAKKkAEEAKKADEAKKKAEEAKKKADaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1636 EMElqlscANRQVSEATKSLGQLQIQIKDLQMQldDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERG--RRL 1713
Cdd:PTZ00121 1386 KAE-----EKKKADEAKKKAEEDKKKADELKKA--AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAeeAKK 1458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1714 SEEELLEATERinlfytQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLER 1793
Cdd:PTZ00121 1459 AEEAKKKAEEA------KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1794 TRENMEQTITDLQKRLAEAEQMALMGSRKQIQKLESRvRELEGELEGEIRRSAEAQRGArrlERCIKELTYQAEEDKKNL 1873
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA-KKAEEDKNMALRKAEEAKKAE---EARIEEVMKLYEEEKKMK 1608
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119600132 1874 SRMQTQMDKLQLKVQNYKQQVEVAEtqanqylsKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQEE 1946
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKK--------KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1301-1928 |
6.59e-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: 6.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1301 RRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSAlahALQKAQRDCDLLREQYEEEQEVKAELHrtlsKVNAEM 1380
Cdd:pfam12128 276 SRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADA---AVAKDRSELEALEDQHGAFLDADIETA----AADQEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1381 V-QWRMKYENnVIQRTEDLEDAKKELAIRLQEAAEAMGVANAR-----NASLERARHQLQLELGDALSDLGKVRSAAarl 1454
Cdd:pfam12128 349 LpSWQSELEN-LEERLKALTGKHQDVTAKYNRRRSKIKEQNNRdiagiKDKLAKIREARDRQLAVAEDDLQALESEL--- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1455 dQKQLQSGKA-LADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKnlqeEISNLTNQVREGTK 1533
Cdd:pfam12128 425 -REQLEAGKLeFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANA----EVERLQSELRQARK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1534 NLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHF----------QLELLEAKAELERklSEKDEEIENFRRKQQ 1603
Cdd:pfam12128 500 RRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFlrkeapdweqSIGKVISPELLHR--TDLDPEVWDGSVGGE 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1604 CTIDSLQssLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQL--NSDLKE 1681
Cdd:pfam12128 578 LNLYGVK--LDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTAlkNARLDL 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1682 QVAVAERRNSLLQseledlrsLQEQTERGRRLSEEEL--LEATERINLFYTQNTSLLSQKKKLEADVARMQK----EAEE 1755
Cdd:pfam12128 656 RRLFDEKQSEKDK--------KNKALAERKDSANERLnsLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYwqvvEGAL 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1756 VVQECQNAEEKAKKAAIEAANLSE-------ELKKK---QDTIAHLERTRENMEQTITDLQKRLAEAEQMalmgsRKQIQ 1825
Cdd:pfam12128 728 DAQLALLKAAIAARRSGAKAELKAletwykrDLASLgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRY-----FDWYQ 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1826 KLESRVRELEGELEGEIRRSAEAQRGarrlercikELTYQAEEDKKNLSRMQTQMDKLQlkvqnyKQQVEVAETqanqyL 1905
Cdd:pfam12128 803 ETWLQRRPRLATQLSNIERAISELQQ---------QLARLIADTKLRRAKLEMERKASE------KQQVRLSEN-----L 862
|
650 660
....*....|....*....|...
gi 119600132 1906 SKYKKQQHELNEVKERAEVAESQ 1928
Cdd:pfam12128 863 RGLRCEMSKLATLKEDANSEQAQ 885
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
864-1163 |
6.99e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.36 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 864 LKEECAQLQKALEKSEFQREELKAKQVSLTQEKndlilQLQAEQETLAnVEEQCEWlikSKIQLEARVKELSERVEEEEE 943
Cdd:pfam17380 301 LRQEKEEKAREVERRRKLEEAEKARQAEMDRQA-----AIYAEQERMA-MEREREL---ERIRQEERKRELERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 944 INSEltaRGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEveflnedISKLNRAAKVVQEAHQQTLDDLH 1023
Cdd:pfam17380 372 MEIS---RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQ-------KVEMEQIRAEQEEARQREVRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1024 MEEEK-LSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMEN-LESSQRHLAEELRK-----KE 1096
Cdd:pfam17380 442 EERAReMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKeLEERKQAMIEEERKrklleKE 521
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119600132 1097 LELSQMNSKVENEKGLVAQLQKTVKELQT--QIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLE 1163
Cdd:pfam17380 522 MEERQKAIYEEERRREAEEERRKQQEMEErrRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1602-1815 |
8.11e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1602 QQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLddstqlnSDLKE 1681
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------AELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1682 QVAVAERRNSLLQSELED-LRSLQEQTERGR---RLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVV 1757
Cdd:COG4942 91 EIAELRAELEAQKEELAElLRALYRLGRQPPlalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 119600132 1758 QECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQM 1815
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1117-1368 |
8.47e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 8.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1117 QKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVggsslaqleitkkqetkfQKLHRDMEEATLH 1196
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL------------------ARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1197 FETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEvddLLTRVEQMTRAKANAEKLCTLYEERLheatAKLD 1276
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLA---LLLSPEDFLDAVRRLQYLKYLAPARR----EQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1277 KVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSnftrQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLR 1356
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|..
gi 119600132 1357 EQYEEEQEVKAE 1368
Cdd:COG4942 230 ARLEAEAAAAAE 241
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1337-1706 |
9.54e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.15 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1337 SQSALAHALQKA--------QRDCDLLREQYEEEQEVKA---ELHRTLS------KVNAEMVQwrmkYENNVIQRTEDLE 1399
Cdd:PRK11281 22 LSSAFARAASNGdlpteadvQAQLDALNKQKLLEAEDKLvqqDLEQTLAlldkidRQKEETEQ----LKQQLAQAPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1400 DAKKELAiRLQEAAEAMGVANARNASLErarhQLQLELGDALSDLGKVRSAAARLDQKqlqsgkaLADWKQKHEESQALL 1479
Cdd:PRK11281 98 QAQAELE-ALKDDNDEETRETLSTLSLR----QLESRLAQTLDQLQNAQNDLAEYNSQ-------LVSLQTQPERAQAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1480 DASQKEVQALSTELLKLKntyeesiVGQETLRRENKN-LQEEISNLTNQVREGTKNLtemekvkklieEEKTEVQVTLEE 1558
Cdd:PRK11281 166 YANSQRLQQIRNLLKGGK-------VGGKALRPSQRVlLQAEQALLNAQNDLQRKSL-----------EGNTQLQDLLQK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1559 tegalerneskilhfQLELLEAK-AELERKLSEKDEEIENFRRKQ-QCTIDSLQSSldsEAKSRIEVTRLKKKmEEDLNe 1636
Cdd:PRK11281 228 ---------------QRDYLTARiQRLEHQLQLLQEAINSKRLTLsEKTVQEAQSQ---DEAARIQANPLVAQ-ELEIN- 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1637 meLQLSCANRQVSEATKSLGQLQIQIKDlqmQLDDSTQLNSDLKEQVAVAerRNSLLQSeledlRSLQEQ 1706
Cdd:PRK11281 288 --LQLSQRLLKATEKLNTLTQQNLRVKN---WLDRLTQSERNIKEQISVL--KGSLLLS-----RILYQQ 345
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1096-1340 |
1.02e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1096 ELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEvggsslaqlei 1175
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1176 tkkQETKFQKLHRDMEEATLHFETTSASLKkrhADSLAELEGQVENLQQV----KQKLEKDKSDlQLEVDDLLTRVEQmt 1251
Cdd:COG3883 84 ---RREELGERARALYRSGGSVSYLDVLLG---SESFSDFLDRLSALSKIadadADLLEELKAD-KAELEAKKAELEA-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1252 rAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQL 1331
Cdd:COG3883 155 -KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
....*....
gi 119600132 1332 EKETKSQSA 1340
Cdd:COG3883 234 AAAAAAAAA 242
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1067-1927 |
1.08e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1067 LEGNLKLNRESMENLESSQRHlaEELRKKELELSQMNS-----KVENEK----GLVAQLQKTVKELQTQIKDLKEKLEAE 1137
Cdd:PRK04863 235 MEAALRENRMTLEAIRVTQSD--RDLFKHLITESTNYVaadymRHANERrvhlEEALELRRELYTSRRQLAAEQYRLVEM 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1138 RTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQEtkfqklhrDMEEATLHFETtSASLKKRHADSLAELEG 1217
Cdd:PRK04863 313 ARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQA--------DLEELEERLEE-QNEVVEEADEQQEENEA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1218 QVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKA---NAEKLCTL-------YEERLHEATAKLDKVTQLANDLA- 1286
Cdd:PRK04863 384 RAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQaleRAKQLCGLpdltadnAEDWLEEFQAKEQEATEELLSLEq 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1287 ------------AQKTKL-------------WSESGEFLRRLEEKEALINQLSREKsnftRQIEDLRGQLEKETKSQSAL 1341
Cdd:PRK04863 464 klsvaqaahsqfEQAYQLvrkiagevsrseaWDVARELLRRLREQRHLAEQLQQLR----MRLSELEQRLRQQQRAERLL 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1342 AHALQKAQRDCDL--LREQYEEEQEVKAElhrTLSKVNAEMVQWRMkyennviqrteDLEDAKKELAIRLQeaaeamgva 1419
Cdd:PRK04863 540 AEFCKRLGKNLDDedELEQLQEELEARLE---SLSESVSEARERRM-----------ALRQQLEQLQARIQ--------- 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1420 naRNASLERARHQLQlelgDALSDLGKvrsaaarldqkqlQSGKALADwkqkheesqalldaSQKEVQALSTELLKLKNT 1499
Cdd:PRK04863 597 --RLAARAPAWLAAQ----DALARLRE-------------QSGEEFED--------------SQDVTEYMQQLLEREREL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1500 YEESivgqETLRRENKNLQEEISNLTNqvREGTknltEMEKVKKLIE----EEKTEV--QVTLEE---TEGALERNESKI 1570
Cdd:PRK04863 644 TVER----DELAARKQALDEEIERLSQ--PGGS----EDPRLNALAErfggVLLSEIydDVSLEDapyFSALYGPARHAI 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1571 LHFQLELLEAK----------------------------AELER----KLSEKDEEIENF-------RRKQQCTIDSLQS 1611
Cdd:PRK04863 714 VVPDLSDAAEQlagledcpedlyliegdpdsfddsvfsvEELEKavvvKIADRQWRYSRFpevplfgRAAREKRIEQLRA 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1612 SLDSE----AKSRIEVTRLKKkMEEDLNEM-------------ELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDdstq 1674
Cdd:PRK04863 794 EREELaeryATLSFDVQKLQR-LHQAFSRFigshlavafeadpEAELRQLNRRRVELERALADHESQEQQQRSQLE---- 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1675 lnsDLKEQVavaerrnSLLQsELEDLRSLQEQTERGRRLSE-EELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEA 1753
Cdd:PRK04863 869 ---QAKEGL-------SALN-RLLPRLNLLADETLADRVEEiREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQF 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1754 EEVVQECQNAEEKAKKAAIEAANLSEELKKK-----QDTIAHLERTRENMEQtitdLQKRLAEAEQMALMgSRKQIQKLE 1828
Cdd:PRK04863 938 EQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEMLAKNSDLNEK----LRQRLEQAEQERTR-AREQLRQAQ 1012
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1829 SRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKnlSRMQTQMDKLQlkvqnykQQVEVAETQANQYLSKY 1908
Cdd:PRK04863 1013 AQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAE--ERARARRDELH-------ARLSANRSRRNQLEKQL 1083
|
970
....*....|....*....
gi 119600132 1909 KKQQHELNEVKERAEVAES 1927
Cdd:PRK04863 1084 TFCEAEMDNLTKKLRKLER 1102
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
861-1215 |
1.24e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 861 VAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDL--ILQLQAEQETLANVEEQCEwlikskiQLEARVKELSERv 938
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIA-------ELEAELERLDAS- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 939 eeeeeiNSELTARGRKLEdecfELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEdisKLNRAAKVVQEAHQQT 1018
Cdd:COG4913 684 ------SDDLAALEEQLE----ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD---RLEAAEDLARLELRAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1019 LDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLN-RESMENLESSQRHLaEELRKKEL 1097
Cdd:COG4913 751 LEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADlDADLESLPEYLALL-DRLEEDGL 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1098 ElsqmnskvenekglvaqlqktvkELQTQIKDLKEKLEAERTTR--AKMERERADLTQDLADLNERLEEV---GGSSLaQ 1172
Cdd:COG4913 830 P-----------------------EYEERFKELLNENSIEFVADllSKLRRAIREIKERIDPLNDSLKRIpfgPGRYL-R 885
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 119600132 1173 LEITKKQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAEL 1215
Cdd:COG4913 886 LEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRL 928
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
974-1172 |
1.47e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 974 VKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQE 1053
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1054 RKARMNCERELHKLE-----GNLK--LNR-ESMENLESSQRHLAEELRKKELELSQMNSKVENEKG----LVAQLQKTVK 1121
Cdd:COG3883 92 ARALYRSGGSVSYLDvllgsESFSdfLDRlSALSKIADADADLLEELKADKAELEAKKAELEAKLAeleaLKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 119600132 1122 ELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQ 1172
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1287-1946 |
1.57e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.19 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1287 AQKTKLWSESGEFLRR-----LEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLRE---- 1357
Cdd:pfam05483 87 AEKIKKWKVSIEAELKqkenkLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKEtcar 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1358 ------QYEEEQEVKAELHRTLSKVNAEMVqwrMKYENNVIQRtedlEDAKKELAIRLQEAAEAMG-VANARNASLERAR 1430
Cdd:pfam05483 167 saektkKYEYEREETRQVYMDLNNNIEKMI---LAFEELRVQA----ENARLEMHFKLKEDHEKIQhLEEEYKKEINDKE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1431 HQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEEsqalLDASQKEVQALSTELLKLKNTYEESIVGQETL 1510
Cdd:pfam05483 240 KQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEN----LKELIEKKDHLTKELEDIKMSLQRSMSTQKAL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1511 RRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEE----TEGALERNESKILHFQLELLEAKAELEr 1586
Cdd:pfam05483 316 EEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEllrtEQQRLEKNEDQLKIITMELQKKSSELE- 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1587 klsekdeEIENFRRKQQCTIDSLQSSLdSEAKSRIEVTRLKKKMEEDLNEMELQLscanrqvseatksLGQLQIQIKDLQ 1666
Cdd:pfam05483 395 -------EMTKFKNNKEVELEELKKIL-AEDEKLLDEKKQFEKIAEELKGKEQEL-------------IFLLQAREKEIH 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1667 mqlddstqlnsDLKEQVAVAERRNSLLQSELEDLRSLQEQtergRRLSEEELLEATERI---NLFYTQNTS-LLSQKKKL 1742
Cdd:pfam05483 454 -----------DLEIQLTAIKTSEEHYLKEVEDLKTELEK----EKLKNIELTAHCDKLlleNKELTQEASdMTLELKKH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1743 EADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTI-AHLERTRENmeqtitdlqkrlAEAEQMALMGSR 1821
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVkCKLDKSEEN------------ARSIEYEVLKKE 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1822 KQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERcikeltyQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQA 1901
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKK-------KGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 119600132 1902 NQYLSKYKKQQHELNEVKERAEVAESQVNKLKikaREFGKKVQEE 1946
Cdd:pfam05483 660 QKEIEDKKISEEKLLEEVEKAKAIADEAVKLQ---KEIDKRCQHK 701
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1534-1715 |
2.08e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1534 NLTEMEKVKKLIEEEKTEVQVTLEETEGALE--RNESKILHFQLE---LLEAKAELERKLSEKDEEIENFRRKqqctIDS 1608
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEaklLLQQLSELESQLAEARAELAEAEAR----LAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1609 LQSSLDS--EAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQ-LNSDLKEQVAV 1685
Cdd:COG3206 245 LRAQLGSgpDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQrILASLEAELEA 324
|
170 180 190
....*....|....*....|....*....|.
gi 119600132 1686 AERRNSLLQSELEDLRS-LQEQTERGRRLSE 1715
Cdd:COG3206 325 LQAREASLQAQLAQLEArLAELPELEAELRR 355
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
926-1164 |
2.35e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 926 QLEARVKelserveeeeeinsELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLN 1005
Cdd:COG4942 24 EAEAELE--------------QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1006 RAAKVVQEahqqtldDLHMEEEKLSSLSKANLKLEQQvDELEGALEQERKARMncERELHKLEGNLKLNRESMENLESSQ 1085
Cdd:COG4942 90 KEIAELRA-------ELEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLDA--VRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119600132 1086 RHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEE 1164
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1210-1600 |
2.56e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1210 DSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEklctlYEERLHEATAKLDkvtqlandlaaqk 1289
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-----LYQELEALEAELA------------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1290 tklwsESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAH-ALQKAQRDCDLLREQYEEEQEVKAE 1368
Cdd:COG4717 143 -----ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1369 LHRTLSKVNAEMVQWRMKYENNVIQRT----------------------------------------------EDLEDAK 1402
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagvlflvlgllallfLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1403 KELAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQsgkaladwkQKHEESQALLDAS 1482
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE---------AEELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1483 QKEVQALsteLLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKV--KKLIEEEKTEVQVTLEETE 1560
Cdd:COG4717 369 EQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELE 445
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 119600132 1561 GALERNESKI--LHFQLELLEAKAELERKLSEKDEEIENFRR 1600
Cdd:COG4717 446 EELEELREELaeLEAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1446-1933 |
3.24e-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: 52.28 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1446 KVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTyEESIVGQETLRRENKNLQEEISNLT 1525
Cdd:TIGR00618 188 KKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQS-HAYLTQKREAQEEQLKKQQLLKQLR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1526 NQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETegALERNESKILHFQLELLEAKAELERKLSEKDEEIENfRRKQQCT 1605
Cdd:TIGR00618 267 ARIEELRAQEAVLEETQERINRARKAAPLAAHIK--AVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ-QSSIEEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1606 IDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMEL-----QLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLK 1680
Cdd:TIGR00618 344 RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLtqhihTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1681 EQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERinlfYTQNTSLLSQKKKLEADVARMQKEAEEVVQEC 1760
Cdd:TIGR00618 424 GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQS----LKEREQQLQTKEQIHLQETRKKAVVLARLLEL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1761 QNAE---EKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLqkrlaEAEQMALMGSRKQIQKLESRVRELEGE 1837
Cdd:TIGR00618 500 QEEPcplCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDV-----YHQLTSERKQRASLKEQMQEIQQSFSI 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1838 LEGEIRRSAEAQRGARRL-ERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELN 1916
Cdd:TIGR00618 575 LTQCDNRSKEDIPNLQNItVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT 654
|
490
....*....|....*..
gi 119600132 1917 EVKERAEVAESQVNKLK 1933
Cdd:TIGR00618 655 LTQERVREHALSIRVLP 671
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1400-1932 |
3.64e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.13 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1400 DAKKELAIRLQEAAEAMGVANARNASLERARHqLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALL 1479
Cdd:pfam10174 40 ELKKERALRKEEAARISVLKEQYRVTQEENQH-LQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1480 DASQKEVQALSTELLKLKNTYEE---SIVGQ--------ETLRRENKNLQ---------EEISNLTNQVREGTKNLTEME 1539
Cdd:pfam10174 119 RRLQSEHERQAKELFLLRKTLEEmelRIETQkqtlgardESIKKLLEMLQskglpkksgEEDWERTRRIAEAEMQLGHLE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1540 KVKKLIEEEKTEVQVTLE-ETEGALERNESKILHFQLELLEAK-AELERKLSEKDEEIEnfrrkqqctidSLQSSLDSEA 1617
Cdd:pfam10174 199 VLLDQKEKENIHLREELHrRNQLQPDPAKTKALQTVIEMKDTKiSSLERNIRDLEDEVQ-----------MLKTNGLLHT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1618 KSRievtrlkkkmEEDLNEMELQLSCAN---RQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSD-------LKEQVAVAE 1687
Cdd:pfam10174 268 EDR----------EEEIKQMEVYKSHSKfmkNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqhievLKESLTAKE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1688 RRNSLLQSELEDLRS--------LQEQTERGRRLSEE------------ELLEATER-INLFYTQNTSLLSQKKkleaDV 1746
Cdd:pfam10174 338 QRAAILQTEVDALRLrleekesfLNKKTKQLQDLTEEkstlageirdlkDMLDVKERkINVLQKKIENLQEQLR----DK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1747 ARMQKEAEEVVQECQnaeekakkaaIEAANLSEELKKKQDTIAHLERTRENM-EQTITDLQKRLAEAEQMalmgsRKQIQ 1825
Cdd:pfam10174 414 DKQLAGLKERVKSLQ----------TDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESL-----KKENK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1826 KLESRVRELEGELEG--------EIRRSAEAQRGARRLERcIKELTYQAEEDKKNLSRMQTQMDKlqlkvqnyKQQVEVA 1897
Cdd:pfam10174 479 DLKEKVSALQPELTEkesslidlKEHASSLASSGLKKDSK-LKSLEIAVEQKKEECSKLENQLKK--------AHNAEEA 549
|
570 580 590
....*....|....*....|....*....|....*
gi 119600132 1898 ETQANQYLSKYKKQQHELNEVKERAEVAESQVNKL 1932
Cdd:pfam10174 550 VRTNPEINDRIRLLEQEVARYKEESGKAQAEVERL 584
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1424-1925 |
3.77e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.13 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1424 ASLERARHQLQLELgDALSDLGKVRSAAARLDQKQLQSGKALADW-KQKHEESQALLDASQKEVQALSTELLKLKNTYEE 1502
Cdd:pfam10174 243 SSLERNIRDLEDEV-QMLKTNGLLHTEDREEEIKQMEVYKSHSKFmKNKIDQLKQELSKKESELLALQTKLETLTNQNSD 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1503 SI----VGQETLRRENKN---LQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILhfql 1575
Cdd:pfam10174 322 CKqhieVLKESLTAKEQRaaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKIN---- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1576 eLLEAKAE-LERKLSEKDEEIENFRRKQQ------CTIDSLQSSLDsEA---KSRIeVTRLKKKME-EDLNEMElqlsca 1644
Cdd:pfam10174 398 -VLQKKIEnLQEQLRDKDKQLAGLKERVKslqtdsSNTDTALTTLE-EAlseKERI-IERLKEQRErEDRERLE------ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1645 nrQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLR-SLQEQTERGRRLseEELLEATE 1723
Cdd:pfam10174 469 --ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEiAVEQKKEECSKL--ENQLKKAH 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1724 RINLFYTQNTSLLSQKKKLEADVARMQKEAeevvqecqnaeekakkaaieaanlseelKKKQDTIAHLERTRENMEQTIT 1803
Cdd:pfam10174 545 NAEEAVRTNPEINDRIRLLEQEVARYKEES----------------------------GKAQAEVERLLGILREVENEKN 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1804 DLQKRLAEAEQMALmgsrKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKE--LTYQAEEDKKNLSRMQTQMD 1881
Cdd:pfam10174 597 DKDKKIAELESLTL----RQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADnsQQLQLEELMGALEKTRQELD 672
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 119600132 1882 KLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEVKERAEVA 1925
Cdd:pfam10174 673 ATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLA 716
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1238-1863 |
4.08e-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: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1238 LEVDDLLTRVEQMtraKANAEKLctlyeERLHEATAKL-DKVTQLA--NDLAAQKTKLWsesgeflRRLEEKEALINQLS 1314
Cdd:COG4913 218 LEEPDTFEAADAL---VEHFDDL-----ERAHEALEDArEQIELLEpiRELAERYAAAR-------ERLAELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1315 REKSnfTRQIEDLRGQLEketksqsALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNaemvqwrmkyennviqr 1394
Cdd:COG4913 283 LWFA--QRRLELLEAELE-------ELRAELARLEAELERLEARLDALREELDELEAQIRGNG----------------- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1395 TEDLEDAKKELAirlqeaaeamgvanarnaslerarhQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALAdwkqkhee 1474
Cdd:COG4913 337 GDRLEQLEREIE-------------------------RLERELEERERRRARLEALLAALGLPLPASAEEFA-------- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1475 sqALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLtnqvREGTKNLT-EMEKVKKLIEEE--KTE 1551
Cdd:COG4913 384 --ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL----ERRKSNIPaRLLALRDALAEAlgLDE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1552 ---------VQVTLEET--EGALERneskILH-FQLELLeAKAELERKLSEKdeeIENFRRKQQCTIDSLQSSLDSEAKS 1619
Cdd:COG4913 458 aelpfvgelIEVRPEEErwRGAIER----VLGgFALTLL-VPPEHYAAALRW---VNRLHLRGRLVYERVRTGLPDPERP 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1620 RIEVTRLKKKMEEDLN------EMEL-------------QLSCANRQVSEA--TKSLGQLQiqikdlqmQLDDSTQLNSD 1678
Cdd:COG4913 530 RLDPDSLAGKLDFKPHpfrawlEAELgrrfdyvcvdspeELRRHPRAITRAgqVKGNGTRH--------EKDDRRRIRSR 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1679 -------------LKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNT--SLLSQKKKLE 1743
Cdd:COG4913 602 yvlgfdnraklaaLEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaELEAELERLD 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1744 A---DVARMQKEAEEVVQEcqnaeekakkaaieAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGS 1820
Cdd:COG4913 682 AssdDLAALEEQLEELEAE--------------LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 119600132 1821 RkqiQKLESRVRELEG-ELEGEIRRSAEAQRGA--RRLERCIKELT 1863
Cdd:COG4913 748 R---ALLEERFAAALGdAVERELRENLEERIDAlrARLNRAEEELE 790
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1582-1814 |
4.43e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1582 AELERKLSEKDEEIENFRRKQQctidslqsSLDSEAKSRIEVTRLKKkMEEDLNEMELQLSCANRQVSEATKSLGQLQIQ 1661
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNG--------LVDLSEEAKLLLQQLSE-LESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1662 IKDLQmqlddSTQLNSDLKEQVAVAERRNSLLQSEL----EDLRSLQEQTERGRRLSEEELLEATERINlfyTQNTSLLS 1737
Cdd:COG3206 256 LPELL-----QSPVIQQLRAQLAELEAELAELSARYtpnhPDVIALRAQIAALRAQLQQEAQRILASLE---AELEALQA 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119600132 1738 QKKKLEADVARMQKEAEEvvqecqnaeekakkaaieaanlseeLKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQ 1814
Cdd:COG3206 328 REASLQAQLAQLEARLAE-------------------------LPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1020-1308 |
5.44e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.84 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1020 DDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELEL 1099
Cdd:pfam19220 27 ADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1100 SQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQ 1179
Cdd:pfam19220 107 EELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1180 ETKFQKLHRDMEEatlhFETTSASLKKRhadsLAELEGQVENLQQVKQK----LEKDKSDLQLEVDDLLTRVEQMTRAKA 1255
Cdd:pfam19220 187 AAELAELTRRLAE----LETQLDATRAR----LRALEGQLAAEQAERERaeaqLEEAVEAHRAERASLRMKLEALTARAA 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 119600132 1256 NAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLwsesgefLRRLEEKEA 1308
Cdd:pfam19220 259 ATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTL-------ERRLAGLEA 304
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
596-687 |
5.82e-06 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 48.50 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 596 GVVPY---NISGWLEKNKDLLNETVVAVFQKSSNRLLAslfenymstdsAIPFGEKKR-----------KKGASFQTVAS 661
Cdd:cd01363 71 GVIPYlasVAFNGINKGETEGWVYLTEITVTLEDQILQ-----------ANPILEAFGnakttrnenssRFGKFIEILLD 139
|
90 100 110
....*....|....*....|....*....|.
gi 119600132 662 L-----HKENLNKLMTNLKSTAPHFVRCINP 687
Cdd:cd01363 140 IagfeiINESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1470-1689 |
6.24e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1470 QKHEESQALLDASQKEVQALSTELLKLKNTyeesivgQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEK 1549
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1550 TEVQVTLEETEGALERNESKI----LHFQLELL---EAKAELERKLsEKDEEIENFRRKQqctIDSLQSSLDSEAKSRIE 1622
Cdd:COG4942 93 AELRAELEAQKEELAELLRALyrlgRQPPLALLlspEDFLDAVRRL-QYLKYLAPARREQ---AEELRADLAELAALRAE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119600132 1623 VTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERR 1689
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1130-1893 |
8.17e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 50.91 E-value: 8.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1130 LKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQ-LEITKKQetkFQKLHRDMEEATLHFETTsaslkkrh 1208
Cdd:pfam07111 21 LERRLDTQRPTVTMWEQDVSGDGQGPGRRGRSLELEGSQALSQqAELISRQ---LQELRRLEEEVRLLRETS-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1209 adslaelegqvenLQQvKQKLEKDKSDLqlevdDLLTRVEQMTRAKAnaeklctlyeERLHEATAKLDKVTQlanDLAAQ 1288
Cdd:pfam07111 90 -------------LQQ-KMRLEAQAMEL-----DALAVAEKAGQAEA----------EGLRAALAGAEMVRK---NLEEG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1289 KTKlwsESGEFLRRLEEKEALINQLSREK-SNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQY---EEEQE 1364
Cdd:pfam07111 138 SQR---ELEEIQRLHQEQLSSLTQAHEEAlSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLsktQEELE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1365 VKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAK--KELAIRLQEAAEAMGVanaRNASLErarHQLQLElgdals 1442
Cdd:pfam07111 215 AQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQhlQEDRADLQATVELLQV---RVQSLT---HMLALQ------ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1443 dlgkvrsaAARLDQKQLQSGKALADWKQKheeSQALLDASQKEVQALSTELLKLKNTYEESIvgqetlrrenKNLQEEIS 1522
Cdd:pfam07111 283 --------EEELTRKIQPSDSLEPEFPKK---CRSLLNRWREKVFALMVQLKAQDLEHRDSV----------KQLRGQVA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1523 NLTNQVregTKNLTEMEKVKKLIEEEKTEVQVtleetegalERNESKILHFQL-ELLEAKAELERKLSEKDEEIENFRRK 1601
Cdd:pfam07111 342 ELQEQV---TSQSQEQAILQRALQDKAAEVEV---------ERMSAKGLQMELsRAQEARRRQQQQTASAEEQLKFVVNA 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1602 QQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVseatkSLGQLQIQIKDLQmqlDDSTQLNSDLKE 1681
Cdd:pfam07111 410 MSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKV-----ALAQLRQESCPPP---PPAPPVDADLSL 481
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1682 QVAVAERRNSLLQSELE-DLRSLQEQTERGRRLSEEELLEaterinlfytqntsLLSQKKKLEADVARMQKEAEEVVQEC 1760
Cdd:pfam07111 482 ELEQLREERNRLDAELQlSAHLIQQEVGRAREQGEAERQQ--------------LSEVAQQLEQELQRAQESLASVGQQL 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1761 QNAEEKAKKAAIEAANLSEELKKKQDTI--AHLERTRE---NMEQTITDLQKRLAEA--EQMALMGSRKQIQK--LESRV 1831
Cdd:pfam07111 548 EVARQGQQESTEEAASLRQELTQQQEIYgqALQEKVAEvetRLREQLSDTKRRLNEArrEQAKAVVSLRQIQHraTQEKE 627
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119600132 1832 RELEGELEGEIRRSAEAQRGARRLercikeltyQAEEDKKNLSRMQTQMDKLqlkVQNYKQQ 1893
Cdd:pfam07111 628 RNQELRRLQDEARKEEGQRLARRV---------QELERDKNLMLATLQQEGL---LSRYKQQ 677
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1265-1488 |
9.48e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1265 EERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHA 1344
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1345 LQKaqrdcdLLREQYEEEQEVKAELhrTLSKVNAEMVQWRMKYENNVIQ----RTEDLEDAKKELAIRLQEAAEAMGVAN 1420
Cdd:COG4942 106 LAE------LLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAParreQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119600132 1421 ARNASLERARHQLQLELGDAlsdlgkvRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQA 1488
Cdd:COG4942 178 ALLAELEEERAALEALKAER-------QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1750-1945 |
1.22e-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: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1750 QKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEqmalmgsrKQIQKLES 1829
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE--------KEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1830 RVRELEGELEGEIRR------------------SAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYK 1891
Cdd:COG4942 98 ELEAQKEELAELLRAlyrlgrqpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 119600132 1892 QQVEVAETQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQE 1945
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1049-1814 |
1.56e-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: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1049 ALEQERKARMNceRELHKLEGnlklnRESM--ENLESSQRHLA---------EELRKKELELSQMNSKVENEKGLVAQL- 1116
Cdd:COG3096 302 AEEQYRLVEMA--RELEELSA-----RESDleQDYQAASDHLNlvqtalrqqEKIERYQEDLEELTERLEEQEEVVEEAa 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1117 -------------QKTVKELQTQIKDLKEKLEAERT------------TRAKMERERADLTQD-----LADLNERLEEVG 1166
Cdd:COG3096 375 eqlaeaearleaaEEEVDSLKSQLADYQQALDVQQTraiqyqqavqalEKARALCGLPDLTPEnaedyLAAFRAKEQQAT 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1167 gSSLAQLEitkkqetkfQKLhRDMEEATLHFETTSASLKKrhadslaeLEGQVENLQ--QVKQKLEKDKSDLQLevddLL 1244
Cdd:COG3096 455 -EEVLELE---------QKL-SVADAARRQFEKAYELVCK--------IAGEVERSQawQTARELLRRYRSQQA----LA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1245 TRVEQMTRAKANAEKLctlyEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQI 1324
Cdd:COG3096 512 QRLQQLRAQLAELEQR----LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1325 EDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQwrmkyENNVIQRTEDLEDAKKE 1404
Cdd:COG3096 588 EQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVE-----RDELAARKQALESQIER 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1405 LA-------IRLQEAAEAMG----------------------VANARNA----SLERARHQLQlELGDALSDL----GKV 1447
Cdd:COG3096 663 LSqpggaedPRLLALAERLGgvllseiyddvtledapyfsalYGPARHAivvpDLSAVKEQLA-GLEDCPEDLylieGDP 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1448 RSAAARLDQKQLQSGKALA-----DWKQKHEESQALLD--ASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEE 1520
Cdd:COG3096 742 DSFDDSVFDAEELEDAVVVklsdrQWRYSRFPEVPLFGraAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQF 821
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1521 ISNLTNQVREGtknltEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHF--QLELLEAKAELERKLSEKD--EEIE 1596
Cdd:COG3096 822 VGGHLAVAFAP-----DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLkeQLQLLNKLLPQANLLADETlaDRLE 896
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1597 NFRRKQQCTIDSlQSSLDSEAKSRIEVTRLKKKMEED-LNEMELQLscanrQVSEATKSLGQLQIQIKDLQ--MQ----- 1668
Cdd:COG3096 897 ELREELDAAQEA-QAFIQQHGKALAQLEPLVAVLQSDpEQFEQLQA-----DYLQAKEQQRRLKQQIFALSevVQrrphf 970
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1669 -LDDSTQL---NSDLKEQvavaerrnsllqseledLRSLQEQTERGRRLSEEELLEATERinlfYTQNTSLLSQKKKLEA 1744
Cdd:COG3096 971 sYEDAVGLlgeNSDLNEK-----------------LRARLEQAEEARREAREQLRQAQAQ----YSQYNQVLASLKSSRD 1029
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119600132 1745 DVARMQKEAEEVVQE--CQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQ 1814
Cdd:COG3096 1030 AKQQTLQELEQELEElgVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAER 1101
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1638-1814 |
2.20e-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: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1638 ELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRS-LQEQTER-GRRLSE 1715
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeIEERREElGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1716 -----------EELLEAT---------ERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNaeeKAKKAAIEAA 1775
Cdd:COG3883 95 lyrsggsvsylDVLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA---LKAELEAAKA 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 119600132 1776 NLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQ 1814
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1512-1926 |
2.20e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1512 RENKNLQEEISNLTNQVREgtknLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFqlELLEAKAELERKLSEK 1591
Cdd:COG4717 71 KELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEKLLQLL--PLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1592 DEEIENFRRKQQctidslqssldseakSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSlgqlqiQIKDLQMQLDD 1671
Cdd:COG4717 145 PERLEELEERLE---------------ELRELEEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1672 STQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEE-LLEATERINLFYTQNTSLLSQKKKLEADVA--- 1747
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlLLLIAAALLALLGLGGSLLSLILTIAGVLFlvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1748 -----------RMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQD-TIAHLERTRENMEQTITDLQKRLAEAEQM 1815
Cdd:COG4717 284 gllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1816 ALMGSRKQIQKLesrVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDK--LQLKVQNYKQQ 1893
Cdd:COG4717 364 QLEELEQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEE 440
|
410 420 430
....*....|....*....|....*....|...
gi 119600132 1894 VEVAETQANQYLSKYKKQQHELNEVKERAEVAE 1926
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
860-1140 |
2.23e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.72 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 860 EVAGLKEECAQLQKAL-EKSEFQR--EELKAKQvsltqekNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSE 936
Cdd:pfam05483 406 ELEELKKILAEDEKLLdEKKQFEKiaEELKGKE-------QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKT 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 937 RVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQ 1016
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFI 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1017 QTLDD----LHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKL-EGNLKLNRESmeNLESSQRHLAE- 1090
Cdd:pfam05483 559 QKGDEvkckLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELhQENKALKKKG--SAENKQLNAYEi 636
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 119600132 1091 ELRKKELELSQMNSKVENekgLVAQLQKTVKELQTQIKDLKEKLEAERTT 1140
Cdd:pfam05483 637 KVNKLELELASAKQKFEE---IIDNYQKEIEDKKISEEKLLEEVEKAKAI 683
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1113-1434 |
2.43e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.35 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1113 VAQLQKTVKELQTQIKdlKEKLEAERTTRAKMERERAdltqdlADLNERLEEVGGSSLAQLEitkKQETKFQKLHRDMEE 1192
Cdd:pfam17380 277 IVQHQKAVSERQQQEK--FEKMEQERLRQEKEEKARE------VERRRKLEEAEKARQAEMD---RQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1193 ATLHFETTSASLKKRHADSLAELEGQVEnLQQVKQkLEKdksdLQLEVDDLLTRVEQMTRAkanAEKLCTLYEERLHeat 1272
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEIAME-ISRMRE-LER----LQMERQQKNERVRQELEA---ARKVKILEEERQR--- 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1273 akldKVTQLANDLAAQKTKLWSESGEFLRRLEEKEAL-INQLSREKSNFTRQIEDLRGQLEKETKSQSalahALQKAQRD 1351
Cdd:pfam17380 414 ----KIQQQKVEMEQIRAEQEEARQREVRRLEEERAReMERVRLEEQERQQQVERLRQQEEERKRKKL----ELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1352 CDLLREQYEE--EQEVKAELHRTLSKVNA-EMVQWRMKYENNVI----QRTEDLEDAKKELAI----RLQEAAEAMGVAN 1420
Cdd:pfam17380 486 RKRAEEQRRKilEKELEERKQAMIEEERKrKLLEKEMEERQKAIyeeeRRREAEEERRKQQEMeerrRIQEQMRKATEER 565
|
330
....*....|....
gi 119600132 1421 ARNASLERARHQLQ 1434
Cdd:pfam17380 566 SRLEAMEREREMMR 579
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
953-1276 |
2.70e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 49.47 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 953 RKLEDECFELKKEIDDLETMLVKS---------EKEKRTTEHKVKN------LTEEVEFLNEDISKLNRAAKVVQEAHQQ 1017
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPselalnemiEKLKKEIDLEYTEaviamgLQERLENLREEFSKANSQDQLMHPVLME 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1018 TLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLnRESMENLESSQRHlaeELRKKEL 1097
Cdd:PLN03229 512 KIEKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKF-KEVMDRPEIKEKM---EALKAEV 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1098 ELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEK--LEAERTTRAKMERERADLTQDLADLNERLEEvggsslaqlEI 1175
Cdd:PLN03229 588 ASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSmgLEVIGVTKKNKDTAEQTPPPNLQEKIESLNE---------EI 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1176 TKKQE--TKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEgqvenlQQVKQKLEK--DKSDLQLEVDDLltRVEQMT 1251
Cdd:PLN03229 659 NKKIErvIRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALE------QQIKQKIAEalNSSELKEKFEEL--EAELAA 730
|
330 340
....*....|....*....|....*
gi 119600132 1252 RAKANAEKLCTLYEERLHEATAKLD 1276
Cdd:PLN03229 731 ARETAAESNGSLKNDDDKEEDSKED 755
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1405-1620 |
2.96e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1405 LAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQK 1484
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1485 EVQALSTELLKLKNTYEESIVGQETLRREN------------------KNLQEEISNLTNQVREGTKNLTEMEKVKKLIE 1546
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPplalllspedfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119600132 1547 EEKTEVQVTLEETEGALERNESKilhfQLELLEAKAELERKLSEKDEEIENFRRKQQcTIDSLQSSLDSEAKSR 1620
Cdd:COG4942 171 AERAELEALLAELEEERAALEAL----KAERQKLLARLEKELAELAAELAELQQEAE-ELEALIARLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1299-1717 |
4.99e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1299 FLRRLE-EKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRdcdlLREQYEEEQEVKAELHRTLSKVN 1377
Cdd:COG4717 47 LLERLEkEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1378 AEMVQWRmkyennVIQRTEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQlELGDALSDLGKVRSAAARLDQK 1457
Cdd:COG4717 123 KLLQLLP------LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA-ELQEELEELLEQLSLATEEELQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1458 QLQsgKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEE------------------SIVGQETLRRENKNLQE 1519
Cdd:COG4717 196 DLA--EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAaaleerlkearlllliaaALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1520 EISNL------------TNQVREGTKNLTEMEKVKKLIEEEKTEvQVTLEETEGALERNESKILHFQLELLEAKAELERK 1587
Cdd:COG4717 274 TIAGVlflvlgllallfLLLAREKASLGKEAEELQALPALEELE-EEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1588 LSEKDE-----EIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSE--ATKSLGQLQI 1660
Cdd:COG4717 353 LREAEEleeelQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEE 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 119600132 1661 QIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEE 1717
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1644-1868 |
5.99e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1644 ANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLrslqeqtERGRRLSEEELLEATE 1723
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-------EQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1724 RINlfyTQNTSLLSQKKKLEADVARMQKEAE----------EVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLER 1793
Cdd:COG4942 91 EIA---ELRAELEAQKEELAELLRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119600132 1794 TRENMEQTITDLQKRLaEAEQMALMGSRKQIQKLESRVRELEGELEGEIrrsAEAQRGARRLERCIKELTYQAEE 1868
Cdd:COG4942 168 ELEAERAELEALLAEL-EEERAALEALKAERQKLLARLEKELAELAAEL---AELQQEAEELEALIARLEAEAAA 238
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1535-1631 |
7.03e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.93 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1535 LTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEA-KAELERKLSEKDEEIENFRRKqqctIDSLQSSL 1613
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAeVEELEAELEEKDERIERLERE----LSEARSEE 457
|
90
....*....|....*...
gi 119600132 1614 DSEAKSRIEVTRLKKKME 1631
Cdd:COG2433 458 RREIRKDREISRLDREIE 475
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
977-1143 |
7.09e-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: 46.46 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 977 EKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAkvvqEAHQQTLDDLHMEEEKLSSLSKAnlkLEQQVDELEGALEQERKA 1056
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARL----EAAKTELEDLEKEIKRLELEIEE---VEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1057 RmncerELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEA 1136
Cdd:COG1579 89 K-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*..
gi 119600132 1137 ERTTRAK 1143
Cdd:COG1579 164 EREELAA 170
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
866-1342 |
8.25e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.51 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 866 EECAQLQKALEKSEFqreeLKAKQVSLTQE---KNDLILQLQAEQETLANVEEQCEWLIK-------SKIQ----LEARV 931
Cdd:pfam10174 272 EEIKQMEVYKSHSKF----MKNKIDQLKQElskKESELLALQTKLETLTNQNSDCKQHIEvlkesltAKEQraaiLQTEV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 932 KELSERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVV 1011
Cdd:pfam10174 348 DALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSL 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1012 QEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGA----LEQERKARMNCERELHKLEGNLKLNRESMENLESSQRH 1087
Cdd:pfam10174 428 QTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRErleeLESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASS 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1088 LAEELRKKELELSQMNSKVENEKglvaqlqKTVKELQTQIKDLKEKLEAERTTRAKMERERAdLTQDLAdlneRLEEVGG 1167
Cdd:pfam10174 508 LASSGLKKDSKLKSLEIAVEQKK-------EECSKLENQLKKAHNAEEAVRTNPEINDRIRL-LEQEVA----RYKEESG 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1168 SSLAQLEitkkqetKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVddlltRV 1247
Cdd:pfam10174 576 KAQAEVE-------RLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEA-----RR 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1248 EQMTRAKANAEKlctlyeeRLHEATAKLDKVTQlanDLAAQKTKLWSESgeflRRLEEKEALINQLSREKsnftrqiedl 1327
Cdd:pfam10174 644 REDNLADNSQQL-------QLEELMGALEKTRQ---ELDATKARLSSTQ----QSLAEKDGHLTNLRAER---------- 699
|
490
....*....|....*..
gi 119600132 1328 RGQLEK--ETKSQSALA 1342
Cdd:pfam10174 700 RKQLEEilEMKQEALLA 716
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1323-1932 |
8.80e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1323 QIEDLRGQLE-KETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRmkyennviQRTEDLEDA 1401
Cdd:PRK02224 188 SLDQLKAQIEeKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR--------EELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1402 KKELAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDA 1481
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1482 SQKEVQALSTELLKLKNTYEEsivgqetLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEG 1561
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEE-------LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1562 ALE--RNESKILHFQLELLEAKAELERKLSEKDEEIENFRRKQQCTidslQSSLDSEAKSRIEVTRLKK-KMEEDLNEME 1638
Cdd:PRK02224 413 FLEelREERDELREREAELEATLRTARERVEEAEALLEAGKCPECG----QPVEGSPHVETIEEDRERVeELEAELEDLE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1639 LQLSCANRQVSEAtKSLGQLQIQIKDLQMQLDDSTQLnsdlkeqvaVAERRNSLlqseledlrslQEQTERGRRLSEEel 1718
Cdd:PRK02224 489 EEVEEVEERLERA-EDLVEAEDRIERLEERREDLEEL---------IAERRETI-----------EEKRERAEELRER-- 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1719 leaterinlfytqntsllsqKKKLEADVARMQKEAEEVVQECQnaeekakKAAIEAANLSEELKKKQDTIAHLER----- 1793
Cdd:PRK02224 546 --------------------AAELEAEAEEKREAAAEAEEEAE-------EAREEVAELNSKLAELKERIESLERirtll 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1794 -TRENMEQTITDLQKRLaeaEQMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLErcikelTYQAEEDKKn 1872
Cdd:PRK02224 599 aAIADAEDEIERLREKR---EALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAE------EYLEQVEEK- 668
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1873 LSRMQTQMDKLQLKVQNYKQQVEvaetqanqylskykkqqhELNEVKERAEVAESQVNKL 1932
Cdd:PRK02224 669 LDELREERDDLQAEIGAVENELE------------------ELEELRERREALENRVEAL 710
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1302-1810 |
9.25e-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: 47.43 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1302 RLEEKEALINQLSREKSNftRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLL-REQYEEEQEVKAElhrTLSKVNAEM 1380
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQ--MELEHKRARIELEKKASALKRQLDRESDRNQELQkRIRLLEKREAEAE---EALREQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1381 VQWRMKYENNVIQRTEDLEDakkelaiRLQEAAEAMGVANARNASLERARHQLQLELGDALSDLGKVRsaaarlDQKQLQ 1460
Cdd:pfam05557 78 NRLKKKYLEALNKKLNEKES-------QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQ------ERLDLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1461 SGKAladwkQKHEESQALLDASQKEvqaLSTELLKLKnTYEESIVGQETLRRENKNLQEEISNLTN------QVREGTKN 1534
Cdd:pfam05557 145 KAKA-----SEAEQLRQNLEKQQSS---LAEAEQRIK-ELEFEIQSQEQDSEIVKNSKSELARIPElekeleRLREHNKH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1535 LTEMEKVKKLIEEEKTEVQVTLEETEGAlerneskilhfqlelLEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSsld 1614
Cdd:pfam05557 216 LNENIENKLLLKEEVEDLKRKLEREEKY---------------REEAATLELEKEKLEQELQSWVKLAQDTGLNLRS--- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1615 SEAKSRievtRLKKKMEEDLNEMElQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQ 1694
Cdd:pfam05557 278 PEDLSR----RIEQLQQREIVLKE-ENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLT 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1695 SELEDLRSLQE-------QTERGRRLSeEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKA 1767
Cdd:pfam05557 353 KERDGYRAILEsydkeltMSNYSPQLL-ERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQE 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 119600132 1768 KKAAIEAANLS-EELKKKQDtiaHLERTRENMEQTITDLQKRLA 1810
Cdd:pfam05557 432 SLADPSYSKEEvDSLRRKLE---TLELERQRLREQKNELEMELE 472
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
871-1363 |
1.20e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 871 LQKALEKsefQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKelserveeeeeinsELTA 950
Cdd:COG4717 47 LLERLEK---EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE--------------ELEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 951 RGRKLEDECFELKKEIDDLETMLVKSEKEKRTTE--HKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQ----TLDDLHM 1024
Cdd:COG4717 110 ELEELREELEKLEKLLQLLPLYQELEALEAELAElpERLEELEERLEELRELEEELEELEAELAELQEEleelLEQLSLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1025 EEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNS 1104
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1105 KVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQdlADLNERLEEVGGSSLAQLEITKKQETKFQ 1184
Cdd:COG4717 270 SLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1185 KLHRDMEEAT---------LHFETTSASLKKRHADSLAELEGQVENLQQvKQKLEKDKSDLQLEVDDLLTRVEQMtRAKA 1255
Cdd:COG4717 348 ELQELLREAEeleeelqleELEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEEL-LEAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1256 NAEKLctlyEERLHEATAKLDKVTQLANDLAAQKTKLWSEsgefLRRLEEKEALinqlsrekSNFTRQIEDLRGQLEKET 1335
Cdd:COG4717 426 DEEEL----EEELEELEEELEELEEELEELREELAELEAE----LEQLEEDGEL--------AELLQELEELKAELRELA 489
|
490 500
....*....|....*....|....*...
gi 119600132 1336 KSQSALAHALQKAQRdcdlLREQYEEEQ 1363
Cdd:COG4717 490 EEWAALKLALELLEE----AREEYREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1209-1453 |
1.26e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1209 ADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQ 1288
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1289 KTKLWSESGEFLR---RLEEKEALINQLSREKSNftrQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEV 1365
Cdd:COG4942 99 LEAQKEELAELLRalyRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1366 KAELhrtlskvnaemvqwrmkyENNVIQRTEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQlelgDALSDLG 1445
Cdd:COG4942 176 LEAL------------------LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE----ALIARLE 233
|
....*...
gi 119600132 1446 KVRSAAAR 1453
Cdd:COG4942 234 AEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1576-1928 |
1.34e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1576 ELLEAKAELERKLSEKDEEIENFRRKQQctidslqssldsEAKSRIEVTRLK-KKMEEDLNEMELQLSCANRQVSEATKS 1654
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAGISKYKERRK------------ETERKLERTRENlDRLEDILNELERQLKSLERQAEKAERY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1655 LgQLQIQIKDLQMQLddstqLNSDLKEQVAVAERrnslLQSELEDLRSLQEQTERGRRLSEEELLEaterinlfytqnts 1734
Cdd:TIGR02168 216 K-ELKAELRELELAL-----LVLRLEELREELEE----LQEELKEAEEELEELTAELQELEEKLEE-------------- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1735 LLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEq 1814
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK- 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1815 malmgsrkqiqklesrvreleGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQV 1894
Cdd:TIGR02168 351 ---------------------EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
330 340 350
....*....|....*....|....*....|....
gi 119600132 1895 EvaetQANQYLSKYKKQQHELNEVKERAEVAESQ 1928
Cdd:TIGR02168 410 E----RLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1439-1629 |
1.37e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1439 DALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESivgqETLRRENKNLQ 1518
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV----EARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1519 EEISNlTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERKLSEKDEEIENF 1598
Cdd:COG1579 83 GNVRN-NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170 180 190
....*....|....*....|....*....|.
gi 119600132 1599 RRKqqctIDSLQSSLDSEAKSRIEVTRLKKK 1629
Cdd:COG1579 162 EAE----REELAAKIPPELLALYERIRKRKN 188
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1482-1946 |
1.37e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1482 SQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEG 1561
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1562 aLERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRKQQCTidslqSSLDSEAKSRIEVTRLKKKMEEDLNEMELQL 1641
Cdd:PRK03918 243 -LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KELKEKAEEYIKLSEFYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1642 SCANRQVSEatkslgqLQIQIKDLQmqlDDSTQLNSDLKEQVAVAERRNSLLQS--ELEDLRSLQEQTERGR-RLSEEEL 1718
Cdd:PRK03918 317 SRLEEEING-------IEERIKELE---EKEERLEELKKKLKELEKRLEELEERheLYEEAKAKKEELERLKkRLTGLTP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1719 LEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEE-----LKKKQDTIAHLER 1793
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1794 TRENMEQTITDLQKRLAEAEQMALMGSR--------KQIQKLESR------------------VRELEGELEGEIRRSAE 1847
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESEliklkelaEQLKELEEKlkkynleelekkaeeyekLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1848 AQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLK-VQNYKQQVEVAETQANQYLS-------------KYKKQQH 1913
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPFYNEYLElkdaekelereekELKKLEE 626
|
490 500 510
....*....|....*....|....*....|...
gi 119600132 1914 ELNEVKERAEVAESQVNKLKIKAREFGKKVQEE 1946
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEE 659
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1734-1931 |
1.45e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1734 SLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAE-- 1811
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEll 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1812 --------AEQMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKL 1883
Cdd:COG4942 111 ralyrlgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 119600132 1884 QLKVQNYKQQVEVAETQANQY---LSKYKKQQHELNEVKERAEVAESQVNK 1931
Cdd:COG4942 191 EALKAERQKLLARLEKELAELaaeLAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1455-1654 |
1.47e-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: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1455 DQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVRE---- 1530
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1531 ---------------GTKNLTE----MEKVKKLIEEEKTEVQvTLEETEGALERNESKILHFQLELLEAKAELERKLSEK 1591
Cdd:COG3883 95 lyrsggsvsyldvllGSESFSDfldrLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119600132 1592 DEEIEnfrrKQQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKS 1654
Cdd:COG3883 174 EAQQA----EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1045-1185 |
1.50e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1045 ELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGL------------ 1112
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyea 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119600132 1113 ----VAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQK 1185
Cdd:COG1579 94 lqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
945-1328 |
1.50e-04 |
|
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: 46.87 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 945 NSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLT--------EEVEFLNEDISKLNRAAKVVQEAHQ 1016
Cdd:COG5185 156 VETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGtvnsikesETGNLGSESTLLEKAKEIINIEEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1017 QTLDDLHMEEEKLsslskanlklEQQVDELEGALEQERKARMNCERELHKLEGNLKLNREsmeNLESSQRHLAEELRKKE 1096
Cdd:COG5185 236 KGFQDPESELEDL----------AQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENAN---NLIKQFENTKEKIAEYT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1097 LELSQMNSKVENEK-----GLVAQLQKTVKELQTQIKDLKEKLE------AERTTRAKMERERADLTQDLADLNERLEEV 1165
Cdd:COG5185 303 KSIDIKKATESLEEqlaaaEAEQELEESKRETETGIQNLTAEIEqgqeslTENLEAIKEEIENIVGEVELSKSSEELDSF 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1166 GgsslAQLEITKKqetKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENL-------QQVKQKLEKDKSDLQL 1238
Cdd:COG5185 383 K----DTIESTKE---SLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQAtssneevSKLLNELISELNKVMR 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1239 EVDDLLTRVEQMTRAKANAEKLCTLYEerlheataKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKS 1318
Cdd:COG5185 456 EADEESQSRLEEAYDEINRSVRSKKED--------LNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLK 527
|
410
....*....|
gi 119600132 1319 NFTRQIEDLR 1328
Cdd:COG5185 528 DFMRARGYAH 537
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
898-1401 |
1.53e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 898 DLILQLQAEQETLANVEEQCEWLIKSKIQLEA--RVKELSERVEEEEEINsELTARGRKLEDECFELKKEIDDLETMLVK 975
Cdd:COG4913 242 EALEDAREQIELLEPIRELAERYAAARERLAEleYLRAALRLWFAQRRLE-LLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 976 SEKEKRTTEHKVKNL-TEEVEFLNEDISKLNRAAKVVQEAH---QQTLDDLHMEE-------EKLSSLSKANL------- 1037
Cdd:COG4913 321 LREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRarlEALLAALGLPLpasaeefAALRAEAAALLealeeel 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1038 -KLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLessQRHLAEELRKKEL------ELSQMNSKVENEK 1110
Cdd:COG4913 401 eALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL---RDALAEALGLDEAelpfvgELIEVRPEEERWR 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1111 G-------------LV-----AQLQKTVKELqtqikDLKEKL--EAERTTRAKMERERADlTQDLAD------------L 1158
Cdd:COG4913 478 GaiervlggfaltlLVppehyAAALRWVNRL-----HLRGRLvyERVRTGLPDPERPRLD-PDSLAGkldfkphpfrawL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1159 NERLEEVGG----SSLAQLE-----IT-----KKQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQ 1224
Cdd:COG4913 552 EAELGRRFDyvcvDSPEELRrhpraITragqvKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEE 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1225 VKQKLEKDKSDLQlEVDDLLTRVEQMTRAKANAEKLctlyEERLHEATAKLDKVTQLANDLAA---QKTKLWSESGEFLR 1301
Cdd:COG4913 632 RLEALEAELDALQ-ERREALQRLAEYSWDEIDVASA----EREIAELEAELERLDASSDDLAAleeQLEELEAELEELEE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1302 RLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSA---------LAHALQKAQRdcDLLREQYEEEQEV-KAELHR 1371
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralleerFAAALGDAVE--RELRENLEERIDAlRARLNR 784
|
570 580 590
....*....|....*....|....*....|
gi 119600132 1372 TLSKVNAEMVQWRMKYENNVIQRTEDLEDA 1401
Cdd:COG4913 785 AEEELERAMRAFNREWPAETADLDADLESL 814
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1210-1815 |
2.16e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1210 DSLAELEGQVENLQQVKQKLEKDKSDL-----QLEVD-----DLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVT 1279
Cdd:PRK01156 173 DVIDMLRAEISNIDYLEEKLKSSNLELenikkQIADDekshsITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1280 QLANDLAAQKTKL---------WSESGEFLRRLEEKEALINQLS-REKSNFTRQIEDLRgQLEKETKSQSALAHALQKAQ 1349
Cdd:PRK01156 253 RYESEIKTAESDLsmeleknnyYKELEERHMKIINDPVYKNRNYiNDYFKYKNDIENKK-QILSNIDAEINKYHAIIKKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1350 RDCDLLREQYEEEQEVKAELHRTLSkvnaEMVQWRMKYE---NNVIQRTEDLEDAKKELAIRLQEAAEAMGVANARNASL 1426
Cdd:PRK01156 332 SVLQKDYNDYIKKKSRYDDLNNQIL----ELEGYEMDYNsylKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1427 ERARHQLQLELGDALSDLGKVRsaaarldqkqlQSGKALADWKQKHEESQALLDAsQKEVQALSTELlklkntyeesivG 1506
Cdd:PRK01156 408 KKELNEINVKLQDISSKVSSLN-----------QRIRALRENLDELSRNMEMLNG-QSVCPVCGTTL------------G 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1507 QETLRRENKNLQEEISNLTNQVREgtknlteMEKVKKLIEEEKTEVQVTLEETEGAlerneskilhfQLELLEAKaelER 1586
Cdd:PRK01156 464 EEKSNHIINHYNEKKSRLEEKIRE-------IEIEVKDIDEKIVDLKKRKEYLESE-----------EINKSINE---YN 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1587 KLSEKDEEIENFRrkqqctiDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSeatkslgqlQIQIKDLQ 1666
Cdd:PRK01156 523 KIESARADLEDIK-------IKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVIS---------LIDIETNR 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1667 MQLDDstqlnsdLKEQVAVAERRNSLLQSELEDLRSLqeqTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLE--- 1743
Cdd:PRK01156 587 SRSNE-------IKKQLNDLESRLQEIEIGFPDDKSY---IDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDnyk 656
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119600132 1744 ---ADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQM 1815
Cdd:PRK01156 657 kqiAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKI 731
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1413-1603 |
2.27e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1413 AEAMGVANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTE 1492
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1493 LLKLKNTYEESIVG-QETLRREN--------KNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEektevqvtLEETEGAL 1563
Cdd:COG3883 81 IEERREELGERARAlYRSGGSVSyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAE--------LEAKKAEL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 119600132 1564 ERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRKQQ 1603
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1042-1600 |
2.56e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1042 QVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLE---SSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQK 1118
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRaeiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1119 TVKELQTQIKDLKEK----------LEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETK------ 1182
Cdd:PRK01156 219 EIERLSIEYNNAMDDynnlksalneLSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKnrnyin 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1183 -FQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDksDLQLEVDDLLTRVEQMTRAKANAEKLC 1261
Cdd:PRK01156 299 dYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYD--DLNNQILELEGYEMDYNSYLKSIESLK 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1262 TLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLE--------- 1332
Cdd:PRK01156 377 KKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcp 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1333 ------KETKSQSALAHALQKAQR---DCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKK 1403
Cdd:PRK01156 457 vcgttlGEEKSNHIINHYNEKKSRleeKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKI 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1404 ELAiRLQEAAEAMGVANARNASLErarhqlqleLGDalsdlgkvrsaaarLDQKQLQSGKALAdwkqkhEESQALLDASQ 1483
Cdd:PRK01156 537 KIN-ELKDKHDKYEEIKNRYKSLK---------LED--------------LDSKRTSWLNALA------VISLIDIETNR 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1484 KEVQALSTELLKLKNTYEESIVGQETLRRENKN----LQEEISNLTNQVREGTKNLTEMEKVKKLIE------------- 1546
Cdd:PRK01156 587 SRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKsireIENEANNLNNKYNEIQENKILIEKLRGKIDnykkqiaeidsii 666
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119600132 1547 EEKTEVQVTLEETEGALERNESKILHFQLELLEAKA----------ELERKLSEKDEEIENFRR 1600
Cdd:PRK01156 667 PDLKEITSRINDIEDNLKKSRKALDDAKANRARLEStieilrtrinELSDRINDINETLESMKK 730
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1476-1707 |
2.97e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1476 QALLDASQKE----VQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIE----- 1546
Cdd:pfam07888 33 QNRLEECLQEraelLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSassee 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1547 --EEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERkLSEKDEEIENFRRKQQCTIDSLQSSLDSeakSRIEVT 1624
Cdd:pfam07888 113 lsEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER-MKERAKKAGAQRKEEEAERKQLQAKLQQ---TEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1625 RLKKKMEEDLNEMELQLSCANRQVSEATKsLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQ 1704
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITT-LTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQR 267
|
...
gi 119600132 1705 EQT 1707
Cdd:pfam07888 268 DRT 270
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
927-1190 |
3.21e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 927 LEARVKELSERVEEEEEINSELTARGRKLEDECFELKKEIddletmlvKSEKEKRTTEhkVKNLTEEVEFLNEDISKLNR 1006
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTI--------KAEIEELTDE--LLNLVMDIEDPSAALNKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1007 AAKVVQEAHQQTLDDLHMEEE---------KLSSLSKANLKLEQQVDELEGALEQERKARMNcerelhklegnlklnres 1077
Cdd:PHA02562 263 AAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDE------------------ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1078 menlESSQRHLAEELRKKELELsqmNSKVENEKGLVAQLQKTVKELQTQIKDLKEkleaerttrakmerERADLTQDLAD 1157
Cdd:PHA02562 325 ----LEEIMDEFNEQSKKLLEL---KNKISTNKQSLITLVDKAKKVKAAIEELQA--------------EFVDNAEELAK 383
|
250 260 270
....*....|....*....|....*....|...
gi 119600132 1158 LNERLEEVggsslaqleITKKQETKFQKLHRDM 1190
Cdd:PHA02562 384 LQDELDKI---------VKTKSELVKEKYHRGI 407
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1265-1492 |
3.26e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1265 EERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHA 1344
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1345 LQKAQRDCDLLrEQYEEEQEVKAELHRtlskvnAEMVQWRMKYENNVIQRT----EDLEDAKKELAIRLQEAAEAMGVAN 1420
Cdd:COG3883 95 LYRSGGSVSYL-DVLLGSESFSDFLDR------LSALSKIADADADLLEELkadkAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119600132 1421 ARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTE 1492
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
855-1165 |
3.35e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 855 SEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEA----- 929
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETelerm 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 930 --RVKELSERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEV------EFLNEDI 1001
Cdd:pfam07888 156 keRAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLttahrkEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1002 SKLNRAAKVVQEAHQQTLDDLHMEEEKLSS--------LSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKL 1073
Cdd:pfam07888 236 LEELRSLQERLNASERKVEGLGEELSSMAAqrdrtqaeLHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1074 NRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGL-VAQLQKTVKELQtqikDLKEKLEAERTTRAKMERERADLT 1152
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCnRVQLSESRRELQ----ELKASLRVAQKEKEQLQAEKQELL 391
|
330
....*....|...
gi 119600132 1153 QDLADLNERLEEV 1165
Cdd:pfam07888 392 EYIRQLEQRLETV 404
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
853-1086 |
3.40e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 853 KSSEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQ--VSLTQEKNDLILQLQAEQETLANVEEQcewliksKIQLEAR 930
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAE-------LAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 931 VKELSERVEEEEEINSELTArgrklEDECFELKKEIDDLETMLvkSEKEKRTTEH--KVKNLTEEVEFLNEDISKlnRAA 1008
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAEL--AELSARYTPNhpDVIALRAQIAALRAQLQQ--EAQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119600132 1009 KVVQEAHQQtlddlhmeeekLSSLSKANLKLEQQVDELEGALEQERKArmncERELHKLEGNLKLNRESMENLESSQR 1086
Cdd:COG3206 313 RILASLEAE-----------LEALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYESLLQRLE 375
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1681-1945 |
3.46e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1681 EQVAVAERRNSLLQSE----LEDLRSLQEQTERGRRLSEE-ELLEATERINlfytQNTSLLSQKKKLEADVARMQKEAEE 1755
Cdd:TIGR02169 180 EEVEENIERLDLIIDEkrqqLERLRREREKAERYQALLKEkREYEGYELLK----EKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1756 VVQECQNAEEKAKKAAIEAANLSEELKKK--------QDTIAHLERTRENMEQTITDLQKRLAEAEQmALMGSRKQIQKL 1827
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDAEE-RLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1828 ESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSK 1907
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270
....*....|....*....|....*....|....*...
gi 119600132 1908 YKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQE 1945
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1675-1909 |
3.55e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1675 LNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRR--LSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKE 1752
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1753 AEEVvqecqNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAeqmalmgsRKQIQKLESRVR 1832
Cdd:COG3206 242 LAAL-----RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL--------RAQIAALRAQLQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119600132 1833 ELEGELEGEIRRSAEAqrgARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQlkvqnykQQVEVAETQANQYLSKYK 1909
Cdd:COG3206 309 QEAQRILASLEAELEA---LQAREASLQAQLAQLEARLAELPELEAELRRLE-------REVEVARELYESLLQRLE 375
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1779-1886 |
3.95e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1779 EELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQmalmgsrkQIQKLESRVRELEGELEGEIRRSAEAQRGAR---RL 1855
Cdd:COG2433 406 RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE--------RIERLERELSEARSEERREIRKDREISRLDReieRL 477
|
90 100 110
....*....|....*....|....*....|.
gi 119600132 1856 ERCIKELTYQAEEDKKNLSRMQtQMDKLQLK 1886
Cdd:COG2433 478 ERELEEERERIEELKRKLERLK-ELWKLEHS 507
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
853-1440 |
4.60e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 853 KSSEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKndlILQLQAEQETLANVEEQCEWLIKS-KIQLEARV 931
Cdd:pfam12128 295 LDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDAD---IETAAADQEQLPSWQSELENLEERlKALTGKHQ 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 932 KELSERVEEEEEINSELTARGRKLEDECFELKKEIDDL----ETMLVKSEKEKRTT-EHKVKNLTEEVEFLNEDISKLnr 1006
Cdd:pfam12128 372 DVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQlavaEDDLQALESELREQlEAGKLEFNEEEYRLKSRLGEL-- 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1007 aaKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKL-EGNLKLNR------ESME 1079
Cdd:pfam12128 450 --KLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALrQASRRLEErqsaldELEL 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1080 NLESSQRHLAEELRKKELELSQMNSKV--------------ENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKME 1145
Cdd:pfam12128 528 QLFPQAGTLLHFLRKEAPDWEQSIGKVispellhrtdldpeVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLD 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1146 RERADLtQDLADLNERLEEVGGSSLAQLEITKKQET-----------KFQKLHRDMEEATLHFETTSASLKKRHADSLAE 1214
Cdd:pfam12128 608 KAEEAL-QSAREKQAAAEEQLVQANGELEKASREETfartalknarlDLRRLFDEKQSEKDKKNKALAERKDSANERLNS 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1215 LEGQVENL----QQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKvTQLANDLAAqkt 1290
Cdd:pfam12128 687 LEAQLKQLdkkhQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE-TWYKRDLAS--- 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1291 klwsesgeflrrLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHA-LQKAQRDCDLLREQYEEEQEVKAEL 1369
Cdd:pfam12128 763 ------------LGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETwLQRRPRLATQLSNIERAISELQQQL 830
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119600132 1370 HRTLSKV---NAEMVQWRMKYENNVIQRTEDLEDAKKELA----IRL-QEAAEAMGVANARNASLERARHQLQLELGDA 1440
Cdd:pfam12128 831 ARLIADTklrRAKLEMERKASEKQQVRLSENLRGLRCEMSklatLKEdANSEQAQGSIGERLAQLEDLKLKRDYLSESV 909
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1463-1676 |
4.70e-04 |
|
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: 44.36 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1463 KALADWKQKHE---ESQALLDASQKEVQALSTELLKLKNTYEESIVGQET--LRRENKNLQEEISNLTNQVRE-GTKNLT 1536
Cdd:pfam09787 7 QELADYKQKAArilQSKEKLIASLKEGSGVEGLDSSTALTLELEELRQERdlLREEIQKLRGQIQQLRTELQElEAQQQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1537 EMEKVKKLIEEEKTEVQVTL---EETEGALERNESKILHFQLELLEAKAELERKLSEKDEEIEnfRRKQQCTIDSLQSSL 1613
Cdd:pfam09787 87 EAESSREQLQELEEQLATERsarREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIE--KLRNQLTSKSQSSSS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119600132 1614 DSEAKSRIevtrlkKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLN 1676
Cdd:pfam09787 165 QSELENRL------HQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKELQGEGSNGTSIN 221
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
954-1912 |
4.98e-04 |
|
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: 45.43 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 954 KLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKN-----LTEEVEFLNEDISK-LNRaakvvqeahqqTLDDLHMEEE 1027
Cdd:TIGR01612 697 KLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNelldiIVEIKKHIHGEINKdLNK-----------ILEDFKNKEK 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1028 KLSSLSKANLKLEQQVDELEGALeQERKARMNCERELHklegNLKlNRESMENLESSQRHLaEELRKKELELSQMNSKVE 1107
Cdd:TIGR01612 766 ELSNKINDYAKEKDELNKYKSKI-SEIKNHYNDQINID----NIK-DEDAKQNYDKSKEYI-KTISIKEDEIFKIINEMK 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1108 NEKGLVaqLQKTVKELQTQiKDLKEKLEAERTTRAKMERE-RADLTQDlaDLNERLEEVGGSSLAQLEITKKQETKFQKL 1186
Cdd:TIGR01612 839 FMKDDF--LNKVDKFINFE-NNCKEKIDSEHEQFAELTNKiKAEISDD--KLNDYEKKFNDSKSLINEINKSIEEEYQNI 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1187 H--RDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQK--LEKDKSDlQLEvddlltrvEQMTRAKANAEKLCT 1262
Cdd:TIGR01612 914 NtlKKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESnlIEKSYKD-KFD--------NTLIDKINELDKAFK 984
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1263 lyEERLHEATAKLDKVTQLANDLaaqKTKLWSESGEFL-RRLEEKEALINQLSREKSNFTRQIEDLrgQLEKETKSQSAL 1341
Cdd:TIGR01612 985 --DASLNDYEAKNNELIKYFNDL---KANLGKNKENMLyHQFDEKEKATNDIEQKIEDANKNIPNI--EIAIHTSIYNII 1057
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1342 AHALQKAQRDCDLLREQYEEEQEVkaelhrtlSKVNAEMVQWRMKYENnviqrtedLEDAKKELAIRLQEaaeamgvana 1421
Cdd:TIGR01612 1058 DEIEKEIGKNIELLNKEILEEAEI--------NITNFNEIKEKLKHYN--------FDDFGKEENIKYAD---------- 1111
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1422 rnaslerarhqlqlelgdalsDLGKVRSAAARLDQKQLQSGKALADWKQKHE----ESQALLDASQKEV-QALSTELLKL 1496
Cdd:TIGR01612 1112 ---------------------EINKIKDDIKNLDQKIDHHIKALEEIKKKSEnyidEIKAQINDLEDVAdKAISNDDPEE 1170
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1497 KNTYEESIVgqeTLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKL-IEEEKTEVQVTLEETEGALERNESKIlhfql 1575
Cdd:TIGR01612 1171 IEKKIENIV---TKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGInLSYGKNLGKLFLEKIDEEKKKSEHMI----- 1242
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1576 ELLEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKME--EDLNEMELQLSCANRQVSEATk 1653
Cdd:TIGR01612 1243 KAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDEniSDIREKSLKIIEDFSEESDIN- 1321
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1654 slgqlQIQiKDLQMQLDDSTQLNSDLKEQVA-VAERRNSL----LQSELEDLRSLQEQTERGRRLSEEElLEATERINLF 1728
Cdd:TIGR01612 1322 -----DIK-KELQKNLLDAQKHNSDINLYLNeIANIYNILklnkIKKIIDEVKEYTKEIEENNKNIKDE-LDKSEKLIKK 1394
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1729 YTQNTSLLSQKKKLEADVarmqkeAEEVVQEC-QNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQK 1807
Cdd:TIGR01612 1395 IKDDINLEECKSKIESTL------DDKDIDECiKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQH 1468
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1808 RLAEAEQMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELT-----YQAEEDKKNLSRMQTQMDK 1882
Cdd:TIGR01612 1469 ILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTellnkYSALAIKNKFAKTKKDSEI 1548
|
970 980 990
....*....|....*....|....*....|
gi 119600132 1883 LQLKVQNYKQQVEVAETQANQYLSKYKKQQ 1912
Cdd:TIGR01612 1549 IIKEIKDAHKKFILEAEKSEQKIKEIKKEK 1578
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1039-1565 |
8.16e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1039 LEQQVDELEGALEQERKArmncERELHKLEGNLKLNRESMENLEssqrHLAEELRKKELELSQmnsKVENEKGLVAQLQK 1118
Cdd:COG3096 517 LRAQLAELEQRLRQQQNA----ERLLEEFCQRIGQQLDAAEELE----ELLAELEAQLEELEE---QAAEAVEQRSELRQ 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1119 TVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVggSSLAQLE---ITKKQETKFQKLHRDMEEATL 1195
Cdd:COG3096 586 QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAM--QQLLEREreaTVERDELAARKQALESQIERL 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1196 H-----FETTSASLKK-----------------------------RHADSLAELEGQVENLQQvkqkLEKDKSDLQL--- 1238
Cdd:COG3096 664 SqpggaEDPRLLALAErlggvllseiyddvtledapyfsalygpaRHAIVVPDLSAVKEQLAG----LEDCPEDLYLieg 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1239 ---EVDDLLTRVEQMTRA-----------------------KANAEKLCTLYEER--LHEATA-------KLDKVTQLAN 1283
Cdd:COG3096 740 dpdSFDDSVFDAEELEDAvvvklsdrqwrysrfpevplfgrAAREKRLEELRAERdeLAEQYAkasfdvqKLQRLHQAFS 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1284 DLAAQKTKLWSEsgeflrrlEEKEALINQLSREKSNFTRQIEDLRGQlekETKSQSALAHA------LQK---------- 1347
Cdd:COG3096 820 QFVGGHLAVAFA--------PDPEAELAALRQRRSELERELAQHRAQ---EQQLRQQLDQLkeqlqlLNKllpqanllad 888
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1348 ---AQRdCDLLREQYEEEQEVKAELHR---TLSKVnAEMVQwrmkyennVIQRT--------EDLEDAKKELAiRLQEAA 1413
Cdd:COG3096 889 etlADR-LEELREELDAAQEAQAFIQQhgkALAQL-EPLVA--------VLQSDpeqfeqlqADYLQAKEQQR-RLKQQI 957
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1414 EAMGVANARNASLERARHQLQLELGDALSDlgKVRSAAARLDQKQLQSGKALADWKQKHEESQALL-------DASQKEV 1486
Cdd:COG3096 958 FALSEVVQRRPHFSYEDAVGLLGENSDLNE--KLRARLEQAEEARREAREQLRQAQAQYSQYNQVLaslkssrDAKQQTL 1035
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1487 QALSTELLKLKNTYEESIVgqETLRRENKNLQEEISNLTNQVREGTKNLT----EMEKVKKLIEEEKTEVQVTLEETEGA 1562
Cdd:COG3096 1036 QELEQELEELGVQADAEAE--ERARIRRDELHEELSQNRSRRSQLEKQLTrceaEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
...
gi 119600132 1563 LER 1565
Cdd:COG3096 1114 KAG 1116
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
992-1138 |
8.78e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 992 EEV--EFLNEDISKLNRAAKVVQEAHQQTLDDlhmEEEKLSSLSKANLKLEQQVDELEGALEQerkarmnCERELHKLEG 1069
Cdd:COG2433 379 EEAleELIEKELPEEEPEAEREKEHEERELTE---EEEEIRRLEEQVERLEAEVEELEAELEE-------KDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119600132 1070 NLKLNRESMEnlessqrhlaEELRKKElELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKE--KLEAER 1138
Cdd:COG2433 449 ELSEARSEER----------REIRKDR-EISRLDREIERLERELEEERERIEELKRKLERLKElwKLEHSG 508
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1115-1372 |
8.97e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 8.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1115 QLQKTVKELQ----TQIKDLKEKLEAERTTrakmereraDLTQDLADLNERLEEVGG-SSLAQLEITKKQETKFQKLhrd 1189
Cdd:PRK05771 17 YKDEVLEALHelgvVHIEDLKEELSNERLR---------KLRSLLTKLSEALDKLRSyLPKLNPLREEKKKVSVKSL--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1190 mEEATLHFETTSASLkkrhADSLAELEGQVENLQQVKQKLEKDKSDLQ------LEVDDLLTR-----------VEQMTR 1252
Cdd:PRK05771 85 -EELIKDVEEELEKI----EKEIKELEEEISELENEIKELEQEIERLEpwgnfdLDLSLLLGFkyvsvfvgtvpEDKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1253 AKANAEKLCTLYEERLHE------ATAK--LDKVTQLANDLAAQKTKLwSESGEFLRRLEEKEALINQLSREksnftrqI 1324
Cdd:PRK05771 160 LKLESDVENVEYISTDKGyvyvvvVVLKelSDEVEEELKKLGFERLEL-EEEGTPSELIREIKEELEEIEKE-------R 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 119600132 1325 EDLRGQLEKETKSqsalahaLQKAQRDCDLLREQYEEEQEVKAELHRT 1372
Cdd:PRK05771 232 ESLLEELKELAKK-------YLEELLALYEYLEIELERAEALSKFLKT 272
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1475-1732 |
1.10e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1475 SQALLDASQKEVQA-LSTELLKLKNTyeesivgqETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEvQ 1553
Cdd:PRK11281 50 KQKLLEAEDKLVQQdLEQTLALLDKI--------DRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLS-T 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1554 VTLEETEGALERNESKILHFQLELLEAKAEL-------ERKLSEKDEeieNFRRKQQctIDSLQSSLDSEAKSRIEVTRL 1626
Cdd:PRK11281 121 LSLRQLESRLAQTLDQLQNAQNDLAEYNSQLvslqtqpERAQAALYA---NSQRLQQ--IRNLLKGGKVGGKALRPSQRV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1627 KKKMEE-------DLNEMELQ-----LSCANRQVSEATKSLGQLQIQIKDLQ-----MQLDDSTQLNSDLKE-QVAVAER 1688
Cdd:PRK11281 196 LLQAEQallnaqnDLQRKSLEgntqlQDLLQKQRDYLTARIQRLEHQLQLLQeainsKRLTLSEKTVQEAQSqDEAARIQ 275
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 119600132 1689 RNSLLQSELEdlrslqeqteRGRRLSEEeLLEATERINLFYTQN 1732
Cdd:PRK11281 276 ANPLVAQELE----------INLQLSQR-LLKATEKLNTLTQQN 308
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1645-1898 |
1.20e-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: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1645 NRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQ---VAVAERRNSLLQsELEDLRSLQEQTERGRRLSEEELLEA 1721
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglVDLSEEAKLLLQ-QLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1722 TERINLFYTQNTSLLS--QKKKLEADVARMQKEAEEvvqecqnaeekakkaaieaanLSEELKKKQDTIAHLERTRENME 1799
Cdd:COG3206 246 RAQLGSGPDALPELLQspVIQQLRAQLAELEAELAE---------------------LSARYTPNHPDVIALRAQIAALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1800 QTITDLQKRLAEAEQMALMGSRKQIQKLESRVRelegELEGEIRRSAEAQRGARRLERcikeltyQAEEDKKNLSRMQTQ 1879
Cdd:COG3206 305 AQLQQEAQRILASLEAELEALQAREASLQAQLA----QLEARLAELPELEAELRRLER-------EVEVARELYESLLQR 373
|
250
....*....|....*....
gi 119600132 1880 MDKLQLKVQNYKQQVEVAE 1898
Cdd:COG3206 374 LEEARLAEALTVGNVRVID 392
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1062-1193 |
1.24e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1062 RELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMnskveneKGLVAQLQKTVKELQTQIKDLKEKLEAERTTR 1141
Cdd:PRK09039 60 SQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRL-------QALLAELAGAGAAAEGRAGELAQELDSEKQVS 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 119600132 1142 AKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDMEEA 1193
Cdd:PRK09039 133 ARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVA 184
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1631-1944 |
1.26e-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: 44.01 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1631 EEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSlqeqterg 1710
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELES-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1711 rRLSEEElleatERinlfytqNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAH 1790
Cdd:pfam01576 83 -RLEEEE-----ER-------SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1791 LERTRENMEQTITDLQKRLAEAEQMALMGSrKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDK 1870
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLS-KLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119600132 1871 KNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQ 1944
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELE 302
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
871-1141 |
1.35e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.74 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 871 LQKALEKSEFQREELKAKQVSLTqeKNDLILQLQAEQEtlANVEEQCEWLIKSKIQLEARVKELSERVEEEEEINSELTA 950
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLS--ETDARIKLAAQEK--IHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 951 RGRKLEDECFELKKEID---DLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRA------AKVvqEAHQQTLDD 1021
Cdd:PLN02939 234 ENMLLKDDIQFLKAELIevaETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLqydcwwEKV--ENLQDLLDR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1022 LHMEEEKLSSLSKANLKLEQQVDELEGALEqerkarmncerelhklEGNL-KLNRESMENLESSQRHLAEELRKKELEls 1100
Cdd:PLN02939 312 ATNQVEKAALVLDQNQDLRDKVDKLEASLK----------------EANVsKFSSYKVELLQQKLKLLEERLQASDHE-- 373
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 119600132 1101 qMNSKVEnekglvaQLQKTVKELQTQIKDLKEklEAERTTR 1141
Cdd:PLN02939 374 -IHSYIQ-------LYQESIKEFQDTLSKLKE--ESKKRSL 404
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1463-1812 |
1.56e-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: 43.89 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1463 KALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETlrrenKNLQEEISNLTNQVR--------EGTKN 1534
Cdd:TIGR01612 620 KKAIDLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIYSTIKSELS-----KIYEDDIDALYNELSsivkenaiDNTED 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1535 LTEMEKVKKLIEEEKTEVQ----VTLEETEGALERNESKILHFqleLLEAKAELERKLS-EKDEEIENFRRKQQctidSL 1609
Cdd:TIGR01612 695 KAKLDDLKSKIDKEYDKIQnmetATVELHLSNIENKKNELLDI---IVEIKKHIHGEINkDLNKILEDFKNKEK----EL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1610 QSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLK----EQVAV 1685
Cdd:TIGR01612 768 SNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKfmkdDFLNK 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1686 AERRNSLLQSELEDLRSLQEQ-TERGRRLSEEElleATERINLF---YTQNTSLLSQ-KKKLEADVARMQ--KEAEEVVQ 1758
Cdd:TIGR01612 848 VDKFINFENNCKEKIDSEHEQfAELTNKIKAEI---SDDKLNDYekkFNDSKSLINEiNKSIEEEYQNINtlKKVDEYIK 924
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 119600132 1759 ECQNAEEKAKKAAIEAANLSEELKKKQDTIAH---LERTREN-MEQTITDLQKRLAEA 1812
Cdd:TIGR01612 925 ICENTKESIEKFHNKQNILKEILNKNIDTIKEsnlIEKSYKDkFDNTLIDKINELDKA 982
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
944-1319 |
1.60e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 944 INSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEhkvKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDdlH 1023
Cdd:pfam12128 630 ANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKN---KALAERKDSANERLNSLEAQLKQLDKKHQAWLE--E 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1024 MEEEKLSSLSKANLKL----------EQQVDELEGALEQERKARMN-CERELHKLEGNLKLNRESMENLESSQRHLA--- 1089
Cdd:pfam12128 705 QKEQKREARTEKQAYWqvvegaldaqLALLKAAIAARRSGAKAELKaLETWYKRDLASLGVDPDVIAKLKREIRTLErki 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1090 EELRKKELELSQ----MNSKVENEK-GLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEE 1164
Cdd:pfam12128 785 ERIAVRRQEVLRyfdwYQETWLQRRpRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRG 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1165 VggsslaQLEITKkqeTKFQKLHRDMEEATLHFETTSASLKkrhaDSLAELEGQVEnlqQVKQKLEKDKSDLQLEVDDLL 1244
Cdd:pfam12128 865 L------RCEMSK---LATLKEDANSEQAQGSIGERLAQLE----DLKLKRDYLSE---SVKKYVEHFKNVIADHSGSGL 928
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1245 TRVEQMTRAKA---NAEKLCTLYEERLheatakLDKVTQLANDLAAQKTKLWSESG--------EFLRRLEEKEALINQL 1313
Cdd:pfam12128 929 AETWESLREEDhyqNDKGIRLLDYRKL------VPYLEQWFDVRVPQSIMVLREQVsilgvdltEFYDVLADFDRRIASF 1002
|
....*.
gi 119600132 1314 SREKSN 1319
Cdd:pfam12128 1003 SRELQR 1008
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
780-1237 |
1.67e-03 |
|
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: 43.59 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 780 GFLGQLEAIRDERLSKVFTLFQARAQGKLMRIKFQKILEERDALILIQWNIRAFMAVKNWPWmrlFFKIKPLVKSSEVGE 859
Cdd:pfam07111 173 GLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQVPPE---VHSQTWELERQELLD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 860 EVAGLKEECAQLQKALEKSEFQREELKAKqvsLTQEKNDLILQLQAEQETLANVEEQCEWLIKSkiqlearvkelseRVE 939
Cdd:pfam07111 250 TMQHLQEDRADLQATVELLQVRVQSLTHM---LALQEEELTRKIQPSDSLEPEFPKKCRSLLNR-------------WRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 940 EEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTL 1019
Cdd:pfam07111 314 KVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1020 DDLHMEEEKL----SSLSKANLKLEQQVDELEGALEQ--ERKARMN-CERELHKLEGnLKLNRESMENLESSQRHLAEEL 1092
Cdd:pfam07111 394 QQTASAEEQLkfvvNAMSSTQIWLETTMTRVEQAVARipSLSNRLSyAVRKVHTIKG-LMARKVALAQLRQESCPPPPPA 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1093 RKKELELS-QMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAK----MERERADLTQDLADLNERLEEV-- 1165
Cdd:pfam07111 473 PPVDADLSlELEQLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEvaqqLEQELQRAQESLASVGQQLEVArq 552
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119600132 1166 -------GGSSLAQlEITKKQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQ 1237
Cdd:pfam07111 553 gqqesteEAASLRQ-ELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQ 630
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
860-1410 |
1.72e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 860 EVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDL---ILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSE 936
Cdd:PRK01156 198 ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLksaLNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 937 RVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLvksekekrttehkvKNLTEEVeflnedisklnraakvvqeahq 1016
Cdd:PRK01156 278 LEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQIL--------------SNIDAEI---------------------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1017 QTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKE 1096
Cdd:PRK01156 322 NKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1097 LELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRA------------------KMERERADLTQDLADL 1158
Cdd:PRK01156 402 IDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlgeeKSNHIINHYNEKKSRL 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1159 NERLEEVggsslaQLEITKKQETKFQ--KLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDL 1236
Cdd:PRK01156 482 EEKIREI------EIEVKDIDEKIVDlkKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRY 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1237 Q-LEVDDLLTRVEQMTRAKANAEKL-CTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLS 1314
Cdd:PRK01156 556 KsLKLEDLDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKY 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1315 REKSNFTRQIEDLRGQLEkETKSQSALAHALQKAQRDcdlLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNvIQR 1394
Cdd:PRK01156 636 NEIQENKILIEKLRGKID-NYKKQIAEIDSIIPDLKE---ITSRINDIEDNLKKSRKALDDAKANRARLESTIEIL-RTR 710
|
570
....*....|....*.
gi 119600132 1395 TEDLEDAKKELAIRLQ 1410
Cdd:PRK01156 711 INELSDRINDINETLE 726
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1060-1172 |
1.80e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1060 CERELHKLEGNL-KLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKtvkelqtqikdLKEKLEAER 1138
Cdd:COG0542 416 LERRLEQLEIEKeALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQE-----------LKEELEQRY 484
|
90 100 110
....*....|....*....|....*....|....*
gi 119600132 1139 TTRAKMERERADLTQDLADLNERL-EEVGGSSLAQ 1172
Cdd:COG0542 485 GKIPELEKELAELEEELAELAPLLrEEVTEEDIAE 519
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
1505-1724 |
1.82e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 42.71 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1505 VGQETLRReNKNLQEEISNLTNQVREGTKNLT----EMEKVKKLI-------EEEKTEvqvtlEETEGALERNESKILHF 1573
Cdd:pfam04849 88 IGQSLLKQ-NSVLTERNEALEEQLGSAREEILqlrhELSKKDDLLqiysndaEESETE-----SSCSTPLRRNESFSSLH 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1574 QLELLEAkaeLERKLSEKDEEIEnfrrkqqctidslqsSLDSEA-KSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEAT 1652
Cdd:pfam04849 162 GCVQLDA---LQEKLRGLEEENL---------------KLRSEAsHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1653 KSLG--------------QLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEEL 1718
Cdd:pfam04849 224 EELArkmeenlrqqeeitSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEEL 303
|
....*.
gi 119600132 1719 LEATER 1724
Cdd:pfam04849 304 KELRKK 309
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
982-1134 |
2.09e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 42.72 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 982 TTEHKVKNLTEEVEFLNEDISKLNRAAKVVqeA----HQQTLDDLHmeeeklsslSKANLKLEQQVDELEGALEQERKAR 1057
Cdd:smart00435 232 TLQEQLKELTAKDGNVAEKILAYNRANREV--AilcnHQRTVSKTH---------EKSMEKLQEKIKALKYQLKRLKKMI 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119600132 1058 MNCERElhklegnlklnRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDlKEKL 1134
Cdd:smart00435 301 LLFEMI-----------SDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEKKKKQIERLEERIEKLEVQATD-KEEN 365
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
854-1223 |
2.09e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 43.40 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 854 SSEVGE-EVAGLKEECaqlqKALEKSEFQREelkaKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQL--EAR 930
Cdd:pfam15818 86 ATEIKEkEIEGLKETL----KALQVSKYSLQ----KKVSEMEQKLQLHLLAKEDHHKQLNEIEKYYATITGQFGLvkENH 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 931 VKELSERVEEEEeINSELTARGRKLEDECFELKKEIDDLETMLVKSekeKRTTEHKVK----NLTEEVEFLNEDISKLNR 1006
Cdd:pfam15818 158 GKLEQNVQEAIQ-LNKRLSALNKKQESEICSLKKELKKVTSDLIKS---KVTCQYKMGeeniNLTIKEQKFQELQERLNM 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1007 AAKVVQEAHQQTLddlHMEEEK---LSSLSKANLKLEQQVD---ELEGALEQERKARMNCERELHKLEGNLKLNRESMEN 1080
Cdd:pfam15818 234 ELELNKKINEEIT---HIQEEKqdiIISFQHMQQLLQQQTQantEMEAELKALKENNQTLERDNELQREKVKENEEKFLN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1081 LESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERttrakmereradlTQDLADLNe 1160
Cdd:pfam15818 311 LQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKK-------------FQNVPEVN- 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119600132 1161 rlEEVGGSSLAQLEITKKQetKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQ 1223
Cdd:pfam15818 377 --NENSEMSTEKSENLIIQ--KYNSEQEIREENTKSFCSDTEYRETEKKKGPPVEEIIIEDLQ 435
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
859-1147 |
2.16e-03 |
|
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: 42.82 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 859 EEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQaeqetlanveeqcEWLIKSKIQLEARVKELSERV 938
Cdd:pfam09731 173 AEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAP-------------ETPPKLPEHLDNVEEKVEKAQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 939 EEEEEIN--SELTARGRKLEDEcfELKKEIDDLETMLVKSEKEKRTTEHK-VKNLTEEVEFLNEDISKLNRAAkvvQEAH 1015
Cdd:pfam09731 240 SLAKLVDqyKELVASERIVFQQ--ELVSIFPDIIPVLKEDNLLSNDDLNSlIAHAHREIDQLSKKLAELKKRE---EKHI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1016 QQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKarmncerelhklegnLKLNRESMENL---------ESSQR 1086
Cdd:pfam09731 315 ERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFERE---------------REEIRESYEEKlrtelerqaEAHEE 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119600132 1087 HLAEELRKKELEL-----SQMNSKVENEKGLvaqLQKTVKELQTQIKDLKEKLEAerttRAKMERE 1147
Cdd:pfam09731 380 HLKDVLVEQEIELqreflQDIKEKVEEERAG---RLLKLNELLANLKGLEKATSS----HSEVEDE 438
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1337-1562 |
2.41e-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: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1337 SQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRmKYENNVIQRTEDLEDAKKELAIRLQEAAEAM 1416
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1417 GVANARNASLERARHQLQL--------ELGDALSDLGKVRSAAARlDQKQLQSGKALadwKQKHEESQALLDASQKEVQA 1488
Cdd:COG3883 86 EELGERARALYRSGGSVSYldvllgseSFSDFLDRLSALSKIADA-DADLLEELKAD---KAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119600132 1489 LSTELLKLKNTYEESIVGQE----TLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGA 1562
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEallaQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1436-1946 |
2.83e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1436 ELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTEL------------LKLKNTYEES 1503
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLeldgfergpfseRQIKNFHTLV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1504 IVGQEtlrRENKNLQEEISNLTNQVREGTKNLTEmekvkklIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAE 1583
Cdd:TIGR00606 400 IERQE---DEAKTAAQLCADLQSKERLKQEQADE-------IRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGS 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1584 LERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKS----RIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQ 1659
Cdd:TIGR00606 470 SDRILELDQELRKAERELSKAEKNSLTETLKKEVKSlqneKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDE 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1660 iQIKDLQMQLDDS----------TQLNSD----LKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEateri 1725
Cdd:TIGR00606 550 -QIRKIKSRHSDEltsllgyfpnKKQLEDwlhsKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSS----- 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1726 nlfYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDL 1805
Cdd:TIGR00606 624 ---YEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDL 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1806 QKRLAEAEQmalmgsrkQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQL 1885
Cdd:TIGR00606 701 QSKLRLAPD--------KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET 772
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119600132 1886 KVQNYKQQVEVAET-QANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQEE 1946
Cdd:TIGR00606 773 LLGTIMPEEESAKVcLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEK 834
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
859-1138 |
2.86e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 859 EEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEArvkelserv 938
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA--------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 939 eeeeeinseltargrkledecfELKKEIDDLETMLVKSEKEKRTTEHKVKnlteeveFLNEDISKLNRAAKVVQEAHQQT 1018
Cdd:COG4942 98 ----------------------ELEAQKEELAELLRALYRLGRQPPLALL-------LSPEDFLDAVRRLQYLKYLAPAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1019 LDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQerkarmncerelhklegnlklnresmenLESSQRHLAEELRKKELE 1098
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERAELEALLAE----------------------------LEEERAALEALKAERQKL 200
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 119600132 1099 LSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAER 1138
Cdd:COG4942 201 LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1340-1570 |
2.93e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1340 ALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQwrmkYENNVIQRTEDLEDAKKELAIRLQEAAEAMGVA 1419
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1420 NARNASLERARHQLQlELGDALSDLGKVRSAAARLDQKQLQSGKALADWkqkheeSQALLDASQKEVQALSTELLKLKNT 1499
Cdd:COG4942 93 AELRAELEAQKEELA-ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY------LKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119600132 1500 YEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKI 1570
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1081-1396 |
3.00e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1081 LESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERadltQDLADLNE 1160
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKY----KELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1161 RLEEVGGSSLAQLEitkkqetkfqklhrDMEEATLHFETTSASLKKRHADSLAELE---GQVENLQQVKQKLEKDKSDLQ 1237
Cdd:pfam07888 112 ELSEEKDALLAQRA--------------AHEARIRELEEDIKTLTQRVLERETELErmkERAKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1238 LEvddLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKtklwsesgeflRRLEEKEALINQLS--R 1315
Cdd:pfam07888 178 AK---LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH-----------RKEAENEALLEELRslQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1316 EKSNFT-RQIEDLRGQLEkETKSQSALAHA------LQKAQRDCDL--LREQYEEEQEVKAELHRTLSKvNAEMVQWRMK 1386
Cdd:pfam07888 244 ERLNASeRKVEGLGEELS-SMAAQRDRTQAelhqarLQAAQLTLQLadASLALREGRARWAQERETLQQ-SAEADKDRIE 321
|
330
....*....|
gi 119600132 1387 YENNVIQRTE 1396
Cdd:pfam07888 322 KLSAELQRLE 331
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1006-1165 |
3.11e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1006 RAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQ 1085
Cdd:COG1196 651 LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1086 RHLAEELRKKELELSQMNSKVENEKGL----VAQLQKTVKELQTQIKDL-------KEKLEAERTTRAKMERERADLTQD 1154
Cdd:COG1196 731 EAEREELLEELLEEEELLEEEALEELPeppdLEELERELERLEREIEALgpvnllaIEEYEELEERYDFLSEQREDLEEA 810
|
170
....*....|.
gi 119600132 1155 LADLNERLEEV 1165
Cdd:COG1196 811 RETLEEAIEEI 821
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
1447-1546 |
3.15e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 41.64 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1447 VRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTN 1526
Cdd:COG4026 112 IKNAIIRAGLKSLQNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKS 191
|
90 100
....*....|....*....|
gi 119600132 1527 QVREGTKNLTEMEKvKKLIE 1546
Cdd:COG4026 192 EYSDLKSRFEELLK-KRLLE 210
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1393-1744 |
3.22e-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: 42.42 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1393 QRTEDLEDAKKElaiRLQEAAEAMGVANARNASLERARHQLQLELGdalsdlgkvRSAAARLDQKQLQSGKALADWKQKH 1472
Cdd:pfam17380 288 QQQEKFEKMEQE---RLRQEKEEKAREVERRRKLEEAEKARQAEMD---------RQAAIYAEQERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1473 EESQALLDASQKEVQALST------ELLKLKNTYEESIVGQETLRRENKNLQEEisnltNQVREGTKNLTEMEKVKKLIE 1546
Cdd:pfam17380 356 EERKRELERIRQEEIAMEIsrmrelERLQMERQQKNERVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQIRAEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1547 EEKT-EVQVTLEETEGALE--RNESKILHFQLELL-EAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIE 1622
Cdd:pfam17380 431 EARQrEVRRLEEERAREMErvRLEEQERQQQVERLrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1623 VTRLKKKMEEdlnEMElqlscanrqvseatkslgqlqiqikdlqmqlDDSTQLNSDLKEQVAVAERRNsllQSELEDLRS 1702
Cdd:pfam17380 511 EERKRKLLEK---EME-------------------------------ERQKAIYEEERRREAEEERRK---QQEMEERRR 553
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 119600132 1703 LQEQTergRRLSEEE-LLEATERINLFYTQNTSLLSQKKKLEA 1744
Cdd:pfam17380 554 IQEQM---RKATEERsRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1674-1946 |
3.28e-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: 42.42 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1674 QLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATErinlfyTQNTSLLSQKKKLEADVARMQKEA 1753
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE------KARQAEMDRQAAIYAEQERMAMER 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1754 EEVVQECQNAEEKAKKAAIEAANLSEELKKkqdtIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQiqklesRVRE 1833
Cdd:pfam17380 347 ERELERIRQEERKRELERIRQEEIAMEISR----MRELERLQMERQQKNERVRQELEAARKVKILEEERQ------RKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1834 LEGELEGEIRRSAEA--QRGARRLErcikeltyqaEEDKKNLSRMQTQMDKLQLKVQNYKQQvEVAETQANQYLSKYKKQ 1911
Cdd:pfam17380 417 QQKVEMEQIRAEQEEarQREVRRLE----------EERAREMERVRLEEQERQQQVERLRQQ-EEERKRKKLELEKEKRD 485
|
250 260 270
....*....|....*....|....*....|....*
gi 119600132 1912 QHELNEVKERAEVAESQVNKLKIKAREFGKKVQEE 1946
Cdd:pfam17380 486 RKRAEEQRRKILEKELEERKQAMIEEERKRKLLEK 520
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1275-1590 |
3.51e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1275 LDKVTQLANDLAAQKTKLwsesgeflRRLEEKEAliNQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDL 1354
Cdd:pfam00038 17 IDKVRFLEQQNKLLETKI--------SELRQKKG--AEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1355 LREQYEEE----QEVKAELHrTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKelaIRLQEAAEAMGVANARNASLERaR 1430
Cdd:pfam00038 87 FRQKYEDElnlrTSAENDLV-GLRKDLDEATLARVDLEAKIESLKEELAFLKK---NHEEEVRELQAQVSDTQVNVEM-D 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1431 HQLQLELGDALSDLGKVRSAAARLDQKQLQsgkalADWKQKHEESQALLDASQKEVQALSTELLKLKNTYeesivgqETL 1510
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAE-----EWYQSKLEELQQAAARNGDALRSAKEEITELRRTI-------QSL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1511 RRENKNLQEEISNLTNQVREgtknltemekvkklieeektevqvtLEET-EGALERNESKILHFQLELLEAKAELERKLS 1589
Cdd:pfam00038 230 EIELQSLKKQKASLERQLAE-------------------------TEERyELQLADYQELISELEAELQETRQEMARQLR 284
|
.
gi 119600132 1590 E 1590
Cdd:pfam00038 285 E 285
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
947-1558 |
3.59e-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: 42.73 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 947 ELTARGRKLEDECFELKKEIDDLETMLVKS-------EKEKR-----TTEHKVKNLTEEVEFLNEDISKLNRAAKVVQE- 1013
Cdd:TIGR01612 1133 ALEEIKKKSENYIDEIKAQINDLEDVADKAisnddpeEIEKKienivTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEv 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1014 -----AHQQTLDDLHME---EEKLSS--LSKANLKLEQQVDELEGAlEQERKARMNCERELHKLEGNLKL-NRESMENLE 1082
Cdd:TIGR01612 1213 kginlSYGKNLGKLFLEkidEEKKKSehMIKAMEAYIEDLDEIKEK-SPEIENEMGIEMDIKAEMETFNIsHDDDKDHHI 1291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1083 SSQRH--LAEELRKKELELSQMNS----------------------------------------KVENEKGLVAQLQKTV 1120
Cdd:TIGR01612 1292 ISKKHdeNISDIREKSLKIIEDFSeesdindikkelqknlldaqkhnsdinlylneianiynilKLNKIKKIIDEVKEYT 1371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1121 KELQTQIKDLKEKLEAERTTRAKME--------RERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDMEE 1192
Cdd:TIGR01612 1372 KEIEENNKNIKDELDKSEKLIKKIKddinleecKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNEN 1451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1193 ATLHFETTS-ASLKKRHADSLAELEGQVE---NLQQVKQKLEKDKSdLQLEVDdlltrveqmtRAKANAEKLCTLYEERL 1268
Cdd:TIGR01612 1452 VLLLFKNIEmADNKSQHILKIKKDNATNDhdfNINELKEHIDKSKG-CKDEAD----------KNAKAIEKNKELFEQYK 1520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1269 HEATAKLDKVTQLANDLAAQKTKlwsesgeflrrlEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKa 1348
Cdd:TIGR01612 1521 KDVTELLNKYSALAIKNKFAKTK------------KDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAK- 1587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1349 qrdcdllreqyeEEQEVKAELHRTLSKVNAEMVQWRM----KYENNVIQRTEDLEDAKKELAIRLQEAAEAmgvanarna 1424
Cdd:TIGR01612 1588 ------------NDKSNKAAIDIQLSLENFENKFLKIsdikKKINDCLKETESIEKKISSFSIDSQDTELK--------- 1646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1425 slerarhqlqlELGDALSDLgkvrsaaarldQKQLQSgkaLADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESI 1504
Cdd:TIGR01612 1647 -----------ENGDNLNSL-----------QEFLES---LKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGI 1701
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119600132 1505 VgqETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKL--------IEEEKTEVQVTLEE 1558
Cdd:TIGR01612 1702 I--EKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLegidpnekLEEYNTEIGDIYEE 1761
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1693-1930 |
3.59e-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: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1693 LQSELEDLRSLQEQTERGRRlsEEELLEATERINLFYTQNTSLLSQKKKLEA--DVARMQKEAEEVVQECQNaeekakka 1770
Cdd:COG4913 230 LVEHFDDLERAHEALEDARE--QIELLEPIRELAERYAAARERLAELEYLRAalRLWFAQRRLELLEAELEE-------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1771 aieaanLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQmalmgsrKQIQKLEsrvreleGELEGEIRRSAEAQR 1850
Cdd:COG4913 300 ------LRAELARLEAELERLEARLDALREELDELEAQIRGNGG-------DRLEQLE-------REIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1851 GARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEvkERAEVAESQVN 1930
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA--EIASLERRKSN 437
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
972-1677 |
3.87e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.48 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 972 MLVKSEKEKRTTEHKVKNLTEEVEFLNED-ISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANlKLEQQVDELEGAL 1050
Cdd:PRK10246 188 MVFEQHKSARTELEKLQAQASGVALLTPEqVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLD-ELQQEASRRQQAL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1051 EQERKARMNCERELHKLEgnLKLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQL----QKTVKELQTQ 1126
Cdd:PRK10246 267 QQALAAEEKAQPQLAALS--LAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIrhhaAKQSAELQAQ 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1127 IKDLKEKLEAE-------------RTTRAKMERERADL---TQDLADLNERLEEVGGSSL--------AQLEITKKQETK 1182
Cdd:PRK10246 345 QQSLNTWLAEHdrfrqwnnelagwRAQFSQQTSDREQLrqwQQQLTHAEQKLNALPAITLtltadevaAALAQHAEQRPL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1183 FQKLhrdmeeATLHfeTTSASLKKRhadsLAELEGQVENLQQVKQKLE----------KDKSDLQLEVDDLLTRVEQMT- 1251
Cdd:PRK10246 425 RQRL------VALH--GQIVPQQKR----LAQLQVAIQNVTQEQTQRNaalnemrqryKEKTQQLADVKTICEQEARIKd 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1252 ----RAKANAEKLCTLYEERLHEATAKLDKVTQLAN----DLAAQKTKLWSESGEFLRrlEEKEALINQLSREKSNFTRQ 1323
Cdd:PRK10246 493 leaqRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNqsrlDALEKEVKKLGEEGAALR--GQLDALTKQLQRDESEAQSL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1324 IEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVK--AELHRTLSKVNAEMVQWRmKYENNVIQRTEDLEDA 1401
Cdd:PRK10246 571 RQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRllSQRHELQGQIAAHNQQII-QYQQQIEQRQQQLLTA 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1402 KKELAIRLQEAAEAMGVANAR--NASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALAD-WKQKHEESQAL 1478
Cdd:PRK10246 650 LAGYALTLPQEDEEASWLATRqqEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDnWRQVHEQCLSL 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1479 ldasQKEVQALSTELLKLKNTYEESIVgQETLRRENKNLQEEISNLTNQVREGTknLTEMEKVKKLIEEEKTEVQVTLEE 1558
Cdd:PRK10246 730 ----HSQLQTLQQQDVLEAQRLQKAQA-QFDTALQASVFDDQQAFLAALLDEET--LTQLEQLKQNLENQRQQAQTLVTQ 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1559 TEGALERNeskilhfqlelleakaelerklsekdeeienfrrkQQCTIDSLQSSLDSEaKSRIEVTRLKKKMEEDLN--- 1635
Cdd:PRK10246 803 TAQALAQH-----------------------------------QQHRPDGLDLTVTVE-QIQQELAQLAQQLRENTTrqg 846
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 119600132 1636 EMELQLscanRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNS 1677
Cdd:PRK10246 847 EIRQQL----KQDADNRQQQQALMQQIAQATQQVEDWGYLNS 884
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1076-1375 |
3.88e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 41.60 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1076 ESMENLESSQRHLAEELRKKELELSQMNSKVENekgLVAQLQKTVKELQTQIKDLKEKLEaerttraKMERERADLTQDL 1155
Cdd:pfam04108 3 SSAQDLCRWANELLTDARSLLEELVVLLAKIAF---LRRGLSVQLANLEKVREGLEKVLN-------ELKKDFKQLLKDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1156 ADLNERLEEVggsslaqLEITKKQETKFQKLHRDMEEATLH-F--ETTSASLKKRHADSLAELEGQVENLQQVKQKLEKD 1232
Cdd:pfam04108 73 DAALERLEET-------LDKLRNTPVEPALPPGEEKQKTLLdFidEDSVEILRDALKELIDELQAAQESLDSDLKRFDDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1233 KSDLQLEVDDLLTRveqmTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQ 1312
Cdd:pfam04108 146 LRDLQKELESLSSP----SESISLIPTLLKELESLEEEMASLLESLTNHYDQCVTAVKLTEGGRAEMLEVLENDARELDD 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119600132 1313 LSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSK 1375
Cdd:pfam04108 222 VVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQLIAEIQSRLPEYLAALKEFEERWEE 284
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1144-1361 |
3.92e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1144 MERERADLTQDLADLNERLEEVGgsslAQLEITKKQETKFQKLHR--DMEEATLHFETTSASLKKRHADSLAELEGQVEN 1221
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELR----KELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1222 LQQVKQKLEKDKSDLQLEVDDllTRVEQMTRAKANAEKLCTLYEERLheaTAKLDKVTQLANDLAAQKTKLWSESGeflR 1301
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARY---TPNHPDVIALRAQIAALRAQLQQEAQ---R 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1302 RLEEKEALINQLSREKSNFTRQIEDLRGQLeketKSQSALAHALQKAQRDCDLLREQYEE 1361
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYES 369
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
859-1305 |
3.93e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 859 EEVAGLKEECAQLQKALEKSEFQREELKAKQ--------VSLTQEKNDLILQLQAEQETLANVEEQCEWL----IKSKIQ 926
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARLEALLAALglplPASAEE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 927 LEARVKELSERVEEEEEINSELTARGRKLEDECFELKKEIDDLetmlvksEKEKRTTEHKVKNLTEEVEF----LNEDIS 1002
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL-------EAEIASLERRKSNIPARLLAlrdaLAEALG 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1003 KLNRAAKVVQEAHQQTLDD----------LH-------MEEEKLSSLSKA--NLKLEQQVDELEGALEQERKARMNCERE 1063
Cdd:COG4913 455 LDEAELPFVGELIEVRPEEerwrgaiervLGgfaltllVPPEHYAAALRWvnRLHLRGRLVYERVRTGLPDPERPRLDPD 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1064 --LHKLEG---------NLKLNR-------ESMENLESSQRHLAEE-LRKKELELSQMNSKVENEKGLV---------AQ 1115
Cdd:COG4913 535 slAGKLDFkphpfrawlEAELGRrfdyvcvDSPEELRRHPRAITRAgQVKGNGTRHEKDDRRRIRSRYVlgfdnraklAA 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1116 LQKTVKELQTQIKDLKEKLEAERTTRAKMeRERADLTQDLADLNERLEEVGGsslAQLEITKKQETKfqklhRDMEEATL 1195
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYSWDEIDVAS---AEREIAELEAEL-----ERLDASSD 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1196 HFETtsasLKKRhadsLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLY-----EERLHE 1270
Cdd:COG4913 686 DLAA----LEEQ----LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElrallEERFAA 757
|
490 500 510
....*....|....*....|....*....|....*...
gi 119600132 1271 ATAKL---DKVTQLANDLAAQKTKLWSESGEFLRRLEE 1305
Cdd:COG4913 758 ALGDAverELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1039-1176 |
4.35e-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: 41.25 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1039 LEQQVDELEGALEQERKARMNCERE---LHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNS----------- 1104
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAEldrLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIdlarrrvlapi 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119600132 1105 ------KVENEKGLVAQLQKTVKELQTQI-KDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVgGSSLAQLEIT 1176
Cdd:pfam00529 136 ggisreSLVTAGALVAQAQANLLATVAQLdQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLA-KLDLERTEIR 213
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1393-1621 |
4.36e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1393 QRTEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSDL----GKVRSAAARLDQKQLQSGKALADW 1468
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIraleQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1469 KQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEE 1548
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119600132 1549 KTEVQVTLEETEGALERNESKILHFQLELLEAK---AELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRI 1621
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAaelAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
894-1250 |
4.48e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 894 QEKNDLilqLQAEQETLANVEEQCEWLIKSKIQLEARVKELSERVEEEEEI-------NSELTARGRKLEDECFELKKEI 966
Cdd:pfam07888 41 QERAEL---LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEElrqsrekHEELEEKYKELSASSEELSEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 967 DDLETMLVKSEKEKRTTEHKVKNLTE-------EVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKL 1039
Cdd:pfam07888 118 DALLAQRAAHEARIRELEEDIKTLTQrvleretELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1040 EQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKEL---ELSQMNSKVENEKGLVAQL 1116
Cdd:pfam07888 198 RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGlgeELSSMAAQRDRTQAELHQA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1117 QKTVKELQTQIKDLKEKLEAERTTRAKmerERADLTQDLADLNERLEevggsslaqleitkKQETKFQKLHRDMEEATLH 1196
Cdd:pfam07888 278 RLQAAQLTLQLADASLALREGRARWAQ---ERETLQQSAEADKDRIE--------------KLSAELQRLEERLQEERME 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 119600132 1197 FETTSASLKKRHADSLAELEGQVENLQQVKQKL---EKDKSDLQLEVDDLLTRVEQM 1250
Cdd:pfam07888 341 REKLEVELGREKDCNRVQLSESRRELQELKASLrvaQKEKEQLQAEKQELLEYIRQL 397
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1465-1711 |
4.56e-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: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1465 LADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKL 1544
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1545 IEEEKTEVQVTL--EETEGALERNE--SKILHFQLELLEAKAELERKLSEKDEEIENfrrkqqctidslqssldseaksr 1620
Cdd:COG3883 98 SGGSVSYLDVLLgsESFSDFLDRLSalSKIADADADLLEELKADKAELEAKKAELEA----------------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1621 ievtrLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDdstqlnsDLKEQVAVAERRNSLLQSELEDL 1700
Cdd:COG3883 155 -----KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA-------ELEAELAAAEAAAAAAAAAAAAA 222
|
250
....*....|.
gi 119600132 1701 RSLQEQTERGR 1711
Cdd:COG3883 223 AAAAAAAAAAA 233
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
918-1945 |
4.81e-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: 42.35 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 918 EWLIKSKI--QLEARVKELSERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKE-------KRTTEHKVK 988
Cdd:TIGR01612 531 DQNIKAKLykEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEiiyinklKLELKEKIK 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 989 NLTEEVEFLNEDISklnraAKVVQEAHQQTLDDL----------HME-EEKLSSLSKANLK--LEQQVDELEGALEQERK 1055
Cdd:TIGR01612 611 NISDKNEYIKKAID-----LKKIIENNNAYIDELakispyqvpeHLKnKDKIYSTIKSELSkiYEDDIDALYNELSSIVK 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1056 armncERELHKLEGNLKLnresmENLESSQRHLAEELRKKELELSQMN-SKVENEKGlvaQLQKTVKELQTQI-----KD 1129
Cdd:TIGR01612 686 -----ENAIDNTEDKAKL-----DDLKSKIDKEYDKIQNMETATVELHlSNIENKKN---ELLDIIVEIKKHIhgeinKD 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1130 LKEKLEAERTTRAKMERERADLTQDLADLN---ERLEEVGGSSLAQLEI--TKKQETKfqklhRDMEEATLHFETTSASl 1204
Cdd:TIGR01612 753 LNKILEDFKNKEKELSNKINDYAKEKDELNkykSKISEIKNHYNDQINIdnIKDEDAK-----QNYDKSKEYIKTISIK- 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1205 kkrhADSLAELEGQVENLQqvkqklekdksdlqlevDDLLTRVEQMTrakaNAEKLCTLYEERLHEATAKLdkVTQLAND 1284
Cdd:TIGR01612 827 ----EDEIFKIINEMKFMK-----------------DDFLNKVDKFI----NFENNCKEKIDSEHEQFAEL--TNKIKAE 879
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1285 LAAQKTKLWSesgeflRRLEEKEALINQLSREKSNFTRQIEDLRgQLEKETKSQSALAHALQKAQRDCDLLREQYeeEQE 1364
Cdd:TIGR01612 880 ISDDKLNDYE------KKFNDSKSLINEINKSIEEEYQNINTLK-KVDEYIKICENTKESIEKFHNKQNILKEIL--NKN 950
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1365 VKaelhrTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEaaeamgvanARNASLERARHQLQLELGDalsdl 1444
Cdd:TIGR01612 951 ID-----TIKESNLIEKSYKDKFDNTLIDKINELDKAFKDASLNDYE---------AKNNELIKYFNDLKANLGK----- 1011
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1445 GKVRSAAARLDQKQlqsgKALADWKQKHEESQAllDASQKEVqALSTELLKLKNTYEESIvgQETLRRENKNLQEEIS-N 1523
Cdd:TIGR01612 1012 NKENMLYHQFDEKE----KATNDIEQKIEDANK--NIPNIEI-AIHTSIYNIIDEIEKEI--GKNIELLNKEILEEAEiN 1082
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1524 LT--NQVREGTKNLTEMEKVKklieEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRK 1601
Cdd:TIGR01612 1083 ITnfNEIKEKLKHYNFDDFGK----EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDV 1158
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1602 QQCTIdSLQSSLDSEAKSRIEVTRLKKKmEEDLNEMELQLScanrQVSEATKSLGQLQiQIKDLQMQLDDStqLNSDLKE 1681
Cdd:TIGR01612 1159 ADKAI-SNDDPEEIEKKIENIVTKIDKK-KNIYDEIKKLLN----EIAEIEKDKTSLE-EVKGINLSYGKN--LGKLFLE 1229
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1682 QVAVAERRNS----LLQSELEDLRSLQEQTERGRRLSEEELLEATER--INLFYTQNTSLLSQKKKLEADVARMQKEAEE 1755
Cdd:TIGR01612 1230 KIDEEKKKSEhmikAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMetFNISHDDDKDHHIISKKHDENISDIREKSLK 1309
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1756 VVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTR--------ENMEQTITDLQKRLAEAEQM------ALMGSR 1821
Cdd:TIGR01612 1310 IIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIAniynilklNKIKKIIDEVKEYTKEIEENnknikdELDKSE 1389
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1822 KQIQKLESRVrelegeLEGEIRRSAEAQRGARRLERCIKELTY-----------------QAEEDKKNLSRMQTQMDKLQ 1884
Cdd:TIGR01612 1390 KLIKKIKDDI------NLEECKSKIESTLDDKDIDECIKKIKElknhilseesnidtyfkNADENNENVLLLFKNIEMAD 1463
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119600132 1885 LKVQN-YKQQVEVAETQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQE 1945
Cdd:TIGR01612 1464 NKSQHiLKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTE 1525
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1721-1928 |
5.29e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1721 ATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQdtiAHLERTRENMEQ 1800
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1801 TITDLQKRLAEAEQM-ALMGSrKQIQKLESRVrelegeleGEIRRSAEAQRgaRRLERcIKELTYQAEEDKKNLSRMQTQ 1879
Cdd:COG3883 91 RARALYRSGGSVSYLdVLLGS-ESFSDFLDRL--------SALSKIADADA--DLLEE-LKADKAELEAKKAELEAKLAE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 119600132 1880 MDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEVKERAEVAESQ 1928
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1210-1382 |
5.29e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1210 DSLAELEGQVENLQQvKQKLEKD-KSDLQLEVDDLLTRVEQmtrAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQ 1288
Cdd:PRK09039 53 SALDRLNSQIAELAD-LLSLERQgNQDLQDSVANLRASLSA---AEAERSRLQALLAELAGAGAAAEGRAGELAQELDSE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1289 KTklwsESGEFLRRLEekeaLINQlsreksnftrQIEDLRGQLeketksqSALAHALQKAqrdcdllrEQYEEEQEVK-A 1367
Cdd:PRK09039 129 KQ----VSARALAQVE----LLNQ----------QIAALRRQL-------AALEAALDAS--------EKRDRESQAKiA 175
|
170
....*....|....*
gi 119600132 1368 ELHRTLSKVNAEMVQ 1382
Cdd:PRK09039 176 DLGRRLNVALAQRVQ 190
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
888-1253 |
5.58e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.60 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 888 KQVSLTQEKNDLILQ----LQAEQETLANVEEQCEWLIKSKIQLEARVKELSERVEEEEEINSELTARGRKLEDECFELK 963
Cdd:pfam05622 21 QQVSLLQEEKNSLQQenkkLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 964 KEIDDL-----ETMLVKSEKEK-RTTEHKVKNLTEEVEFLN---EDISKLNRAAKVVQEAH----QQTLDdlHMEEEKLS 1030
Cdd:pfam05622 101 HRNEELtslaeEAQALKDEMDIlRESSDKVKKLEATVETYKkklEDLGDLRRQVKLLEERNaeymQRTLQ--LEEELKKA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1031 SLSKANLKL-EQQVDELEGALEQERKARMNCERELHKLEGN---LKLNRESMENLESSQRHLAEELRKKELELSQMNSKV 1106
Cdd:pfam05622 179 NALRGQLETyKRQVQELHGKLSEESKKADKLEFEYKKLEEKleaLQKEKERLIIERDTLRETNEELRCAQLQQAELSQAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1107 ENEKGLVAQLQKTVKELQ-TQIKDLKEKLEAE----RTTRAKMERER-ADLTQDLADLNERLEEVGGSSLAQLEITKKQE 1180
Cdd:pfam05622 259 ALLSPSSDPGDNLAAEIMpAEIREKLIRLQHEnkmlRLGQEGSYRERlTELQQLLEDANRRKNELETQNRLANQRILELQ 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119600132 1181 TKFQKLHRDMEEATLHFETTSASLKK--RHADSLAELEGQVENLQQVKQKLEKD-KSDLQLEVDDL---LTRVEQMTRA 1253
Cdd:pfam05622 339 QQVEELQKALQEQGSKAEDSSLLKQKleEHLEKLHEAQSELQKKKEQIEELEPKqDSNLAQKIDELqeaLRKKDEDMKA 417
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
859-1224 |
5.94e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 859 EEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANV------EEQCEWLIKSKIQLEARVK 932
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVqtalrqQEKIERYQADLEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 933 ELSERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLvkSEKEKRTTE-HKVKNLTEEVEFLNEDISKLNRAAKVV 1011
Cdd:PRK04863 366 EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAL--DVQQTRAIQyQQAVQALERAKQLCGLPDLTADNAEDW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1012 QE---AHQQTLDD-LHMEEEKLSSLSKANlkleqqvDELEGALEQERKARMNCERELHKLEGnlklnRESMENLESsQRH 1087
Cdd:PRK04863 444 LEefqAKEQEATEeLLSLEQKLSVAQAAH-------SQFEQAYQLVRKIAGEVSRSEAWDVA-----RELLRRLRE-QRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1088 LAEELRKKELELSQMNSKVENEKGLVAQLQKTVK-----------------ELQTQIKDLKEKLEAERTTRAKMERERAD 1150
Cdd:PRK04863 511 LAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKrlgknlddedeleqlqeELEARLESLSESVSEARERRMALRQQLEQ 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1151 LTQDLADL----------NERLEEVGGSSLAQLEITKKQETKFQKLHRDMEEATLHfettsaslKKRHADSLAELEGQVE 1220
Cdd:PRK04863 591 LQARIQRLaarapawlaaQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVE--------RDELAARKQALDEEIE 662
|
....
gi 119600132 1221 NLQQ 1224
Cdd:PRK04863 663 RLSQ 666
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1389-1637 |
6.16e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1389 NNVIQRTEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQLELGDAL----SDLGKVRSAAARLD--------- 1455
Cdd:PLN02939 159 EKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLirgaTEGLCVHSLSKELDvlkeenmll 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1456 QKQLQSGKALADWKQKHEES-------QALLDASQKEVQ----ALSTELLKLkntyeeSIVGQETLRRENKNLQEEISNL 1524
Cdd:PLN02939 239 KDDIQFLKAELIEVAETEERvfklekeRSLLDASLRELEskfiVAQEDVSKL------SPLQYDCWWEKVENLQDLLDRA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1525 TNQVREGTKNLTEMEKVKKLIEEektevqvtLEETEGalERNESKILHFQLELLEAKAE-LERKLSEKDEEIENFRRKQQ 1603
Cdd:PLN02939 313 TNQVEKAALVLDQNQDLRDKVDK--------LEASLK--EANVSKFSSYKVELLQQKLKlLEERLQASDHEIHSYIQLYQ 382
|
250 260 270
....*....|....*....|....*....|....
gi 119600132 1604 CTIDSLQSSLdseaKSRIEVTRlKKKMEEDLNEM 1637
Cdd:PLN02939 383 ESIKEFQDTL----SKLKEESK-KRSLEHPADDM 411
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1255-1415 |
6.27e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1255 ANAEKLCTLYEerLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKE 1334
Cdd:COG1579 1 AMPEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1335 TKSQS---------ALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKEL 1405
Cdd:COG1579 79 EEQLGnvrnnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|
gi 119600132 1406 AIRLQEAAEA 1415
Cdd:COG1579 159 EELEAEREEL 168
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
954-1110 |
6.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 954 KLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAK----------VVQEAhqQTLDDLH 1023
Cdd:COG3883 41 ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsggsvsyldVLLGS--ESFSDFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1024 MEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMN 1103
Cdd:COG3883 119 DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
....*..
gi 119600132 1104 SKVENEK 1110
Cdd:COG3883 199 AELEAEL 205
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1076-1231 |
6.52e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 41.36 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1076 ESMENLESSQRHLA--EELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQ----------IKDLKEKLEAERTTRAK 1143
Cdd:pfam15066 302 QSFESLQPLEEDMAlnEVLQKLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKitkqqvfvdiINKLKENVEELIEDKYN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1144 MERERADLTQDLADLNE-------RLEEVGGSSLA-QLEItKKQETKFQKLH-RDMEEatLHFETTSASLKKRHADSLAE 1214
Cdd:pfam15066 382 VILEKNDINKTLQNLQEilantqkHLQESRKEKETlQLEL-KKIKVNYVHLQeRYITE--MQQKNKSVSQCLEMDKTLSK 458
|
170
....*....|....*..
gi 119600132 1215 LEGQVENLQQVKQKLEK 1231
Cdd:pfam15066 459 KEEEVERLQQLKGELEK 475
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
1016-1233 |
6.55e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.89 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1016 QQTLDDLHMeeeKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKK 1095
Cdd:pfam15619 17 QNELAELQS---KLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1096 ELELSQMNSKVenekglvAQLQKTVKElqtqiKDLkekleaerttrakmeRERADLTQDLADLNERLEEvggsslaqlei 1175
Cdd:pfam15619 94 EAELLRLRDQL-------KRLEKLSED-----KNL---------------AEREELQKKLEQLEAKLED----------- 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 119600132 1176 tkkQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKL-EKDK 1233
Cdd:pfam15619 136 ---KDEKIQDLERKLELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLkEKER 191
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1606-1934 |
8.35e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1606 IDSLQSSLDSeakSRIEVTRLKKKMEED---LNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQ 1682
Cdd:PRK01156 185 IDYLEEKLKS---SNLELENIKKQIADDeksHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1683 vavaerrNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAE-----EVV 1757
Cdd:PRK01156 262 -------ESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAiikklSVL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1758 QECQNAEEKAKKAAIEAANLSEELKKKQD-------TIAHLERTRENMEQTITDLQKRLAEAEQMALMGS---------- 1820
Cdd:PRK01156 335 QKDYNDYIKKKSRYDDLNNQILELEGYEMdynsylkSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPdaikkelnei 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1821 RKQIQKLESRV------RELEGELEGEIRRSAEAQRG--------------------------ARRLERCIKELTYQA-- 1866
Cdd:PRK01156 415 NVKLQDISSKVsslnqrIRALRENLDELSRNMEMLNGqsvcpvcgttlgeeksnhiinhynekKSRLEEKIREIEIEVkd 494
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1867 -EEDKKNLSRMQTQMDKLQL-KVQNYKQQVEVAETQanqyLSKYKKQQHELNEVKERAEVAESQVNKLKI 1934
Cdd:PRK01156 495 iDEKIVDLKKRKEYLESEEInKSINEYNKIESARAD----LEDIKIKINELKDKHDKYEEIKNRYKSLKL 560
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1005-1135 |
8.80e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1005 NRAAKVVQEAHQQtlddlhMEEEKlsslSKANLKLEQQVDELEGALEQERKARmncERELHKLEGNLKlNREsmENLESS 1084
Cdd:PRK12704 38 EEAKRILEEAKKE------AEAIK----KEALLEAKEEIHKLRNEFEKELRER---RNELQKLEKRLL-QKE--ENLDRK 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 119600132 1085 QrhlaEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQikdLKEKLE 1135
Cdd:PRK12704 102 L----ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE---QLQELE 145
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1212-1571 |
9.43e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.71 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1212 LAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTK 1291
Cdd:COG5185 189 LKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1292 LWSESGEFLRRLEEkealinqlsrEKSNFTRQIEDLRGQLEKETKSQSALAHALQKaqrdcdllrEQYEEEQEVKAELHR 1371
Cdd:COG5185 269 KLGENAESSKRLNE----------NANNLIKQFENTKEKIAEYTKSIDIKKATESL---------EEQLAAAEAEQELEE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1372 TLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKEL-----AIRLQEAAEAMGVANARNASLERARHQLQLELGDALSD-LG 1445
Cdd:COG5185 330 SKRETETGIQNLTAEIEQGQESLTENLEAIKEEIenivgEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEiLA 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1446 KVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTEL--LKLKNTYEESIVGQETLRRENKNLQEEISN 1523
Cdd:COG5185 410 TLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREAdeESQSRLEEAYDEINRSVRSKKEDLNEELTQ 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 119600132 1524 LTNQVREGT----KNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKIL 1571
Cdd:COG5185 490 IESRVSTLKatleKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1658-1929 |
9.96e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1658 LQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLS 1737
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1738 QKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMAL 1817
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600132 1818 MGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVA 1897
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270
....*....|....*....|....*....|..
gi 119600132 1898 ETQANQYLSKYKKQQHELNEVKERAEVAESQV 1929
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLAL 300
|
|
| |
