|
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 ... |
159-820 |
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: 1415.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAAMSEPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 318
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 319 DIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFLPD 398
Cdd:cd14929 161 DIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDILGFLPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 399 EKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQVTCAV 478
Cdd:cd14929 241 EKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTYAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 479 GALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYKKE 558
Cdd:cd14929 321 GALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 559 SIEWVSIGFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFELVHYAG 638
Cdd:cd14929 401 GIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHFELVHYAG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 639 VVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKKRKKGTSFQTAASLHKENLNKLMTNLKS 718
Cdd:cd14929 481 VVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQFGEKKRKKGASFQTVASLHKENLNKLMTNLKS 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 719 TAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVSSRKAAEE 798
Cdd:cd14929 561 TAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSSRKAAEE 640
|
650 660
....*....|....*....|..
gi 1411134203 799 LLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14929 641 LLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
159-820 |
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: 1233.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAAMSEPR----KKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 314
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKkesgKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 315 SVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQK-ELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDIL 393
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADpELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 394 GFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQ 473
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 474 VTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQE 553
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 554 EYKKESIEWVSIGFGLDLQACIDLIEKP-MGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPdkKKFEAHFE 632
Cdd:cd01377 401 EYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKP--KKSEAHFI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 633 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAipfGEKKRKKGTSFQTAASLHKENLNKL 712
Cdd:cd01377 479 LKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGG---GGKKKKKGGSFRTVSQLHKEQLNKL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 713 MTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSkFVSS 792
Cdd:cd01377 556 MTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKG-FDDG 634
|
650 660
....*....|....*....|....*...
gi 1411134203 793 RKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd01377 635 KAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
159-820 |
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: 1174.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAAMSE---------PRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGA 309
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDgpgkkaqflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 310 RGMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQK-ELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQ 388
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKpELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 389 AMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRG 468
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 469 QTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMF 548
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 549 VLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKK-KF 627
Cdd:cd14927 401 ILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKrKY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 628 EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFG---EKKRKKGTSFQTAASL 704
Cdd:cd14927 481 EAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEDPKsgvKEKRKKAASFQTVSQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 705 HKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTF 784
Cdd:cd14927 561 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAI 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 1411134203 785 PKSKFVSSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14927 641 PDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
160-820 |
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: 1065.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 239
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 240 SGAGKTVNSKHIIQYFATIAAMSEPRKK-----PGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 314
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKkdskmKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 315 SVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQK-ELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDIL 393
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKpELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 394 GFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQ 473
Cdd:cd14913 242 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 474 VTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQE 553
Cdd:cd14913 322 VHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 554 EYKKESIEWVSIGFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFEL 633
Cdd:cd14913 402 EYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFSL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 634 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKKRKKGTSFQTAASLHKENLNKLM 713
Cdd:cd14913 482 IHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKLM 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 714 TNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVSSR 793
Cdd:cd14913 562 SNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSK 641
|
650 660
....*....|....*....|....*..
gi 1411134203 794 KAAEELLGSLKIDHTQYRFGITKVFFK 820
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 ... |
160-820 |
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: 982.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 239
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 240 SGAGKTVNSKHIIQYFATIAAMSEPRKK-----PGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 314
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKdqtpgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 315 SVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQK-ELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDIL 393
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKpELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 394 GFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQ 473
Cdd:cd14917 242 GFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 474 VTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQE 553
Cdd:cd14917 322 VIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 554 EYKKESIEWVSIGFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFEL 633
Cdd:cd14917 402 EYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHFSL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 634 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKKRKKGTSFQTAASLHKENLNKLM 713
Cdd:cd14917 482 IHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLM 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 714 TNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVSSR 793
Cdd:cd14917 562 TNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSR 641
|
650 660
....*....|....*....|....*..
gi 1411134203 794 KAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14917 642 KGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
147-820 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 958.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 147 IEDMAMLTHLNEASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDML 226
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 227 HNRENQSILFTGESGAGKTVNSKHIIQYFATIAAmSEPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMH 306
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSG-SGSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 307 FGARGMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQK-ELHDMLLVSaNPSDFHFCS-CGAVTVESLDDAEELL 384
Cdd:pfam00063 160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASaQLKKELRLT-NPKDYHYLSqSGCYTIDGIDDSEEFK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 385 ATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEY 464
Cdd:pfam00063 239 ITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRET 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 465 VTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAK-LSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFF 543
Cdd:pfam00063 319 VSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKtIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 544 NRHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGIFSILEEECMFPKATDLTFKTKLFDnHFGKSVHLQKPKP 622
Cdd:pfam00063 399 NHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYS-TFSKHPHFQKPRL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 623 dkkKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGE----KKRKKGTSF 698
Cdd:pfam00063 477 ---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESgkstPKRTKKKRF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 699 QTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCI 778
Cdd:pfam00063 554 ITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRI 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1411134203 779 LNPRTFPKSkFVSSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:pfam00063 634 LAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
160-820 |
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: 957.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 239
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 240 SGAGKTVNSKHIIQYFATIAAMSEPRKK------PGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 313
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKenpnanKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 314 SSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQK-ELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDI 392
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKpELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 393 LGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIE 472
Cdd:cd14916 242 LGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 473 QVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQ 552
Cdd:cd14916 322 QVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 553 EEYKKESIEWVSIGFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFE 632
Cdd:cd14916 402 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHFS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 633 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIP-FGEKKRKKGTSFQTAASLHKENLNK 711
Cdd:cd14916 482 LVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSgKGKGGKKKGSSFQTVSALHRENLNK 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 712 LMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVS 791
Cdd:cd14916 562 LMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFID 641
|
650 660
....*....|....*....|....*....
gi 1411134203 792 SRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14916 642 SRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
160-820 |
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: 950.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 239
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 240 SGAGKTVNSKHIIQYFATIAAMSE------PRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 313
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDkkkeqqPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 314 SSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQK-ELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDI 392
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKpELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAIDI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 393 LGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIE 472
Cdd:cd14923 242 LGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 473 QVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQ 552
Cdd:cd14923 322 QVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 553 EEYKKESIEWVSIGFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFE 632
Cdd:cd14923 402 EEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHFS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 633 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKK--RKKGTSFQTAASLHKENLN 710
Cdd:cd14923 482 LVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSGGSKKggKKKGSSFQTVSAVFRENLN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 711 KLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSKFV 790
Cdd:cd14923 562 KLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQFI 641
|
650 660 670
....*....|....*....|....*....|
gi 1411134203 791 SSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14923 642 DSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
161-820 |
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: 934.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 161 VLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGES 240
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 241 GAGKTVNSKHIIQYFATIAAMSEPRKKP-----GALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 315
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEEsgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 316 VDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQK-ELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILG 394
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 395 FLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQV 474
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 475 TCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEE 554
Cdd:cd14918 323 YNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 555 YKKESIEWVSIGFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFELV 634
Cdd:cd14918 403 YKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFSLI 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 635 HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKKRKKGTSFQTAASLHKENLNKLMT 714
Cdd:cd14918 483 HYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAKKKGSSFQTVSALFRENLNKLMT 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 715 NLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVSSRK 794
Cdd:cd14918 563 NLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDSKK 642
|
650 660
....*....|....*....|....*.
gi 1411134203 795 AAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14918 643 ASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
140-832 |
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: 931.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 140 NPPEFEMIEDMAMLTHLNEASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVAN 219
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 220 NAFQDMLHNRENQSILFTGESGAGKTVNSKHIIQYFAtiaAMSEPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRF 299
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLA---SVSGSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 300 GKFIRMHFGARGMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSG--QKELHDMLLvsANPSDFHFCS-CGAVTVES 376
Cdd:smart00242 158 GKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGasEELKKELGL--KSPEDYRYLNqGGCLTVDG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 377 LDDAEELLATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEA-DGTENADKAAFLMGINSSELVKDLIH 455
Cdd:smart00242 236 IDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTvKDKEELSNAAELLGVDPEELEKALTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 456 PRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFT 535
Cdd:smart00242 316 RKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 536 NEKLQQFFNRHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGIFSILEEECMFPKATDLTFKTKLfDNHFGKS 614
Cdd:smart00242 396 NEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKL-NQHHKKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 615 VHLQKPkpdKKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYmstdsaipfgEKKRKK 694
Cdd:smart00242 474 PHFSKP---KKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG----------VSNAGS 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 695 GTSFQTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQ 774
Cdd:smart00242 541 KKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQ 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1411134203 775 RYCILNPRTFPkSKFVSSRKAAEELLGSLKIDHTQYRFGITKVFFKAGFLGQLEAMRD 832
Cdd:smart00242 621 RYRVLLPDTWP-PWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
160-820 |
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: 931.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 239
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 240 SGAGKTVNSKHIIQYFATIAAMSEPRKKP-------GALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 312
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEaasgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 313 LSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQK-ELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 391
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 392 ILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTI 471
Cdd:cd14915 242 ILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 472 EQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLE 551
Cdd:cd14915 322 QQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 552 QEEYKKESIEWVSIGFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHF 631
Cdd:cd14915 402 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAHF 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 632 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEK-KRKKGTSFQTAASLHKENLN 710
Cdd:cd14915 482 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKgGKKKGSSFQTVSALFRENLN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 711 KLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSKFV 790
Cdd:cd14915 562 KLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI 641
|
650 660 670
....*....|....*....|....*....|
gi 1411134203 791 SSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14915 642 DSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
160-820 |
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: 927.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 239
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 240 SGAGKTVNSKHIIQYFATIAAMSEPRKKP-------GALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 312
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEatsgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 313 LSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQK-ELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 391
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 392 ILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTI 471
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 472 EQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLE 551
Cdd:cd14910 322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 552 QEEYKKESIEWVSIGFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHF 631
Cdd:cd14910 402 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAHF 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 632 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEK-KRKKGTSFQTAASLHKENLN 710
Cdd:cd14910 482 SLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKgGKKKGSSFQTVSALFRENLN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 711 KLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSKFV 790
Cdd:cd14910 562 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI 641
|
650 660 670
....*....|....*....|....*....|
gi 1411134203 791 SSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
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 ... |
160-820 |
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: 926.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 239
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 240 SGAGKTVNSKHIIQYFATIAAMSEPRKKP-------GALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 312
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 313 LSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQK-ELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 391
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 392 ILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTI 471
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 472 EQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLE 551
Cdd:cd14912 322 EQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 552 QEEYKKESIEWVSIGFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHF 631
Cdd:cd14912 402 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAHF 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 632 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKK---RKKGTSFQTAASLHKEN 708
Cdd:cd14912 482 SLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKkggKKKGSSFQTVSALFREN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 709 LNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSK 788
Cdd:cd14912 562 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 641
|
650 660 670
....*....|....*....|....*....|..
gi 1411134203 789 FVSSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14912 642 FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
159-820 |
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: 919.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAAMSEPRKK-PGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 317
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDgKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 318 IDIYFLEKSRVIFQQPGERNYHIFYQILSGQK-ELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFL 396
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKpELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 397 PDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQVTC 476
Cdd:cd14934 241 AEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 477 AVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYK 556
Cdd:cd14934 321 SIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 557 KESIEWVSIGFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDK-KKFEAHFELVH 635
Cdd:cd14934 401 REGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKgKGPEAHFELVH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 636 YAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEnymstDSAIPFGEKKRKKGTSFQTAASLHKENLNKLMTN 715
Cdd:cd14934 481 YAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFK-----EEEAPAGSKKQKRGSSFMTVSNFYREQLNKLMTT 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 716 LKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSkFVSSRKA 795
Cdd:cd14934 556 LHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVDNKKA 634
|
650 660
....*....|....*....|....*
gi 1411134203 796 AEELLGSLKIDHTQYRFGITKVFFK 820
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 ... |
159-820 |
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: 899.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAAMS---EPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 315
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKktdEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 316 VDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQ-KELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILG 394
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSvPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 395 FLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQV 474
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 475 TCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEE 554
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 555 YKKESIEWVSIGFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEA-HFEL 633
Cdd:cd14909 401 YKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAaHFAI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 634 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYmSTDSAIPFGEK--KRKKGTSFQTAASLHKENLNK 711
Cdd:cd14909 481 AHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADH-AGQSGGGEQAKggRGKKGGGFATVSSAYKEQLNS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 712 LMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSKfvS 791
Cdd:cd14909 560 LMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE--D 637
|
650 660
....*....|....*....|....*....
gi 1411134203 792 SRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14909 638 PKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
95-1564 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 818.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 95 KCWIPDGENAYIEAEVKGSEDDGTVIVET---TDGKSLSIKEDKIQQ--MNPPEFEMIEDMAMLTHLNEASVLHALKRRY 169
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPAVLHNLEKRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 170 GQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGESGAGKTVNSK 249
Cdd:COG5022 91 NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 250 HIIQYFATIAAMSEPRKkpGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDIDIYFLEKSRVI 329
Cdd:COG5022 171 RIMQYLASVTSSSTVEI--SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 330 FQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCSCGAVT-VESLDDAEELLATEQAMDILGFLPDEKYGCFKLTG 408
Cdd:COG5022 249 HQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 409 AIMHFGNMKFKqKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYER 488
Cdd:COG5022 329 AILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 489 MFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYKKESIEWVSIGFg 568
Cdd:COG5022 408 LFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY- 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 569 LDLQACIDLIEK--PMGIFSILEEECMFPKATDLTFKTKLFDN-HFGKSVHLQKPKPDKKKfeahFELVHYAGVVPYNIS 645
Cdd:COG5022 487 FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVKHYAGDVEYDVE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 646 GWLEKNKDLLNETVVAVFQKSSNRLLASLFENYmstdsaipfgEKKRKKGTsFQTAASLHKENLNKLMTNLKSTAPHFVR 725
Cdd:COG5022 563 GFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE----------ENIESKGR-FPTLGSRFKESLNSLMSTLNSTQPHYIR 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 726 CINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNP---RTFPKSKFVSSRKAAEELLGS 802
Cdd:COG5022 632 CIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPsksWTGEYTWKEDTKNAVKSILEE 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 803 LKIDHTQYRFGITKVFFKAGFLGQLEAMRDERLSKVFTLFQARAQGKLMRIKFQKILEERDALILIQWNIRAFMAVKNWA 882
Cdd:COG5022 712 LVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYEL 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 883 WMRLFFKIKPLVKSSERGEEIaGLKEECAQlqkaleksEFQREELKAKQVSLTQEKNDLIlqlqaeqetlanveeQCEWL 962
Cdd:COG5022 792 KWRLFIKLQPLLSLLGSRKEY-RSYLACII--------KLQKTIKREKKLRETEEVEFSL---------------KAEVL 847
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 963 IKSKIQLEARVKELSERVEEEEEINSelTARGRKLEDECSELKKEIDDLETM-LVKSEKEKRTTEHK---VKNLTEEVEF 1038
Cdd:COG5022 848 IQKFGRSLKAKKRFSLLKKETIYLQS--AQRVELAERQLQELKIDVKSISSLkLVNLELESEIIELKkslSSDLIENLEF 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1039 LNEDISKL-----NRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCER---ELHKLE 1110
Cdd:COG5022 926 KTELIARLkkllnNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNfkkELAELS 1005
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1111 GDLKLNQESMENLESSQRHLAE-----ELRKKELENSQMNSKVENEKGLvaqLQKMVKELQTQIKDLKEKLEaerttrak 1185
Cdd:COG5022 1006 KQYGALQESTKQLKELPVEVAElqsasKIISSESTELSILKPLQKLKGL---LLLENNQLQARYKALKLRRE-------- 1074
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1186 mekeradlTQDLADLNERLEEVGGASLAQLEITKKQETKFQKLRRDMEEATLHFEATSASLKKRHADSLAELegqVENLQ 1265
Cdd:COG5022 1075 --------NSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQL---VNTLE 1143
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1266 QVKQKLEKDrsdlQLEVDDLLTriEQMTRAKANAEKLCTLYEERLNEANA-------KLDKVTQLANDLAAQKTELWSES 1338
Cdd:COG5022 1144 PVFQKLSVL----QLELDGLFW--EANLEALPSPPPFAALSEKRLYQSALydeksklSSSEVNDLKNELIALFSKIFSGW 1217
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1339 --GEFLRRLEEKEALINQLSreksnfTRQIEELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLS 1416
Cdd:COG5022 1218 prGDKLKKLISEGWVPTEYS------TSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQ 1291
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1417 KVNAEMVQ--------WRMKYENNVIQKTEDLEDAKKELAI-RLQETAEamgvanarnaSLERARHRLQLELGDaLSDLG 1487
Cdd:COG5022 1292 YINVGLFNalrtkassLRWKSATEVNYNSEELDDWCREFEIsDVDEELE----------ELIQAVKVLQLLKDD-LNKLD 1360
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1488 KVRSAAARLDQKQLQsgKALADWKQKHEESQTlldasRKEIQ-ALSTELLK--LKHAYKESIVGQETLRRENKNLQEEIS 1564
Cdd:COG5022 1361 ELLDACYSLNPAEIQ--NLKSRYDPADKENNL-----PKEILkKIEALLIKqeLQLSLEGKDETEVHLSEIFSEEKSLIS 1433
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
159-820 |
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: 785.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRR-SEAPPHIFAVANNAFQDMLHNRENQSILFT 237
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 238 GESGAGKTVNSKHIIQYFATIAAMSEPRKKPGA--LEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 315
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSAssIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 316 VDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQ-----KELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAM 390
Cdd:cd00124 161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLsdgarEELKLELLLSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 391 DILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREE--QLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRG 468
Cdd:cd00124 241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 469 QTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQF--FTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRH 546
Cdd:cd00124 321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEStsFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 547 MFVLEQEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKK 625
Cdd:cd00124 401 VFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 626 kfeaHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSsnrllaslfenymstdsaipfgekkrkkgtsfqtaaSLH 705
Cdd:cd00124 480 ----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG------------------------------------SQF 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 706 KENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRtFP 785
Cdd:cd00124 520 RSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPG-AT 598
|
650 660 670
....*....|....*....|....*....|....*
gi 1411134203 786 KSKFVSSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
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 ... |
159-820 |
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: 733.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAAmSEPRKKP-------------GALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRM 305
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAA-SKPKGSGavphpavnpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 306 HFGARGMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLA 385
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 386 TEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYV 465
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 466 TRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFTGILDITGFEILEYNSLEQLCINFTNEKLQQFF 543
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLD-RTKRQgaSFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 544 NRHMFVLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHfgkSVHlqkPKPD 623
Cdd:cd14911 399 NHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH---SMH---PKFM 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 624 KKKFE--AHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSA------IPFGEKKRKKg 695
Cdd:cd14911 473 KTDFRgvADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAqqaltdTQFGARTRKG- 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 696 tSFQTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQR 775
Cdd:cd14911 552 -MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQR 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1411134203 776 YCILNPRTFPKSkFVSSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14911 631 YELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
159-820 |
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: 721.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAAMSEPRKK---PGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 315
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDhniPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 316 VDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKE--LHDMLLVSANpsDFHFCSCGAVTVESLDDAEELLATEQAMDIL 393
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEhlKSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 394 GFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQ 473
Cdd:cd14920 239 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 474 VTCAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLE 551
Cdd:cd14920 319 ADFAVEALAKATYERLFRWLVHRINKALD-RTKRQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 552 QEEYKKESIEWVSIGFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKpdKKKFE 628
Cdd:cd14920 398 QEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPR--QLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 629 AHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY-----MSTDSAIP---FGEKKRKKGTSFQT 700
Cdd:cd14920 475 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgLDQVTGMTetaFGSAYKTKKGMFRT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 701 AASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILN 780
Cdd:cd14920 555 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1411134203 781 PRTFPKSkFVSSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14920 635 PNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
160-820 |
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: 665.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQW-MIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATiaaMSEPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 318
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFAT---VGGSSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 319 DIYFLEKSRVIFQQPGERNYHIFYQILSG--QKELHDMLLVSANpSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFL 396
Cdd:cd01380 159 RTYLLEKSRVVFQAEEERNYHIFYQLCAAasLPELKELHLGSAE-DFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGIS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 397 PDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQVTC 476
Cdd:cd01380 238 EEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 477 AVGALSKSMYERMFKWLVARINRALDAKLSRQF--FTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEE 554
Cdd:cd01380 318 ARDALAKHIYAQLFDWIVDRINKALASPVKEKQhsFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 555 YKKESIEWVSIGFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSV-HLQKPKPDKKKfeahFEL 633
Cdd:cd01380 398 YVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkHFKKPRFSNTA----FIV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 634 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRllaslfenymstdsaipfgeKKrkkgtsfqTAASLHKENLNKLM 713
Cdd:cd01380 473 KHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR--------------------KK--------TVGSQFRDSLILLM 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 714 TNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSKfvSSR 793
Cdd:cd01380 525 ETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRD--DKK 602
|
650 660
....*....|....*....|....*..
gi 1411134203 794 KAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd01380 603 KTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
159-820 |
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: 663.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAAMSEPRKKPGA-------LEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARG 311
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSialshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 312 MLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 391
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 392 ILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTI 471
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 472 EQVTCAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFV 549
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALD-KTKRQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 550 LEQEEYKKESIEWVSIGFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKpdKKK 626
Cdd:cd14932 400 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQ-GNNPKFQKPK--KLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 627 FEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY--------MSTDSAIPFGEKKRKKGTsF 698
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdrivgldkVAGMGESLHGAFKTRKGM-F 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 699 QTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCI 778
Cdd:cd14932 556 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1411134203 779 LNPRTFPKSkFVSSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14932 636 LTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
159-820 |
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: 643.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAAMSEPRKKP---GALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 315
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 316 VDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKEL--HDMLLVSANpsDFHFCSCGAVTVESLDDAEELLATEQAMDIL 393
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKmrSDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETLEAMSIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 394 GFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQ 473
Cdd:cd14921 239 GFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 474 VTCAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLE 551
Cdd:cd14921 319 ADFAIEALAKATYERLFRWILTRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 552 QEEYKKESIEWVSIGFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKPDKKKFE 628
Cdd:cd14921 398 QEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 629 ahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY----------MSTDSAIPfGEKKRKKGTsF 698
Cdd:cd14921 477 --FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqmaKMTESSLP-SASKTKKGM-F 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 699 QTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCI 778
Cdd:cd14921 553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1411134203 779 LNPRTFPKSkFVSSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
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 ... |
159-820 |
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: 636.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAAMSEPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 318
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 319 DIYFLEKSRVIFQQPGERNYHIFYQILSGQKE--LHDMLLVSANpsDFHFCSCGAVTVESLDDAEELLATEQAMDILGFL 396
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEhlKTDLLLEPYN--KYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 397 PDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQVTC 476
Cdd:cd14919 239 EEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 477 AVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEE 554
Cdd:cd14919 319 AIEALAKATYERMFRWLVLRINKALD-KTKRQgaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 555 YKKESIEWVSIGFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKPDKKKfeAHF 631
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK--ADF 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 632 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMS----------TDSAIPfGEKKRKKGTsFQTA 701
Cdd:cd14919 475 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmSETALP-GAFKTRKGM-FRTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 702 ASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNP 781
Cdd:cd14919 553 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 632
|
650 660 670
....*....|....*....|....*....|....*....
gi 1411134203 782 RTFPKSkFVSSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14919 633 NSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
159-820 |
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: 632.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAAMSEPRK-------KPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARG 311
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKdqnslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 312 MLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 391
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 392 ILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTI 471
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 472 EQVTCAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFV 549
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALD-KTKRQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 550 LEQEEYKKESIEWVSIGFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNhfgKSVHLQKPKPDKKK 626
Cdd:cd15896 400 LEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQE---QGTHPKFFKPKKLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 627 FEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY--------MSTDSAIPfGEKKRKKGTsF 698
Cdd:cd15896 477 DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVdrivgldkVSGMSEMP-GAFKTRKGM-F 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 699 QTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCI 778
Cdd:cd15896 555 RTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 634
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1411134203 779 LNPRTFPKSkFVSSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd15896 635 LTPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
159-820 |
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: 619.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAAMSEPRKKPGA---LEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 315
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 316 VDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCSCGAVTVESlDDAEELLATEQAMDILGF 395
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 396 LPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQVT 475
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 476 CAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQE 553
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 554 EYKKESIEWVSIGFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNhfgKSVHLQKPKPDKKKFEAH 630
Cdd:cd14930 399 EYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQE---QGGHPKFQRPRHLRDQAD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 631 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF---------ENYMSTDSAIPFGEKKRKKgtsFQTA 701
Cdd:cd14930 476 FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegivglEQVSSLGDGPPGGRPRRGM---FRTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 702 ASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNP 781
Cdd:cd14930 553 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 632
|
650 660 670
....*....|....*....|....*....|....*....
gi 1411134203 782 RTFPKSkFVSSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14930 633 NAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
165-820 |
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: 608.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 165 LKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGESGAGK 244
Cdd:cd01378 7 LKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESGAGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 245 TVNSKHIIQYFATIAAMSEPrkKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDIDIYFLE 324
Cdd:cd01378 87 TEASKRIMQYIAAVSGGSES--EVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 325 KSRVIFQQPGERNYHIFYQILSG--QKELHdMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFLPDEKYG 402
Cdd:cd01378 165 KSRVVGQIKGERNFHIFYQLLKGasQEYLQ-ELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQDS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 403 CFKLTGAIMHFGNMKFKQKPREEQLEADGTEnADKAAFLMGINSSELVKDLIHPRIKVGNEY---VTRGQTIEQVTCAVG 479
Cdd:cd01378 244 IFRILAAILHLGNIQFAEDEEGNAAISDTSV-LDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQAAYARD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 480 ALSKSMYERMFKWLVARINRALDAKLSRQFFT-GILDITGFEILEYNSLEQLCINFTNEKLQQFFNRhmFVL--EQEEYK 556
Cdd:cd01378 323 ALAKAIYSRLFDWIVERINKSLAAKSGGKKKViGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE--LTLkaEQEEYV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 557 KESIEWVSIGFgLDLQACIDLIE-KPMGIFSILEEECMFP-KATDLTFKTKLfDNHFGKSVHLQKPKPDKKKFEAHFELV 634
Cdd:cd01378 401 REGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHFELRRGEFRIK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 635 HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSaipfgeKKRKkgtsfQTAASLHKENLNKLMT 714
Cdd:cd01378 479 HYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDS------KKRP-----PTAGTKFKNSANALVE 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 715 NLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSKFvSSRK 794
Cdd:cd01378 548 TLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDG-TWQG 626
|
650 660
....*....|....*....|....*.
gi 1411134203 795 AAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd01378 627 GVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
160-820 |
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: 605.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYkGKRRSEaPPHIFAVANNAFQDMLHNRENQSILFTGE 239
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY-RQKLLD-SPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 240 SGAGKTVNSKHIIQYFATIAAMSeprkkpGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDID 319
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGS------SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 320 IYFLEKSRVIFQQPGERNYHIFYQILSG-QKELHDMLLVSAnPSDFHFCS-CGAVTVESLDDAEELLATEQAMDILGFLP 397
Cdd:cd01383 154 TYLLEKSRVVQLANGERSYHIFYQLCAGaSPALREKLNLKS-ASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGISK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 398 DEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQVTCA 477
Cdd:cd01383 233 EDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 478 VGALSKSMYERMFKWLVARINRALDAKLSRqffTG----ILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQE 553
Cdd:cd01383 313 RDALAKAIYASLFDWLVEQINKSLEVGKRR---TGrsisILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 554 EYKKESIEWVSIGFgLDLQACIDLIE-KPMGIFSILEEECMFPKATDLTFKTKLfdnhfgkSVHLQKPKPDKKKFEAHFE 632
Cdd:cd01383 390 EYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-------KQHLKSNSCFKGERGGAFT 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 633 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQkSSNRLLASLFENYMSTDSAIPFGEKKRKKGTSF-QTAASLHKENLNK 711
Cdd:cd01383 462 IRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLS-SCSCQLPQLFASKMLDASRKALPLTKASGSDSQkQSVATKFKGQLFK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 712 LMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVS 791
Cdd:cd01383 541 LMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPL 620
|
650 660
....*....|....*....|....*....
gi 1411134203 792 SRKAAeeLLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd01383 621 STSVA--ILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
159-820 |
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: 600.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAAmseprkKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 318
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISG------QHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 319 DIYFLEKSRVIFQQPGERNYHIFYQILSG-QKELHDMLLVSaNPSDFHFCSCG-AVTVESLDDAEELLATEQAMDILGFL 396
Cdd:cd01381 155 EQYLLEKSRIVSQAPDERNYHIFYCMLAGlSAEEKKKLELG-DASDYYYLTQGnCLTCEGRDDAAEFADIRSAMKVLMFT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 397 PDEKYGCFKLTGAIMHFGNMKFKQKPRE--EQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQV 474
Cdd:cd01381 234 DEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 475 TCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFT---GILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLE 551
Cdd:cd01381 314 LDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSRtsiGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 552 QEEYKKESIEWVSIGFgLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLqKPKPDkkkFEAH 630
Cdd:cd01381 394 QEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYL-KPKSD---LNTS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 631 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMStdsaipFGEKKRKKGtsfQTAASLHKENLN 710
Cdd:cd01381 469 FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDIS------MGSETRKKS---PTLSSQFRKSLD 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 711 KLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTfPKSKFV 790
Cdd:cd01381 540 QLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGI-PPAHKT 618
|
650 660 670
....*....|....*....|....*....|
gi 1411134203 791 SSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd01381 619 DCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
160-820 |
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: 598.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 239
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 240 SGAGKTVNSKHIIQYFATIAAmseprkKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDID 319
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTN------NHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 320 IYFLEKSRVIFQQPGERNYHIFYQILSG---QKELHDMLLVSaNPSDFHFCS-CGAVTVESLDDAEELLATEQAMDILGF 395
Cdd:cd14883 156 DYLLEQSRITFQAPGERNYHVFYQLLAGakhSKELKEKLKLG-EPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVLGI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 396 LPDEKYGCFKLTGAIMHFGNMKFKQKPREE-QLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQV 474
Cdd:cd14883 235 PEEMQEGIFSVLSAILHLGNLTFEDIDGETgALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 475 TCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEE 554
Cdd:cd14883 315 RDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 555 YKKESIEWVSIGFGlDLQACIDLIEK-PMGIFSILEEECMFPKATDLTFKTKLFDNHfgkSVHLQKPKPDKKKFEAHFEL 633
Cdd:cd14883 395 YEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH---EKHPYYEKPDRRRWKTEFGV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 634 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF-----ENYMSTDSAIPFGEKKRKKGTSFQTAASLHKEN 708
Cdd:cd14883 471 KHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtypdlLALTGLSISLGGDTTSRGTSKGKPTVGDTFKHQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 709 LNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSK 788
Cdd:cd14883 551 LQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADH 630
|
650 660 670
....*....|....*....|....*....|..
gi 1411134203 789 fVSSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14883 631 -KETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
159-820 |
1.07e-177 |
|
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: 555.36 E-value: 1.07e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP-VYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 237
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 238 GESGAGKTVNSKHIIQYFATIAAMSEPRKKPgaLEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 317
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRS--VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 318 IDIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHF---CSCgaVTVESLDDAEELLATEQAMDILG 394
Cdd:cd01384 159 IRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYlnqSKC--FELDGVDDAEEYRATRRAMDVVG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 395 FLPDEKYGCFKLTGAIMHFGNMKFKQKPreeqlEADGTENADK--------AAFLMGINSSELVKDLIHPRIKVGNEYVT 466
Cdd:cd01384 237 ISEEEQDAIFRVVAAILHLGNIEFSKGE-----EDDSSVPKDEksefhlkaAAELLMCDEKALEDALCKRVIVTPDGIIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 467 RGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRH 546
Cdd:cd01384 312 KPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 547 MFVLEQEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGIFSILEEECMFPKATDLTFKTKLFDNhFGKSVHLQKPKPDKK 625
Cdd:cd01384 392 VFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPKLSRT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 626 KfeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEnymstdsaiPFGEKKRKKGTSFQTAASLH 705
Cdd:cd01384 470 D----FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFP---------PLPREGTSSSSKFSSIGSRF 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 706 KENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFP 785
Cdd:cd01384 537 KQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLK 616
|
650 660 670
....*....|....*....|....*....|....*
gi 1411134203 786 KSKfvSSRKAAEELLGslKIDHTQYRFGITKVFFK 820
Cdd:cd01384 617 GSD--DEKAACKKILE--KAGLKGYQIGKTKVFLR 647
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
159-820 |
8.03e-165 |
|
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: 520.10 E-value: 8.03e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAAMSeprkkpGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 318
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGST------NGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 319 DIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSAnpSDFHFCSC-GAVTVESLDDAEELLATEQAMDILGFLP 397
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSS--AAYGYLSLsGCIEVEGVDDVADFEEVVLAMEQLGFDD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 398 DEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENAD---KAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQ-TIEQ 473
Cdd:cd14872 233 ADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDvlkEVATLLGVDAATLEEALTSRLMEIKGCDPTRIPlTPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 474 VTCAVGALSKSMYERMFKWLVARINRALD-AKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQ 552
Cdd:cd14872 313 ATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 553 EEYKKESIEWVSIGFgLDLQACIDLIEK-PMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKpkpDKKKFEAHF 631
Cdd:cd14872 393 ALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYA---EVRTSRTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 632 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEnymstdsaiPFGEKKRkkgTSFQTAASLHKENLNK 711
Cdd:cd14872 469 IVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP---------PSEGDQK---TSKVTLGGQFRKQLSA 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 712 LMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILnPRTFPKSKFVS 791
Cdd:cd14872 537 LMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIAKRVGPD 615
|
650 660
....*....|....*....|....*....
gi 1411134203 792 SRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14872 616 DRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
159-820 |
1.11e-164 |
|
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: 519.88 E-value: 1.11e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP-VYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 237
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 238 GESGAGKTVNSKHIIQYFATIAAmseprKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 317
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWG-----SGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 318 IDIYFLEKSRVIFQQPGERNYHIFYQILSGQKE-LHDMLLvsanpsdfhfcscgavTVESLDDAEELLATEQAMDILGFL 396
Cdd:cd01382 156 VSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEdLREKLL----------------KDPLLDDVGDFIRMDKAMKKIGLS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 397 PDEKYGCFKLTGAIMHFGNMKFKQKPREE----QLEADGTENADKAAFLMGINSSELVKDLIHpRIKVGNEYVTRGQTI- 471
Cdd:cd01382 220 DEEKLDIFRVVAAVLHLGNIEFEENGSDSgggcNVKPKSEQSLEYAAELLGLDQDELRVSLTT-RVMQTTRGGAKGTVIk 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 472 -----EQVTCAVGALSKSMYERMFKWLVARINRALDAKLSrQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRH 546
Cdd:cd01382 299 vplkvEEANNARDALAKAIYSKLFDHIVNRINQCIPFETS-SYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNER 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 547 MFVLEQEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGIFSILEEECMFPKATdltfktklfDNHFGKSVHLQKPK---- 621
Cdd:cd01382 378 ILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPS---------DQHFTSAVHQKHKNhfrl 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 622 --PDKKKFEAHFELV--------HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSaipfGEKK 691
Cdd:cd01382 448 siPRKSKLKIHRNLRddegflirHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK----DSKQ 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 692 RKKGTSFQTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYAD 771
Cdd:cd01382 524 KAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHD 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1411134203 772 FKQRY--------CILNPRTFPKSkfvssrkaaeeLLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd01382 604 LYNMYkkylppklARLDPRLFCKA-----------LFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
159-820 |
4.05e-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: 519.25 E-value: 4.05e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP-VYKKEVVAAYKGKRRSeAPPHIFAVANNAFQDMLHNRENQSILFT 237
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSIS-KSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 238 GESGAGKTVNSKHIIQYFATiaAMSEPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHF---------G 308
Cdd:cd14888 80 GESGAGKTESTKYVMKFLAC--AGSEDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklkskrmsG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 309 ARGMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKEL-----------------HDMLLVSANPSDFH------ 365
Cdd:cd14888 158 DRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAkntglsyeendeklakgADAKPISIDMSSFEphlkfr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 366 --FCScGAVTVESLDDAEELLATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFK-QKPREE--QLEADGTENADKAAF 440
Cdd:cd14888 238 ylTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEnNEACSEgaVVSASCTDDLEKVAS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 441 LMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALD-AKLSRQFFTGILDITGF 519
Cdd:cd14888 317 LLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGVLDIFGF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 520 EILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLI-EKPMGIFSILEEECMFPKAT 598
Cdd:cd14888 397 ECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEECFVPGGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 599 DLTFKTKLFDNHFG-KSVHLQKPKPDKkkfeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN 677
Cdd:cd14888 476 DQGLCNKLCQKHKGhKRFDVVKTDPNS------FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 678 YMstDSAIPFGEKKRKkgtsFQTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIR 757
Cdd:cd14888 550 YL--RRGTDGNTKKKK----FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQ 623
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411134203 758 ICREGFPNRLQYADFKQRYCILNPrtfpkskfvssrkaaeellGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14888 624 VSRAGYPVRLSHAEFYNDYRILLN-------------------GEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
160-820 |
1.95e-160 |
|
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: 507.58 E-value: 1.95e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 239
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 240 SGAGKTVNSKHIIQYFATIAamsepRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDID 319
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG-----KANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 320 IYFLEKSRVIFQQPGERNYHIFYQILSG---QKELHDMLLVSANPSD-FHFCSCGAVTVESLD-DAEELLATEQAMDILG 394
Cdd:cd01379 157 EYLLEKSRVVHQAIGERNFHIFYYIYAGlaeDKKLAKYKLPENKPPRyLQNDGLTVQDIVNNSgNREKFEEIEQCFKVIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 395 FLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEAD----GTENADKAAFLMGINSSELVKDLIHprikvgNEYVTRGQT 470
Cdd:cd01379 237 FTKEEVDSVYSILAAILHIGDIEFTEVESNHQTDKSsrisNPEALNNVAKLLGIEADELQEALTS------HSVVTRGET 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 471 I------EQVTCAVGALSKSMYERMFKWLVARINRALdaKLSR-----QFFTGILDITGFEILEYNSLEQLCINFTNEKL 539
Cdd:cd01379 311 IirnntvEEATDARDAMAKALYGRLFSWIVNRINSLL--KPDRsasdePLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 540 QQFFNRHMFVLEQEEYKKESIEWVSIGFG-----LDLqacidLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHfgKS 614
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 615 VHLQKPKPDkkkfEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLAslfenymstdsaipfgekkrkk 694
Cdd:cd01379 462 KYYWRPKSN----ALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR---------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 695 gtsfQTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQ 774
Cdd:cd01379 516 ----QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLK 591
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1411134203 775 RYCILnprTFPKSKFV-SSRKAAEELLGSLKIDHtqYRFGITKVFFK 820
Cdd:cd01379 592 RYYFL---AFKWNEEVvANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
159-820 |
6.83e-160 |
|
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: 506.99 E-value: 6.83e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP-VYKkevVAAYKGKRRSEA-----PPHIFAVANNAFQDMLHNR--- 229
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPlLYD---VPGFDSQRKEEAtasspPPHVFSIAERAYRAMKGVGkgq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 230 -ENQSILFTGESGAGKTVNSKHIIQYFATIAAMSE-PRKKPGA------LEEQIMQANIILEAFGNAKTLRNDNSSRFGK 301
Cdd:cd14892 78 gTPQSIVVSGESGAGKTEASKYIMKYLATASKLAKgASTSKGAanahesIEECVLLSNLILEAFGNAKTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 302 FIRMHFGARGMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCSCG-AVTVESLDDA 380
Cdd:cd14892 158 YIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGVDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 381 EELLATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQ--KPREEQLEADGTENADKAAFLMGINSSELVKDLIhPRI 458
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLV-TQT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 459 KVGneyvTRGQ------TIEQVTCAVGALSKSMYERMFKWLVARINRA----------LDAKLSRQFFTGILDITGFEIL 522
Cdd:cd14892 317 TST----ARGSvleiklTAREAKNALDALCKYLYGELFDWLISRINAChkqqtsgvtgGAASPTFSPFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 523 EYNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIEK-PMGIFSILEEECMFP-KATDL 600
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 601 TFKTKLFDNHFGKSVHLQKPkpdkkKFEA-HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNrllaslfenym 679
Cdd:cd14892 472 QLLTIYHQTHLDKHPHYAKP-----RFECdEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK----------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 680 stdsaipfgekkrkkgtsFQTaaslhkeNLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRIC 759
Cdd:cd14892 536 ------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIR 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411134203 760 REGFPNRLQYADFKQRYCIL-----NPRTFPKSKFVSSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14892 591 REGFPIRRQFEEFYEKFWPLarnkaGVAASPDACDATTARKKCEEIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
159-820 |
1.97e-159 |
|
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: 505.85 E-value: 1.97e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP-VYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 237
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 238 GESGAGKTVNSKHIIQYFATIAamseprkkpGALE----EQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 313
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA---------GGLNdstiKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 314 SSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFcSCGAVTVESLDDAEELLATEQAMDIL 393
Cdd:cd14903 152 VGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 394 GFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLE--ADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTI 471
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 472 EQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLE 551
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 552 QEEYKKESIEWVSIGFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHf 631
Cdd:cd14903 391 QIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIK- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 632 elvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEK----KRKKGT-SFQTAASLHK 706
Cdd:cd14903 469 ---HYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLArgarRRRGGAlTTTTVGTQFK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 707 ENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPK 786
Cdd:cd14903 546 DSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGRNT 625
|
650 660 670
....*....|....*....|....*....|....*
gi 1411134203 787 SKFVssRKAAEELLGSLKIDH-TQYRFGITKVFFK 820
Cdd:cd14903 626 DVPV--AERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
159-820 |
1.56e-156 |
|
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: 497.74 E-value: 1.56e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAamseprKKPGAL-EEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFgARGMLSSVD 317
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN------QRRNNLvTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 318 IDIYFLEKSRVIFQQPGERNYHIFYQILSG--QKELHDMLLVSANPSdFHFCSCGAVTVESLDDAEELLATEQAMDILGF 395
Cdd:cd01387 154 TSQYLLEKSRIVTQAKNERNYHVFYELLAGlpAQLRQKYGLQEAEKY-FYLNQGGNCEIAGKSDADDFRRLLAAMQVLGF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 396 LPDEKYGCFKLTGAIMHFGNMKFKQKPRE---EQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIE 472
Cdd:cd01387 233 SSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTID 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 473 QVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQ 552
Cdd:cd01387 313 QALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 553 EEYKKESIEWVSIGFgLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKPDkkkfEAHF 631
Cdd:cd01387 393 EEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPRMP----LPEF 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 632 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMS-TDSAIPFGEKKR---KKGTSFQTAASLHkE 707
Cdd:cd01387 467 TIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAqTDKAPPRLGKGRfvtMKPRTPTVAARFQ-D 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 708 NLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKS 787
Cdd:cd01387 546 SLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRP 625
|
650 660 670
....*....|....*....|....*....|....
gi 1411134203 788 -KFVSSRKAAEELLGSLKIDhtQYRFGITKVFFK 820
Cdd:cd01387 626 aPGDMCVSLLSRLCTVTPKD--MYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
159-820 |
1.93e-155 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 496.13 E-value: 1.93e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYfatIAAMSEPRKKPGaLEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 318
Cdd:cd01385 81 ESGSGKTESTNFLLHH---LTALSQKGYGSG-VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 319 DIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCSCGA-VTVESLDDAEELLATEQAMDILGFLP 397
Cdd:cd01385 157 EKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDcYTLEGEDEKYEFERLKQAMEMVGFLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 398 DEKYGCFKLTGAIMHFGNMKFKQKP--REEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQVT 475
Cdd:cd01385 237 ETQRQIFSVLSAVLHLGNIEYKKKAyhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 476 CAVGALSKSMYERMFKWLVARINRALDAKLS----RQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLE 551
Cdd:cd01385 317 ATRDAMAKCLYSALFDWIVLRINHALLNKKDleeaKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 552 QEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGIFSILEEECMFPKATDLTFKTKlFDNHFGKSVHLQKPkpdkKKFEAH 630
Cdd:cd01385 397 QEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKP----QVMEPA 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 631 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSN-----------------RLLASLFENYM-------------- 679
Cdd:cd01385 471 FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSafvreligidpvavfrwAVLRAFFRAMAafreagrrraqrta 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 680 ---------STDSAIPFGEKKRKKGTSFQTAASlhkenLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCN 750
Cdd:cd01385 551 ghsltlhdrTTKSLLHLHKKKKPPSVSAQFQTS-----LSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYT 625
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 751 GVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSKfvSSRKaaeELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd01385 626 GMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSK--EDIK---DFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
159-818 |
2.14e-154 |
|
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: 492.00 E-value: 2.14e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAY------KGKRRSEAPPHIFAVANNAFQDMLHNRE-- 230
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 231 --NQSILFTGESGAGKTVNSKHIIQYfatIAAMSEPRKKPGALEEQ------IMQANIILEAFGNAKTLRNDNSSRFGKF 302
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNY---LASVSSATTHGQNATERenvrdrVLESNPILEAFGNARTNRNNNSSRFGKF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 303 IRMHFGARGMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSG--QKELHDMLLVSANPSDFHFCSCGAVTVESLDDA 380
Cdd:cd14901 158 IRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGasSDELHALGLTHVEEYKYLNSSQCYDRRDGVDDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 381 EELLATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPRE-EQLEADGTENADKAAFLMGINSSELVKDLIHPRIK 459
Cdd:cd14901 238 VQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEgGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 460 VGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLS--RQFFTGILDITGFEILEYNSLEQLCINFTNE 537
Cdd:cd14901 318 AGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFANE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 538 KLQQFFNRHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGIFSILEEECMFPKATDLTFKTKLFDNhFGKSVH 616
Cdd:cd14901 398 KLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHAS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 617 LQKPKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASlfenymstdsaipfgekkrkkgt 696
Cdd:cd14901 476 FSVSKLQQGK--RQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 697 sfqTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRY 776
Cdd:cd14901 531 ---TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTY 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1411134203 777 CILNPRTfpKSKFVSSRKAAEELLGSLKI------DHTQYRFGITKVF 818
Cdd:cd14901 608 SCLAPDG--ASDTWKVNELAERLMSQLQHselnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
159-820 |
4.22e-154 |
|
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: 491.21 E-value: 4.22e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP-VYKKEVVAAYKGKRRSEAPPHIFAVANNAF----QDMLHNRENQS 233
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtqliQSGVLDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 234 ILFTGESGAGKTVNSKHIIQYFATI-------------AAMSEPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFG 300
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARItsgfaqgasgegeAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 301 KFIRMHFGARGMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCSCGAVTVESLDDA 380
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 381 EELLATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGT-ENADKAAFLMGINSSELVKDLIHPRIK 459
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 460 VGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKL 539
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 540 QQFFNRHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-----KPmGIFSILEEECMFPKA-TDLTFKTKLFDNHFGK 613
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgkvngKP-GIFITLDDCWRFKGEeANKKFVSQLHASFGRK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 614 SV------------HLQKPKPDKKKfeaHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLlaslfenymst 681
Cdd:cd14890 479 SGsggtrrgssqhpHFVHPKFDADK---QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI----------- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 682 dsaipfgekkRKKGTSFQTAASLHkenlnKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICRE 761
Cdd:cd14890 545 ----------REVSVGAQFRTQLQ-----ELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQ 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1411134203 762 GFPNRLQYADFKQRYCILNPRTFPKSKFVssrkaaEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14890 610 GFALREEHDSFFYDFQVLLPTAENIEQLV------AVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
159-820 |
2.82e-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: 477.75 E-value: 2.82e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP-VYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 237
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 238 GESGAGKTVNSKHIIQYFATIAAMS---EPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 314
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSlelSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 315 SVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCS-CGAVTVESLDDAEELLATEQAMDIL 393
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 394 GFLPDEKYGCFKLTGAIMHFGNMKFkqkpreeqLEADGTENADKAAF-----LMGINSSELVKDLIHPRIKVGNEYVTRG 468
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKTALgrsaeLLGLDPTQLTDALTQRSMFLRGEEILTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 469 QTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFtGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMF 548
Cdd:cd14873 313 LNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFKSI-GILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 549 VLEQEEYKKESIEWVSIGFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLfdnhfgKSVHLQKPKPDKKKFE 628
Cdd:cd14873 392 SLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKL------HSQHANNHFYVKPRVA 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 629 AH-FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN--YMSTDSAIPFGEKKRKKGTSFQtaaslH 705
Cdd:cd14873 465 VNnFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHvsSRNNQDTLKCGSKHRRPTVSSQ-----F 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 706 KENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTfp 785
Cdd:cd14873 540 KDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL-- 617
|
650 660 670
....*....|....*....|....*....|....*
gi 1411134203 786 kSKFVSSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14873 618 -ALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
159-820 |
5.13e-146 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 468.02 E-value: 5.13e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKR-RSEAPPHIFAVANNAFQDMLHNRENQSILFT 237
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 238 GESGAGKTVNSKHIIQYFATIAAMSEPRkkpgaLEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 317
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSD-----LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 318 IDIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQA-------M 390
Cdd:cd14897 156 IDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDSEELEYYRQMfhdltniM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 391 DILGFLPDEKYGCFKLTGAIMHFGNMKFkqkprEEQLEADGTENADK-----AAFLMGINSSELVKDLIHPRIKVGNEYV 465
Cdd:cd14897 236 KLIGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTIRGERI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 466 TRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFT-----GILDITGFEILEYNSLEQLCINFTNEKLQ 540
Cdd:cd14897 311 QSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMTrgpsiGILDMSGFENFKINSFDQLCINLSNERLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 541 QFFNRHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKLfDNHFGKSVHLQK 619
Cdd:cd14897 391 QYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVA 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 620 PKPDKKKFEAHfelvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMstdsaipfgekkrkkgtsfq 699
Cdd:cd14897 469 SPGNRVAFGIR----HYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSYF-------------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 700 taaslhKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCIL 779
Cdd:cd14897 525 ------KRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEI 598
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1411134203 780 NPrtFPKSKFVSSRKAAEELLGSLKIDhtQYRFGITKVFFK 820
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 ... |
161-820 |
1.89e-140 |
|
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: 453.21 E-value: 1.89e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 161 VLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDML----HNRENQSILF 236
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 237 TGESGAGKTVNSKHIIQYfatiaaMSEPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFgARGMLSSV 316
Cdd:cd14889 83 SGESGAGKTESTKLLLRQ------IMELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 317 DIDIYFLEKSRVIFQQPGERNYHIFYQILSG----QKELHDMLlvsaNPSDFHFCSCGAVTVESLD----DAEELLateQ 388
Cdd:cd14889 156 KINEYLLEKSRVVHQDGGEENFHIFYYMFAGisaeDRENYGLL----DPGKYRYLNNGAGCKREVQywkkKYDEVC---N 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 389 AMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQkpreEQLEADGTENADK-----AAFLMGINSSELVKDLIHPRIKVGNE 463
Cdd:cd14889 229 AMDMVGFTEQEEVDMFTILAGILSLGNITFEM----DDDEALKVENDSNgwlkaAAGQFGVSEEDLLKTLTCTVTFTRGE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 464 YVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQF---FTGILDITGFEILEYNSLEQLCINFTNEKLQ 540
Cdd:cd14889 305 QIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVelrEIGILDIFGFENFAVNRFEQACINLANEQLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 541 QFFNRHMFVLEQEEYKKESIEWVSIGFgLDLQACIDL-IEKPMGIFSILEEECMFPKATDLTFKTKLfDNHFGKSVHLQK 619
Cdd:cd14889 385 YFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 620 PKPDKKKfeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKKRKKG---- 695
Cdd:cd14889 463 SRSKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGsdnf 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 696 --TSFQTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFK 773
Cdd:cd14889 539 nsTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFA 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1411134203 774 QRYCILnprtFPKSKFVSSRKAAEELLGSLKIdhTQYRFGITKVFFK 820
Cdd:cd14889 619 ERYKIL----LCEPALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
159-799 |
5.02e-138 |
|
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: 448.57 E-value: 5.02e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP-VYKKEVVAAYK--------GKRRSEAPPHIFAVANNAFQDMLHN- 228
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 229 RENQSILFTGESGAGKTVNSKHIIQYFATI----AAMSEPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIR 304
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgrdqSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 305 MHFGARGMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSG-QKELHDMLLVSAN----PSDFHFCSCGAVTVESLDD 379
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGaDKTLLDLLGLQKGgkyeLLNSYGPSFARKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 380 AEELLATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFK---QKPREEQLEADGTENADKAAFLMGINSSELVKDLIHP 456
Cdd:cd14902 241 AQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTaenGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 457 RIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFT---------GILDITGFEILEYNSL 527
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSISdedeelatiGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 528 EQLCINFTNEKLQQFFNRHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGIFSILEEECMFPKATDLTFKTKL 606
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSNQALSTKF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 607 FDNHFGksvhlqkpkpdkkkfEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIP 686
Cdd:cd14902 480 YRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSPGAD 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 687 FGEKKRKKGTSFQTA--ASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFP 764
Cdd:cd14902 545 NGAAGRRRYSMLRAPsvSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYS 624
|
650 660 670
....*....|....*....|....*....|....*
gi 1411134203 765 NRLQYADFKQRYCILNPrtFPKSKFVSSRKAAEEL 799
Cdd:cd14902 625 VRLAHASFIELFSGFKC--FLSTRDRAAKMNNHDL 657
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
160-779 |
2.31e-135 |
|
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: 437.82 E-value: 2.31e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP-VYKKEVVAAY-----------KGKRRSEAPPHIFAVANNAFQDMLH 227
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 228 NR----ENQSILFTGESGAGKTVNSKHIIQYFATI------AAMSEPRKKPGaLEEQIMQANIILEAFGNAKTLRNDNSS 297
Cdd:cd14900 82 GLngvmSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlaASVSMGKSTSG-IAAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 298 RFGKFIRMHFGARGMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHdmllvsanpsdfhfcscgavtvESL 377
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAA----------------------RKR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 378 DDAEELLAteqAMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENA-------DKAAFLMGINSSELV 450
Cdd:cd14900 219 DMYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 451 KDLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRAL---DAKLSRQ--FFTGILDITGFEILEYN 525
Cdd:cd14900 296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGglHFIGILDIFGFEVFPKN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 526 SLEQLCINFTNEKLQQFFNRHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKT 604
Cdd:cd14900 376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLAS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 605 KLFdNHFGKSVHLQKPKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQkssnrllaslfenymstdsa 684
Cdd:cd14900 455 KLY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV-------------------- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 685 ipfgekkrkKGTSFqtaaslhKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFP 764
Cdd:cd14900 512 ---------YGLQF-------KEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFP 575
|
650
....*....|....*
gi 1411134203 765 NRLQYADFKQRYCIL 779
Cdd:cd14900 576 IRLLHDEFVARYFSL 590
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
159-820 |
6.95e-129 |
|
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: 420.50 E-value: 6.95e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP-VYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 237
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 238 GESGAGKTVNSKHIIQYFATIAamseprkkpGALEE----QIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 313
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA---------GGRKDktiaKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 314 SSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSG--QKELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 391
Cdd:cd14904 152 IGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlsSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 392 ILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGtENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTI 471
Cdd:cd14904 232 LIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNG-SQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 472 EQVTCAVGALSKSMYERMFKWLVARINRAL---DAKLSRQFftGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMF 548
Cdd:cd14904 311 VEAEENRDALAKAIYSKLFDWMVVKINAAIstdDDRIKGQI--GVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 549 VLEQEEYKKESIEWVSIGFGlDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNH--FGKSVHLQKPKPDKKK 626
Cdd:cd14904 389 KTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKRTQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 627 FEAHfelvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIpfGEKKRKKGTSFQTAASLHK 706
Cdd:cd14904 468 FIIN----HYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETK--EGKSGKGTKAPKSLGSQFK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 707 ENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILnprtFPK 786
Cdd:cd14904 542 TSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM----FPP 617
|
650 660 670
....*....|....*....|....*....|....*.
gi 1411134203 787 SKFV-SSRKAAEELLGSL-KIDHTQYRFGITKVFFK 820
Cdd:cd14904 618 SMHSkDVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
159-788 |
1.19e-128 |
|
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: 420.59 E-value: 1.19e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP---------VYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNR 229
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 230 ENQSILFTGESGAGKTVNSKHIIQYFATIAA--------------MSEPRKKPGALEEQIMQANIILEAFGNAKTLRNDN 295
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 296 SSRFGKFIRMHFGAR-GMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSG--QKELHDMLLVSANPSDFHFC--SCG 370
Cdd:cd14907 161 SSRFGKYVSILVDKKkRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGadQQLLQQLGLKNQLSGDRYDYlkKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 371 AVTVESLDDAEELLATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQKP--REEQLEADGTENADKAAFLMGINSSE 448
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 449 LVKDLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRAL--------DAKLSRQFFTGILDITGFE 520
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 521 ILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYKKESIE-WVS-IGFgLDLQACIDLIEK-PMGIFSILEEECMFPKA 597
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdYLNqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 598 TDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEahfeLVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF-- 675
Cdd:cd14907 480 TDEKLLNKIKKQHKNNSKLIFPNKINKDTFT----IRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFsg 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 676 ENYMSTDSAIPFGEKKRKK---GTSFqtaaslhKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGV 752
Cdd:cd14907 556 EDGSQQQNQSKQKKSQKKDkflGSKF-------RNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGV 628
|
650 660 670
....*....|....*....|....*....|....*..
gi 1411134203 753 LEGIRICREGFPNRLQYADFKQRYCILNP-RTFPKSK 788
Cdd:cd14907 629 LESIRVRKQGYPYRKSYEDFYKQYSLLKKnVLFGKTK 665
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
121-873 |
1.05e-126 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 420.21 E-value: 1.05e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 121 VETTDGKSLSIKEDKIQQMNPP-EFEMIEDMAMLTHLNEASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVV 199
Cdd:PTZ00014 71 IDPPTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 200 AAYKGKRRSEA-PPHIFAVANNAFQDMLHNRENQSILFTGESGAGKTVNSKHIIQYFATiaamSEPRKKPGALEEQIMQA 278
Cdd:PTZ00014 151 RRYRDAKDSDKlPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS----SKSGNMDLKIQNAIMAA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 279 NIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSG-----QKELHd 353
Cdd:PTZ00014 227 NPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGandemKEKYK- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 354 mlLVSANpsDFHFCSCGAVTVESLDDAEELLATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTE 433
Cdd:PTZ00014 306 --LKSLE--EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAIS 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 434 NADKAAF-----LMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQ 508
Cdd:PTZ00014 382 DESLEVFneaceLLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFK 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 509 FFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPMGIFSIL 588
Cdd:PTZ00014 462 VFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSIL 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 589 EEECMFPKATDLTFkTKLFDNHFGKSVHLQKPKPDKKKfeaHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSN 668
Cdd:PTZ00014 542 EDQCLAPGGTDEKF-VSSCNTNLKNNPKYKPAKVDSNK---NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPN 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 669 RLLASLFENYMSTDSAIpfgekkrKKGtsfQTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLR 748
Cdd:PTZ00014 618 PLVRDLFEGVEVEKGKL-------AKG---QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLH 687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 749 CNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFPKSKfVSSRKAAEELLGSLKIDHTQYRFGITKVFFKAGFLGQLE 828
Cdd:PTZ00014 688 SLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSS-LDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELT 766
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1411134203 829 AMRDERLSKVFTLFQArAQGKLMRIKFQKILEER-DALILIQWNIR 873
Cdd:PTZ00014 767 QIQREKLAAWEPLVSV-LEALILKIKKKRKVRKNiKSLVRIQAHLR 811
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
159-820 |
4.94e-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: 412.13 E-value: 4.94e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRY---GQwMIYTYSGLFCVTINPYKWLPVYKKEvvaAYKGKRRSEAPPHIFAVANNAFQDMLHNRE---NQ 232
Cdd:cd14891 1 AGILHNLEERSkldNQ-RPYTFMANVLIAVNPLRRLPEPDKS---DYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 233 SILFTGESGAGKTVNSKHIIQY------------FATIAAMSEPRKKPGA-LEEQIMQANIILEAFGNAKTLRNDNSSRF 299
Cdd:cd14891 77 SIVISGESGAGKTETSKIILRFlttravggkkasGQDIEQSSKKRKLSVTsLDERLMDTNPILESFGNAKTLRNHNSSRF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 300 GKFIRMHFGARGM-LSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCS-CGAVTVESL 377
Cdd:cd14891 157 GKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 378 DDAEELLATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKA----AFLMGINSSELVKDL 453
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEAlataAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 454 IHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILE-YNSLEQLCI 532
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 533 NFTNEKLQQFFNRHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKLfDNHF 611
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETL-HKTH 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 612 GKSVHLQKPKPDKKKFEahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFqKSSNRLLASLFEnymstdsaipfgekk 691
Cdd:cd14891 475 KRHPCFPRPHPKDMREM--FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLL-ASSAKFSDQMQE--------------- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 692 rkkgtsfqtaaslhkenlnkLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYAD 771
Cdd:cd14891 537 --------------------LVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAE 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1411134203 772 FKQRYCILNPrTFPKSKFVSSRKA-AEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14891 597 LVDVYKPVLP-PSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
159-788 |
2.11e-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: 411.61 E-value: 2.11e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYK--GKRRS---EAP----PHIFAVANNAFQDMLHN- 228
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 229 RENQSILFTGESGAGKTVNSKHIIQYFATIAAMSE------PRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKF 302
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEgapnegEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 303 IRMHFGARGMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSG-------QKELHDMLLVSAN-PSDFHFCSCG-AVT 373
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGgdeeeheKYEFHDGITGGLQlPNEFHYTGQGgAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 374 VESLDDAEELLATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENAD---KAAFLMGINSSELV 450
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKclaRVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 451 KDLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFT--GILDITGFEILEYNSLE 528
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIRSsvGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 529 QLCINFTNEKLQQFFNRHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGIFSILEEECMFP-KATDLTFKTKL 606
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 607 FDNHFGKSvhlQKPKPDKKKFEAH--------FELVHYAGVVPYNI-SGWLEKNKDLLNETVvavfqkssnrllASLFEN 677
Cdd:cd14908 480 YETYLPEK---NQTHSENTRFEATsiqktkliFAVRHFAGQVQYTVeTTFCEKNKDEIPLTA------------DSLFES 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 678 ymstdsaipfgekkrkkGTSFqtaaslhKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIR 757
Cdd:cd14908 545 -----------------GQQF-------KAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVR 600
|
650 660 670
....*....|....*....|....*....|.
gi 1411134203 758 ICREGFPNRLQYADFKQRYCILNPrTFPKSK 788
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 ... |
159-820 |
2.38e-122 |
|
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: 401.47 E-value: 2.38e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAamsepRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFgARGMLSSVDI 318
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLY-----QDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 319 DIYFLEKSRVIFQQPGERNYHIFYQILSG----QKELhdmLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILG 394
Cdd:cd14896 155 SHYLLETSRVVFQAQAERSFHVFYELLAGldpeEREQ---LSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 395 FLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENAD--KAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIE 472
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 473 QVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFT--GILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVL 550
Cdd:cd14896 312 GAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDAtiGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 551 EQEEYKKESIEWVSIgFGLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKPDKKKFEA 629
Cdd:cd14896 392 EEEECQRELLPWVPI-PQPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQLPLPVFTV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 630 HfelvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENymstdsaipfGEKKRKKGTSFQTAASLHKENL 709
Cdd:cd14896 470 R----HYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE----------AEPQYGLGQGKPTLASRFQQSL 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 710 NKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRtfpKSKF 789
Cdd:cd14896 536 GDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSE---RQEA 612
|
650 660 670
....*....|....*....|....*....|..
gi 1411134203 790 VSSR-KAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14896 613 LSDReRCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
899-1977 |
1.54e-120 |
|
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: 409.95 E-value: 1.54e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 899 RGEEIAGLKEEcaQLQKALE---KSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKE 975
Cdd:pfam01576 2 RQEEEMQAKEE--ELQKVKErqqKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 976 LSERVEEEEEINSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQE 1055
Cdd:pfam01576 80 LESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1056 AHQQTLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMENLESSQRHLAEELR 1135
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1136 KKELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVGGASLAQL 1215
Cdd:pfam01576 240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1216 EITKKQETKFQKLRRDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRA 1295
Cdd:pfam01576 320 ELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1296 KANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEK 1375
Cdd:pfam01576 400 KQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1376 ETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYEnNVIQKTEDLEDAKKELAIRLQETA 1455
Cdd:pfam01576 480 ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE-EDAGTLEALEEGKKRLQRELEALT 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1456 EAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALSTEL 1535
Cdd:pfam01576 559 QQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1536 LKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKILRF 1615
Cdd:pfam01576 639 LSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRL 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1616 QLELLKAKAELERKLSEKDEELENFRRKQQCTIDSMQSSLDSEAKSRIEATRLKKKMEEDLNEMELQLSCANRQVSEATK 1695
Cdd:pfam01576 719 EVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVK 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1696 SLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNT 1775
Cdd:pfam01576 799 QLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKS 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1776 SLLSQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAE 1855
Cdd:pfam01576 879 ALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEME 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1856 QTALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVHNYKQQ 1935
Cdd:pfam01576 959 GTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQ 1038
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|..
gi 1411134203 1936 VEVAEAQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIK 1977
Cdd:pfam01576 1039 LEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
160-820 |
4.97e-120 |
|
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: 397.02 E-value: 4.97e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP------VYKKEVVAAykgkrrSEAPPHIFAVANNAFQDM---LH--- 227
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPglydlhKYREEMPGW------TALPPHVFSIAEGAYRSLrrrLHepg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 228 -NRENQSILFTGESGAGKTVNSKHIIQYFATIA----AMSEPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKF 302
Cdd:cd14895 76 aSKKNQTILVSGESGAGKTETTKFIMNYLAESSkhttATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 303 IRMHFGARGMLSSV-----DIDIYFLEKSRVIFQQPGERNYHIFYQILSG-----QKELHdmlLVSANPSDFHFCSCGAV 372
Cdd:cd14895 156 VRMFFEGHELDTSLrmigtSVETYLLEKVRVVHQNDGERNFHVFYELLAGaaddmKLELQ---LELLSAQEFQYISGGQC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 373 TV--ESLDDAEELLATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENA--------------- 435
Cdd:cd14895 233 YQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvq 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 436 ---DKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDaklSRQF--- 509
Cdd:cd14895 313 qhlDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASP---QRQFaln 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 510 -----------FTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYKKESIEWVSIGFGLDlQACIDLI 578
Cdd:cd14895 390 pnkaankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEML 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 579 E-KPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSvHLQKPKPDKKKFEahFELVHYAGVVPYNISGWLEKNKDLLNE 657
Cdd:cd14895 469 EqRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHS-NFSASRTDQADVA--FQIHHYAGAVRYQAEGFCEKNKDQPNA 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 658 TVVAVFQKSSNRLLASLFENY-MSTDSAIPFGEKKRKKGTSFQTA---ASLHKENLNKLMTNLKSTAPHFVRCINPNVNK 733
Cdd:cd14895 546 ELFSVLGKTSDAHLRELFEFFkASESAELSLGQPKLRRRSSVLSSvgiGSQFKQQLASLLDVVQQTQTHYIRCIKPNDES 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 734 MPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYcilnpRTFPKSKFVSSRKAAeELLGSLKIDHTQyrFG 813
Cdd:cd14895 626 ASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQY-----RLLVAAKNASDATAS-ALIETLKVDHAE--LG 697
|
....*..
gi 1411134203 814 ITKVFFK 820
Cdd:cd14895 698 KTRVFLR 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
159-820 |
3.83e-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: 378.18 E-value: 3.83e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKG-KRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 237
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 238 GESGAGKTVNSKHIIQYFAtiAAMSEPRKkpGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 317
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA--SAKSGNMD--LRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 318 IDIYFLEKSRVIFQQPGERNYHIFYQILSG----QKELHDMLLVSanpsDFHFCSCGAVTVESLDDAEELLATEQAMDIL 393
Cdd:cd14876 157 VVAFLLEKSRIVTQDDNERSYHIFYQLLKGadseMKSKYHLLGLK----EYKFLNPKCLDVPGIDDVADFEEVLESLKSM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 394 GFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAF-----LMGINSSELVKDLIHPRIKVGNEYVTRG 468
Cdd:cd14876 233 GLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISNESLEVFkeacsLLFLDPEALKRELTVKVTKAGGQEIEGR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 469 QTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMF 548
Cdd:cd14876 313 WTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 549 VLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTF----KTKLFDNhfgksvhlQKPKPDK 624
Cdd:cd14876 393 ERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFvsacVSKLKSN--------GKFKPAK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 625 KKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENymstdsaIPFGEKKRKKGtsfQTAASL 704
Cdd:cd14876 465 VDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG-------VVVEKGKIAKG---SLIGSQ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 705 HKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPrTF 784
Cdd:cd14876 535 FLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDL-GI 613
|
650 660 670
....*....|....*....|....*....|....*.
gi 1411134203 785 PKSKFVSSRKAAEELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14876 614 ANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
159-776 |
9.39e-112 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 373.66 E-value: 9.39e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP-VYKKEVVAAYK-------GKRRSEA---PPHIFAVANNAFQDMLH 227
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 228 NRENQSILFTGESGAGKTVNSKHIIQYFA------------TIAAMSEPRKKPGALEEQIMQANIILEAFGNAKTLRNDN 295
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnnnltnSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 296 SSRFGKFIRMHF-GARGMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSG-----QKELHDMLLVSANPSDFHFC-- 367
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLnq 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 368 SCGAVTVESLDDAEELLATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQKP--REEQLEADGTENA---------- 435
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPhkGDDTVFADEARVMssttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 436 DKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQF------ 509
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 510 ---------FTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYKKESIEWVSIGFGLDlQACIDLIE- 579
Cdd:cd14899 401 vddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEh 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 580 KPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETV 659
Cdd:cd14899 480 RPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 660 VAVFQKSSNRLLASL-----FENYMSTDSAIPFGEKKRKKGTSFQTAASL---HKENLNKLMTNLKSTAPHFVRCINPNV 731
Cdd:cd14899 560 AQLLAGSSNPLIQALaagsnDEDANGDSELDGFGGRTRRRAKSAIAAVSVgtqFKIQLNELLSTVRATTPRYVRCIKPND 639
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1411134203 732 NKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRY 776
Cdd:cd14899 640 SHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
159-818 |
5.70e-111 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 369.56 E-value: 5.70e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP-VYKKEVVAAYKGKRRSEA-PPHIFAVANNAFQDMLHNRE--NQSI 234
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 235 LFTGESGAGKTVNSKHIIQYFATIAAMS---EPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARG 311
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPtswESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 312 MLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCSCGAVTVESlDDAEellATEQAMD 391
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNLEE-DCFE---VTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 392 ILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQ---LEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRG 468
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQpcqPMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQVFK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 469 QTIEQVTCAV--GALSKSMYERMFKWLVARINRALDAKLSR-QFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNR 545
Cdd:cd14880 317 KPCSRAECDTrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 546 HMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGIFSILEEECMFPKATDLT-FKTKLfdnhfgKSVHLQKPKPD 623
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSAAqLQTRI------ESALAGNPCLG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 624 KKKF--EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF--------ENYMSTDSAIPfgekkrk 693
Cdd:cd14880 470 HNKLsrEPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFpanpeektQEEPSGQSRAP------- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 694 kgtsFQTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFK 773
Cdd:cd14880 543 ----VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFV 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1411134203 774 QRYCILNPRTFPKSKFVSSRKAAEELLGSLKIdhtqyrfGITKVF 818
Cdd:cd14880 619 ERYKLLRRLRPHTSSGPHSPYPAKGLSEPVHC-------GRTKVF 656
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
159-780 |
3.21e-106 |
|
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: 357.75 E-value: 3.21e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP-VYKKEVVAAYKGKRR-SEAPPHIFAVANNAFQDMLHNRENQSILF 236
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 237 TGESGAGKTVNSKHIIQYF-----ATIAAMSEPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHF-GAR 310
Cdd:cd14906 81 SGESGSGKTEASKTILQYLintssSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 311 GMLSSVDIDIYFLEKSRvIFQQPGERN--YHIFYQILSG-QKELHDMLLVSANPSDFHFCSCGAVTVESL---------- 377
Cdd:cd14906 161 GKIDGASIETYLLEKSR-ISHRPDNINlsYHIFYYLVYGaSKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsn 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 378 -----DDAEELLATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQKP---REEQLEADGTENADKAAFLMGINSSEL 449
Cdd:cd14906 240 hnnktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 450 VKDLIHPRIKVGNE--YVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRA---------LDAKLSRQ--FFTGILDI 516
Cdd:cd14906 320 KQALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKfnqntqsndLAGGSNKKnnLFIGVLDI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 517 TGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGIFSILEEECMFP 595
Cdd:cd14906 400 FGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMP 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 596 KATDLTFKTKlfdnhFGKSVHlQKPKPDKKKF-EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASL 674
Cdd:cd14906 479 KGSEQSLLEK-----YNKQYH-NTNQYYQRTLaKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 675 FENYMSTDSaipfgeKKRKKGTSFQTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLE 754
Cdd:cd14906 553 FQQQITSTT------NTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLN 626
|
650 660
....*....|....*....|....*..
gi 1411134203 755 GIRICREGFPNRLQYADFKQRY-CILN 780
Cdd:cd14906 627 TIKVRKMGYSYRRDFNQFFSRYkCIVD 653
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
159-820 |
1.65e-105 |
|
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: 354.69 E-value: 1.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAAMSEPRKKPgaleEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 318
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSV----EKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 319 DIYFLEKSRVIFQQPGERNYHIFYQILSG-----QKELHDMLLVSANPSDFHFCSCGAvtvESLDDAEELLATEQAMDIL 393
Cdd:cd01386 157 QTLLLERSRVARRPEGESNFNVFYYLLAGadaalRTELHLNQLAESNSFGIVPLQKPE---DKQKAAAAFSKLQAAMKTL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 394 GFLPDEKYGCFKLTGAIMHFGN---MKFKQKPREEQLEadgTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQT 470
Cdd:cd01386 234 GISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFAR---PEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 471 IEQVTC------------AVGALSKSMYERMFKWLVARINRALDaklSRQFFTG---ILDITGFEILEYN------SLEQ 529
Cdd:cd01386 311 QESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLS---SSHHSTSsitIVDTPGFQNPAHSgsqrgaTFED 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 530 LCINFTNEKLQQFFNRHMFVLEQEEYKKESIEwVSIGFGLD-LQACIDLIEK---------------PMGIFSILEEECM 593
Cdd:cd01386 388 LCHNYAQERLQLLFHERTFVAPLERYKQENVE-VDFDLPELsPGALVALIDQapqqalvrsdlrdedRRGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 594 FPKATDLTFKTKLFdNHFGKSVHLQKPKPDKKKFEA-HFELVHYAGV--VPYNISGWLEKNK-DLLNETVVAVFQkSSNR 669
Cdd:cd01386 467 YPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQ-ESQK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 670 LLASLfenymstdsaipfgekkRKKGTSFQTaaslhKENLNKLMTNLKSTAPHFVRCINPNVNKMPG------------I 737
Cdd:cd01386 545 ETAAV-----------------KRKSPCLQI-----KFQVDALIDTLRRTGLHFVHCLLPQHNAGKDerstsspaagdeL 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 738 LDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNP----RTFPKSKFVSSRKAAEELLGSLKIDHTQYRFG 813
Cdd:cd01386 603 LDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkKLGLNSEVADERKAVEELLEELDLEKSSYRIG 682
|
....*..
gi 1411134203 814 ITKVFFK 820
Cdd:cd01386 683 LSQVFFR 689
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
159-820 |
1.26e-100 |
|
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: 339.48 E-value: 1.26e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMI-YTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEA-PPHIFAVANNAF-QDMLHNRENQSIL 235
Cdd:cd14875 1 ATLLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 236 FTGESGAGKTVNSKHIIQYFATIAAM----SEPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHF-GAR 310
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMhssnTSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFdPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 311 GMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSG-----QKELHDMllvsANPSDFHFCSCG------AVTVESLDD 379
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGlspeeKKELGGL----KTAQDYKCLNGGntfvrrGVDGKTLDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 380 AEELLATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENAdKAAFLMGINSsELVKDLIhpRIK 459
Cdd:cd14875 237 AHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDP-AKLRECF--LVK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 460 VGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKL--SRQFFTGILDITGFEILEYNSLEQLCINFTNE 537
Cdd:cd14875 313 SKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQLCINYANE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 538 KLQQFFNRHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVH 616
Cdd:cd14875 393 SLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 617 LQKPK---PDKkkfeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFenymSTDSaipfGEKKRK 693
Cdd:cd14875 472 FVLPKstiPNQ------FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL----STEK----GLARRK 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 694 kgtsfQTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFK 773
Cdd:cd14875 538 -----QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFC 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1411134203 774 QRYCILNPRTfPKSKFVSSR--KAAEELLGS----LKIDHTQYRFGITKVFFK 820
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 ... |
159-820 |
9.95e-100 |
|
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: 336.47 E-value: 9.95e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP-VYKKEVVAAYKGKRRS-----EAPPHIFAVANNAFQDMLHNRENQ 232
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 233 SILFTGESGAGKTVNSKHIIQYFATiaamsEPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 312
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAY-----GHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 313 LSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSG----QKELHDMLLVSAnpsdFHFCSCG-AVTVESLDDAEELLATE 387
Cdd:cd14886 156 LKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGlspeEKKSLGFKSLES----YNFLNASkCYDAPGIDDQKEFAPVR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 388 QAMDILgFLPDEKYGCFKLTGAIMHFGNMKFKQKPR---EEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEY 464
Cdd:cd14886 232 SQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNET 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 465 VTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFN 544
Cdd:cd14886 311 IISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 545 RHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIEKP-MGIFSILEEECMFPKATDLTF----KTKLFDNHFGKSvhlqk 619
Cdd:cd14886 391 NQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFtsscKSKIKNNSFIPG----- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 620 pkpdkKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIpfgeKKRKKGTSFQ 699
Cdd:cd14886 465 -----KGSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNM----KGKFLGSTFQ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 700 TAaslhkenLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCIL 779
Cdd:cd14886 536 LS-------IDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKIL 608
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1411134203 780 NPRTFPKSKFVSSRKAA-EELLGSLKIDHTQYRFGITKVFFK 820
Cdd:cd14886 609 ISHNSSSQNAGEDLVEAvKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
159-820 |
3.43e-97 |
|
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: 329.47 E-value: 3.43e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAY---KGKRRSEAPPHIFAVANNAFQDMLHNRENQSIL 235
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 236 FTGESGAGKTVNSKHIIQYFATIAAMSEPrkkpgALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGAR-GMLS 314
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT-----TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERkKHLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 315 SVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCSCGA----VTVESLDDAEELLATEQAM 390
Cdd:cd14878 156 GARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredvSTAERSLNREKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 391 DILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQT 470
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 471 IEQVTCAVGALSKSMYERMFKWLVARINRAL----DAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRH 546
Cdd:cd14878 316 IQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 547 MFVLEQEEYKKESIEWVSIGFGLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKL---FDNHFGKSVHLQKP-- 620
Cdd:cd14878 396 LFLQEQTECVQEGVTMETAYSPGNQTGVLDFFfQKPSGFLSLLDEESQMIWSVEPNLPKKLqslLESSNTNAVYSPMKdg 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 621 --KPDKKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTdsaipfgekkrkkgtsf 698
Cdd:cd14878 476 ngNVALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLVT----------------- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 699 qtAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCI 778
Cdd:cd14878 539 --IASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKP 616
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1411134203 779 LNPRTFPKSKFVSSRKAAEELLGSLKIDHTQyrFGITKVFFK 820
Cdd:cd14878 617 LADTLLGEKKKQSAEERCRLVLQQCKLQGWQ--MGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
159-820 |
1.18e-96 |
|
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: 326.97 E-value: 1.18e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEvvaaYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAamseprKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 318
Cdd:cd14937 77 ESGSGKTEASKLVIKYYLSGV------KEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 319 DIYFLEKSRVIFQQPGERNYHIFYQILSG-QKELHDMLLVSANpSDFHFCSCGAVTVESLDDAEELLATEQAMDILGfLP 397
Cdd:cd14937 151 EIFLLENIRVVSQEEEERGYHIFYQIFNGmSQELKNKYKIRSE-NEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMN-MH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 398 DEKYGCFKLTGAIMHFGNMKFKQ-----KPREEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIE 472
Cdd:cd14937 229 DMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 473 QVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQ 552
Cdd:cd14937 309 ESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKET 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 553 EEYKKESIEWVSIGFGLDlQACIDLIEKPMGIFSILEEECMFPKATDLTFkTKLFDNHFGKSVHLQKPKPDKKKfeaHFE 632
Cdd:cd14937 389 ELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYASTKKDINK---NFV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 633 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAipfgekKRKKGTSFQtaaslHKENLNKL 712
Cdd:cd14937 464 IKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESL------GRKNLITFK-----YLKNLNNI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 713 MTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRIcREGFPNRLQYADFKQRYCILNPRTFPKSKFVSS 792
Cdd:cd14937 533 ISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDK 611
|
650 660
....*....|....*....|....*...
gi 1411134203 793 RKAAEELLGSlkIDHTQYRFGITKVFFK 820
Cdd:cd14937 612 EKVSMILQNT--VDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
160-784 |
1.76e-91 |
|
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: 310.29 E-value: 1.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKwlPVYKKEVVAAYKgKRRSEAPPHIFAVANNAFQDMLHNrENQSILFTGE 239
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 240 SGAGKTVNSKHIIQYFATIAAMSEprkkpgALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFgaRGMLSSVDID 319
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKITGAKFE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 320 IYFLEKSRVIFQQPGERNYHIFYQILSGQKelhdmlLVSANpsDFHFCSCGAVTVESLDD-AEELLATEQAMDILGFLPD 398
Cdd:cd14898 150 TYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKN--DFIDTSSTAGNKESIVQlSEKYKMTCSAMKSLGIANF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 399 EKYGCFKLtgAIMHFGNMKFKQkprEEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQVTCAV 478
Cdd:cd14898 222 KSIEDCLL--GILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 479 GALSKSMYERMFKWLVARINRALDAKLSRQFftGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYKKE 558
Cdd:cd14898 297 NSMARLLYSNVFNYITASINNCLEGSGERSI--SVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 559 SIEWVSIGFgLDLQACIDLIEKPMGIFSILEEECMFPKAT--DLTFKTKLFDNHFGKSvhlqkpkpdkkKFEAHFELVHY 636
Cdd:cd14898 375 GIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNGFINT-----------KARDKIKVSHY 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 637 AGVVPYNISGWLEKNKdllnetvvavfQKSSNRllasLFENYMSTDSaipfgEKKRKKGTSFqtaaslhKENLNKLMTNL 716
Cdd:cd14898 443 AGDVEYDLRDFLDKNR-----------EKGQLL----IFKNLLINDE-----GSKEDLVKYF-------KDSMNKLLNSI 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411134203 717 KSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTF 784
Cdd:cd14898 496 NETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLF 563
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
174-820 |
1.96e-82 |
|
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: 288.09 E-value: 1.96e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 174 IYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGESGAGKTVNSKHIIQ 253
Cdd:cd14887 24 IYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQSILISGESGAGKTETSKHVLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 254 YfatIAAMSEPRK--KPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDIDIYFLEKSRVIFQ 331
Cdd:cd14887 104 Y---LAAVSDRRHgaDSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 332 QPGERNYHIFYQILSGQKELHDMLLVSAnpsdfhfcscgavtvESLDDAEELLATEQAMDILGFLPDEKYGCFKLTGAIM 411
Cdd:cd14887 181 PSDEFSFHIFYALCNAAVAAATQKSSAG---------------EGDPESTDLRRITAAMKTVGIGGGEQADIFKLLAAIL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 412 HFGNMKF--KQKPRE-------------EQLEADGTENADKAAFLMGINSSE--------LVKDLIHPRIKVGNEYV--- 465
Cdd:cd14887 246 HLGNVEFttDQEPETskkrkltsvsvgcEETAADRSHSSEVKCLSSGLKVTEasrkhlktVARLLGLPPGVEGEEMLrla 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 466 --------TRGQ-TIEQVTCAVGALSKSMYERMFKWLVARINRAL-------------DAKLSRQF-FTGILDITGFEIL 522
Cdd:cd14887 326 lvsrsvreTRSFfDLDGAAAARDAACKNLYSRAFDAVVARINAGLqrsakpsesdsdeDTPSTTGTqTIGILDLFGFEDL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 523 E---YNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYKKES--IEWVSIGFGLDLQACIDLIEKP---------------- 581
Cdd:cd14887 406 RnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCSAFPFSFPLASTLTSSPsstspfsptpsfrsss 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 582 --------MGIFSILEEE-CMFPKATDLTFKTKLFDNHFGK----SVHLQKPKPDKKKFEAHFELVHYAGVVPYNISGWL 648
Cdd:cd14887 486 afatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKNITPALSRENLEFTVSHFACDVTYDARDFC 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 649 EKNKDLLNETVVAVFQKSSNRLLaslfENYMSTDSAIPFGEKKRKkgtsfqTAASLHKENLNKLMTNLKSTAPHFVRCIN 728
Cdd:cd14887 566 RANREATSDELERLFLACSTYTR----LVGSKKNSGVRAISSRRS------TLSAQFASQLQQVLKALQETSCHFIRCVK 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 729 PNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPRTFpkSKFVSSRKAAEELLGSLKIDHT 808
Cdd:cd14887 636 PNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMAL--REALTPKMFCKIVLMFLEINSN 713
|
730
....*....|..
gi 1411134203 809 QYRFGITKVFFK 820
Cdd:cd14887 714 SYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
156-819 |
1.26e-81 |
|
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: 283.67 E-value: 1.26e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 156 LNEASVLHALKRRYGQWMIYTY---SGLfcVTINPYKWLPVYKKEVVAAYK-------GKRRSEAPPHIFAVANNAFQDM 225
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 226 LHNRENQSILFTGESGAGKTVNSKHIIQyfaTIAAMSEPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRM 305
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLR---QLLRLSSHSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 306 HFGARGMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSG-QKELHDMLLVSaNPSDF-----HFCSCGAVTVESlDD 379
Cdd:cd14879 156 QFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGaSPEERQHLGLD-DPSDYallasYGCHPLPLGPGS-DD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 380 AEELLATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFkqkpreeQLEADGTENA---------DKAAFLMGINSSELV 450
Cdd:cd14879 234 AEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEF-------TYDHEGGEESavvkntdvlDIVAAFLGVSPEDLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 451 KDLIHpRIKvgneYVTRgqtiEQVTC---AVGA------LSKSMYERMFKWLVARINRALdAKLSRQF--FTGILDITGF 519
Cdd:cd14879 307 TSLTY-KTK----LVRK----ELCTVfldPEGAaaqrdeLARTLYSLLFAWVVETINQKL-CAPEDDFatFISLLDFPGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 520 EIL---EYNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYKKE--SIEWVSIgfgLDLQACIDLI-EKPMGIFSILEEEC- 592
Cdd:cd14879 377 QNRsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEgvSVPATSY---FDNSDCVRLLrGKPGGLLGILDDQTr 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 593 MFPKATDLTFKTKL---FDNHfgKSVHLQKPKPDKKKFeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVavfqkssnr 669
Cdd:cd14879 454 RMPKKTDEQMLEALrkrFGNH--SSFIAVGNFATRSGS-ASFTVNHYAGEVTYSVEGFLERNGDVLSPDFV--------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 670 llaSLFenymstdsaipfgekkrkKGTSFQTAAslhkenLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRC 749
Cdd:cd14879 522 ---NLL------------------RGATQLNAA------LSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRS 574
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 750 NGVLEGIRICREGFPNRLQYADFKQRYCilnprtfPKSKFVSSRKAAEELLGSLKIDHTQYRFGITKVFF 819
Cdd:cd14879 575 LGLPELAARLRVEYVVSLEHAEFCERYK-------STLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
159-767 |
3.34e-73 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 259.84 E-value: 3.34e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP-VYKKEVVAAYKGKRRSEA-------PPHIFAVANNAFQDMLHNRE 230
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 231 NQSILFTGESGAGKTVNSKHIIQYFATIAAMSEPRKkpgaLEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGAR 310
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTE----RIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 311 ---------GMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSG--QKELHDMLLVS-------ANPSDFHFCSCGAV 372
Cdd:cd14884 157 entqknmfnGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlsDEDLARRNLVRncgvyglLNPDESHQKRSVKG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 373 TVESLDDAEELLATEQAMDILGF------LPDEKYGCFKLT------GAIMHFGNMKFKQkpreeqleadgtenadkAAF 440
Cdd:cd14884 237 TLRLGSDSLDPSEEEKAKDEKNFvallhgLHYIKYDERQINeffdiiAGILHLGNRAYKA-----------------AAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 441 LMGINSSELVKDLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRAL------------DAKLSRQ 508
Cdd:cd14884 300 CLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdneDIYSINE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 509 FFTGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYKKESIEWVSIgfglDLQACIDLIEKPMGIFSIL 588
Cdd:cd14884 380 AIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSD----VAPSYSDTLIFIAKIFRRL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 589 EEECMFP----KATDLTFKTKLFDNH----------FGK-SVHLQKPKPDKKKFEAH-FELVHYAGVVPYNISGWLEKNK 652
Cdd:cd14884 456 DDITKLKnqgqKKTDDHFFRYLLNNErqqqlegkvsYGFvLNHDADGTAKKQNIKKNiFFIRHYAGLVTYRINNWIDKNS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 653 DLLNETVVAVFQKSSNRLLASLFENymstdsaipfgekkrKKGTSFQTAASLHKENLNKLMTNLKSTAPHFVRCINPNVN 732
Cdd:cd14884 536 DKIETSIETLISCSSNRFLREANNG---------------GNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAK 600
|
650 660 670
....*....|....*....|....*....|....*
gi 1411134203 733 KMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRL 767
Cdd:cd14884 601 MLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKI 635
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
160-786 |
1.61e-70 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 250.42 E-value: 1.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKwlpvykkEVVAA--YKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 237
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYR-------DVGNPltLTSTRSSPLAPQLLKVVQEAVRQQSETGYPQAIILS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 238 GESGAGKTVNSKHIIQYFATIAAmseprkkpGALE----EQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFgARGML 313
Cdd:cd14881 75 GTSGSGKTYASMLLLRQLFDVAG--------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDGAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 314 SSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSG--QKELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 391
Cdd:cd14881 146 YRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGlsQEERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKACLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 392 ILG--FLpdekyGCFKLTGAIMHFGNMKFKQKPREEQLEADGTEnADKAAFLMGINSSELVKDLIhprIKVGNeyvTRGQ 469
Cdd:cd14881 226 ILGipFL-----DVVRVLAAVLLLGNVQFIDGGGLEVDVKGETE-LKSVAALLGVSGAALFRGLT---TRTHN---ARGQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 470 TIEQVtCAVG-------ALSKSMYERMFKWLVARIN--RALDAKLSRQF---FTGILDITGFEILEYNSLEQLCINFTNE 537
Cdd:cd14881 294 LVKSV-CDANmsnmtrdALAKALYCRTVATIVRRANslKRLGSTLGTHAtdgFIGILDMFGFEDPKPSQLEHLCINLCAE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 538 KLQQFFNRHMFVLEQEEYKKESIEW-VSIGFgLDLQACIDLIEK-PMGIFSILEEECMfPKATDLTFKTKLFDNHFGKSV 615
Cdd:cd14881 373 TMQHFYNTHIFKSSIESCRDEGIQCeVEVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPR 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 616 HLQKPKPDKKKfeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSnrllaslfenymstdsaIPFGekkrkkg 695
Cdd:cd14881 451 LFEAKPQDDRM----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN-----------------CNFG------- 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 696 tsFQTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQR 775
Cdd:cd14881 503 --FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNAR 580
|
650
....*....|.
gi 1411134203 776 YCILNPRTFPK 786
Cdd:cd14881 581 YRLLAPFRLLR 591
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
160-820 |
1.24e-68 |
|
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: 245.04 E-value: 1.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 239
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 240 SGAGKTVNSKHIIQYFATIAAMseprkKPGAlEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDID 319
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDG-----NRGA-TGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 320 IYFLEKSRVIFQQPGERNYHIFYQI---LSGQKELHDMLL------------VSANPSDFHFC-SCGAVTVESLDDAEEL 383
Cdd:cd14882 156 MYQLEKLRVSTTDGNQSNFHIFYYFydfIEAQNRLKEYNLkagrnyrylripPEVPPSKLKYRrDDPEGNVERYKEFEEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 384 LateQAMDilgFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEadGTENADKAAFLMGINSSELVKDLIHPRIKVGNE 463
Cdd:cd14882 236 L---KDLD---FNEEQLETVRKVLAAILNLGEIRFRQNGGYAELE--NTEIASRVAELLRLDEKKFMWALTNYCLIKGGS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 464 YVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINraldAKLS--RQFF-----TGILDITGFEILEYNSLEQLCINFTN 536
Cdd:cd14882 308 AERRKHTTEEARDARDVLASTLYSRLVDWIINRIN----MKMSfpRAVFgdkysISIHDMFGFECFHRNRLEQLMVNTLN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 537 EKLQQFFNRHMFVLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPMGIFSILEEECmfpkatdltfKTKLFDNHFGKSVH 616
Cdd:cd14882 384 EQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDAS----------RSCQDQNYIMDRIK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 617 lQKPKPDKKKFEAH-FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMStdsaipfgEKKRKKG 695
Cdd:cd14882 454 -EKHSQFVKKHSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQV--------RNMRTLA 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 696 TSFQtAASLhkENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQR 775
Cdd:cd14882 525 ATFR-ATSL--ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRR 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1411134203 776 YCILnprTFPKSKFVS-SRKAAEELLGSLKIDhtQYRFGITKVFFK 820
Cdd:cd14882 602 YQFL---AFDFDETVEmTKDNCRLLLIRLKME--GWAIGKTKVFLK 642
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
159-779 |
3.60e-68 |
|
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: 243.62 E-value: 3.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 159 ASVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYkgkrrseappHIFAVANNAFQDMLHNREN-QSILFT 237
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 238 GESGAGKTVNSKHIIQYFAtiaamSEPRKKPGALEEQIMQAniILEAFGNAKTLRNDNSSRFGKFIRMHFgARGMLSSVD 317
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT-----SQPKSKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 318 IDIYF-LEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFL 396
Cdd:cd14874 143 LKYTVpLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 397 PDEKYGCFKLTGAIMHFGNMKFKQKPR---EEQLEADGTENADK-AAFLMGINSSELVKDLIhPRIKVGNEYvtrgqTIE 472
Cdd:cd14874 223 DDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKwVAFLLEVDFDQLVNFLL-PKSEDGTTI-----DLN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 473 QVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTgILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQ 552
Cdd:cd14874 297 AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGVIS-ILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 553 EEYKKESIEwvsigfgLDLQ--ACID-------LIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPD 623
Cdd:cd14874 376 VDYAKDGIS-------VDYKvpNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 624 KKKFEAHfelvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIpfgekkrkkgtsFQTAAS 703
Cdd:cd14874 449 RLEFGVR----HCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDM------------IVSQAQ 512
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411134203 704 LHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRY-CIL 779
Cdd:cd14874 513 FILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYrCLL 589
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
160-784 |
5.02e-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: 244.23 E-value: 5.02e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKWLP-VYKKEVVAAYKGKRrsEAPPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFATIAAmseprKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 318
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDL-----SRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 319 DIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCS-CGAVTVESLDDAEELLATEQAMDILGFlP 397
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNqGGSISVESIDDNRVFDRLKMSFVFFDF-P 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 398 DEKYG-CFKLTGAIMHFGNMKFKQKprEEQLEADGTENADKAAFLMGINSSELVKDLIHPRIKVGNEYVTRGQTieqvtc 476
Cdd:cd14905 234 SEKIDlIFKTLSFIIILGNVTFFQK--NGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENRDS------ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 477 avgaLSKSMYERMFKWLVARINRALDAKLSRQFFtGILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYK 556
Cdd:cd14905 306 ----LARSLYSALFHWIIDFLNSKLKPTQYSHTL-GILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 557 KESIEWVS-IGFGlDLQACIDLIEKpmgIFSILEEECMFPKATDLTFKTKLfdNHFGKSVHLQKPKPDKkkfeahFELVH 635
Cdd:cd14905 381 TERIPWMTpISFK-DNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--QNFLSRHHLFGKKPNK------FGIEH 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 636 YAGVVPYNISGWLEKNKDL-------------------------LNETVVAVFQ-----KSSNRLLASLFENYMSTDSAI 685
Cdd:cd14905 449 YFGQFYYDVRGFIIKNRDEilqrtnvlhknsitkylfsrdgvfnINATVAELNQmfdakNTAKKSPLSIVKVLLSCGSNN 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 686 P------------------FGEKKRKKGTSFQTAASLHKEnlnklmTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQL 747
Cdd:cd14905 529 PnnvnnpnnnsgggggggnSGGGSGSGGSTYTTYSSTNKA------INNSNCDFHFIRCIKPNSKKTHLTFDVKSVNEQI 602
|
650 660 670
....*....|....*....|....*....|....*....
gi 1411134203 748 RCNGVLEGIRICREGFPNRLQYADFKQRYCIL--NPRTF 784
Cdd:cd14905 603 KSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFfqNQRNF 641
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
162-819 |
6.39e-68 |
|
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: 245.65 E-value: 6.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 162 LHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRR----------SEAPPHIFAVANNAFQDMLHNREN 231
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 232 QSILFTGESGAGKTVNSKHIIQYFATIAAMSEPRK----KPGALE---EQIMQANIILEAFGNAKTLRNDNSSRFGKFIR 304
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPdsegASGVLHpigQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 305 MHFGARGMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKE---LHDMLLVSANPSDFHFCSCGA--VTVESLD- 378
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdptLRDSLEMNKCVNEFVMLKQADplATNFALDa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 379 -DAEELLATEQAMDIlgfLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQLEADGTENA----------DKAAFLMginSS 447
Cdd:cd14893 244 rDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTvsdaqscalkDPAQILL---AA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 448 ELVKdlIHPRI------------KVGNEYVTRGQ--TIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFTGI 513
Cdd:cd14893 318 KLLE--VEPVVldnyfrtrqffsKDGNKTVSSLKvvTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRYEKSNI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 514 ---------LDITGFEILE--YNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYKKESIEW-------VSIGFGLDLQACI 575
Cdd:cd14893 396 vinsqgvhvLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVenrltvnSNVDITSEQEKCL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 576 DLIE-KPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVhLQKPKPD----------KKKFEAHFELVHYAGVVPYNI 644
Cdd:cd14893 476 QLFEdKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGG-LSRPNMGadttneylapSKDWRLLFIVQHHCGKVTYNG 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 645 SGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYM---STDSAIPFGEKKRKKGTSFQTAASLHKENLN----------- 710
Cdd:cd14893 555 KGLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMaaaSSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvyn 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 711 ---KLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYcilnprtfpkS 787
Cdd:cd14893 635 qadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY----------K 704
|
730 740 750
....*....|....*....|....*....|....*.
gi 1411134203 788 KFVSSRKAAEELLGSLK----IDHTQYRFGITKVFF 819
Cdd:cd14893 705 NVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
181-305 |
1.95e-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: 1.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 181 FCVTINPYKWLPVYKKEVV-AAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGESGAGKTVNSKHIIQYFATIA 259
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1411134203 260 A----------MSEPRKKPGALEEQIMQANIILEAFGNAKTLRNDNSSRFGKFIRM 305
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 ... |
160-818 |
1.01e-48 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 187.35 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 160 SVLHALKRRYGQWMIYTYSGLFCVTINPYKWLPVYKKEVVAAYKGKRRSE-APPHIFAVANNAFQDMLHNRENQSILFTG 238
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 239 ESGAGKTVNSKHIIQYFA--TIAAMSEPRKKPGALE----------------EQIMQANIILEAFGNAKTLRNDNSSRFG 300
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAyqVKGSRRLPTNLNDQEEdnihneentdyqfnmsEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 301 KFIRMHFGARgMLSSVDIDIYFLEKSRVIFQQPGERNYHIFYQILSGQKELHDMLLVSANPSDFHFCSCGAVTVESLDDA 380
Cdd:cd14938 162 KFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 381 EELLATEQAMDILGFLPDEKYGCFKLTGAIMHFGNMKFKQKPREEQL-----------------------EADGTENADK 437
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRKKSLlmgknqcgqninyetilselensEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 438 ----AAFLMGINSSELVK---------DLIhpRIKVGNEyvtrgqtiEQVTCAVGALSKSMYERMFKWLVARINRALDAK 504
Cdd:cd14938 321 nlllACKLLSFDIETFVKyfttnyifnDSI--LIKVHNE--------TKIQKKLENFIKTCYEELFNWIIYKINEKCTQL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 505 LSRQFFT---GILDITGFEILEYNSLEQLCINFTNEKLQQFFNRHMFVLEQEEYKKESIEWVSIGFGLDLQACIDLIEKP 581
Cdd:cd14938 391 QNININTnyiNVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 582 M--GIFSILEEECMfPKATDLTFKTKLFDNHFGKSVHLQKpKPDKKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETV 659
Cdd:cd14938 471 TegSLFSLLENVST-KTIFDKSNLHSSIIRKFSRNSKYIK-KDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRF 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 660 VAVFQKSSNRLLASL--FENYMSTDS--------AIPFGEK--KRKKGTSFQTAASLHKENLNKLMTNLKSTAPHFVRCI 727
Cdd:cd14938 549 IDMVKQSENEYMRQFcmFYNYDNSGNiveekrrySIQSALKlfKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCM 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 728 NPNVNK-MPGILDPYLVLQQLRCNGVLEGIRICREGFPNRLQYADFKQRYCILNPrtfpkskfvSSRKAAEELLGSLKID 806
Cdd:cd14938 629 KPNESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQIS 699
|
730
....*....|..
gi 1411134203 807 HTQYRFGITKVF 818
Cdd:cd14938 700 NYEWMIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1227-1992 |
8.58e-31 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 133.26 E-value: 8.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1227 KLRRDMEEATLHFEATSASLKkRHADSLAELEGQVENLQ-QVKQ-----KLEKDRSDLQLEVddLLTRIEQMTRAKANAE 1300
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLD-RLEDILNELERQLKSLErQAEKaerykELKAELRELELAL--LVLRLEELREELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1301 KLCTLYEERLNEANAKLDKVTqlandlaAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQ 1380
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELE-------EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1381 SALAHALQKAQRDCDLLRE---QYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQKTEDLEDAKKELAIRLQETAEA 1457
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEelaELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1458 MG---VANARNASLERARHRLQLELGDALSDLgkVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALSTE 1534
Cdd:TIGR02168 399 NNeieRLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1535 LLKLKHAYKESIVGQETLrrenKNLQEEISNLTNQVREGTKNLTEMEK----VKKLIEQEK---TEVQVTLEETEGALER 1607
Cdd:TIGR02168 477 LDAAERELAQLQARLDSL----ERLQENLEGFSEGVKALLKNQSGLSGilgvLSELISVDEgyeAAIEAALGGRLQAVVV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1608 NESKILRFQLELLKaKAELERKL-----SEKDEELENFRRKQQCTIDSMQSSLDSEAKSRIE------------------ 1664
Cdd:TIGR02168 553 ENLNAAKKAIAFLK-QNELGRVTflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkalsyllggvlvvddl 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1665 --ATRLKKKMEEDLNEMELQLSCANRQ------VSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQ 1736
Cdd:TIGR02168 632 dnALELAKKLRPGYRIVTLDGDLVRPGgvitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1737 SELEDLRSLQEQTERGRRLSEEELLEATERINlfytqntsllsqkkKLEADVAQMQKEAEEVVQEcqnaeekakkaateA 1816
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVE--------------QLEERIAQLSKELTELEAE--------------I 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1817 ANLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEqTALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARR 1896
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-EALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1897 LERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVHNYKQQVEVAEAQANQYLSKYKKQQHELNEVkeraevaESQVNKLKI 1976
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL-------ESKRSELRR 915
|
810
....*....|....*.
gi 1411134203 1977 KAREFGKKVRQAQTEL 1992
Cdd:TIGR02168 916 ELEELREKLAQLELRL 931
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
996-1850 |
1.88e-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: 128.64 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 996 KLEDECSELKKEIDDLETMLVKSEK------EKRTTEHKVknLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEE 1069
Cdd:TIGR02168 190 RLEDILNELERQLKSLERQAEKAERykelkaELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1070 KLSSLSKANLKLEQQVVGLEGALEQERKarincerELHKLEGDLKLNQESMENLESSQRHLAEELRKKElensqmnSKVE 1149
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALAN-------EISRLEQQKQILRERLANLERQLEELEAQLEELE-------SKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1150 NEKGLVAQLQKMVKELQTQIKDLKEKLEaerttraKMEKERADLTQDLADLNERLEEVGGASLAQLEITKKQETKFQKLR 1229
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELE-------ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1230 RDMEeatlhfeatsaSLKKRHADSLAELEGQVENLQqvkqklEKDRSDLQLEVDDLLTRIEQMTRAKANAEKLCTLYEER 1309
Cdd:TIGR02168 407 ARLE-----------RLEDRRERLQQEIEELLKKLE------EAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1310 LNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSALAHALQ- 1388
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQa 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1389 -------KAQRDCDLLREQYEEEQ---EVKAELHRTLSKVNAEMVQWRMKYENNVIQKTEDLEDAKKELAIRLQETAEAM 1458
Cdd:TIGR02168 550 vvvenlnAAKKAIAFLKQNELGRVtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1459 GVANA-RNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALSTELLK 1537
Cdd:TIGR02168 630 DLDNAlELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEE 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1538 LKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKILRFQL 1617
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1618 ELLKAKAEL---ERKLSEKDEELENFRR---KQQCTIDSMQSSLDSEAKSRIEATRLKKKMEEdlnemelqlscanrQVS 1691
Cdd:TIGR02168 790 QIEQLKEELkalREALDELRAELTLLNEeaaNLRERLESLERRIAATERRLEDLEEQIEELSE--------------DIE 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1692 EATKSLGQLQIQIKDLQMQLDDstqlnsdLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFY 1771
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEA-------LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1772 TQNTSLLSQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAA-------------NLS-----EELKKKQDTIAH- 1832
Cdd:TIGR02168 929 LRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLkrlenkikelgpvNLAaieeyEELKERYDFLTAq 1008
|
890 900
....*....|....*....|.
gi 1411134203 1833 ---LEKTRENMEQTITDLQKR 1850
Cdd:TIGR02168 1009 kedLTEAKETLEEAIEEIDRE 1029
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
889-1801 |
3.73e-27 |
|
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: 121.32 E-value: 3.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 889 KIKPLVKSSERGEEIAGLKEECAQLQKALEKSEFqrEELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQ 968
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELRELELALLVLRL--EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 969 LEARVkelserveeeeeinseltargRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNR 1048
Cdd:TIGR02168 279 LEEEI---------------------EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1049 AAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMENLESSQR 1128
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1129 HLAEELRkkELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEevg 1208
Cdd:TIGR02168 418 RLQQEIE--ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD--- 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1209 gaslaqleitkkqetkfqKLRRDMEEATLHFEATSASLKKRHAdsLAELEGQVENLQQVKQKLEKDRS-DLQLEVDDLLT 1287
Cdd:TIGR02168 493 ------------------SLERLQENLEGFSEGVKALLKNQSG--LSGILGVLSELISVDEGYEAAIEaALGGRLQAVVV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1288 RIEQMTRAKANAEKlctlyeerlneaNAKLDKVTQLANDLAAQkTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIE 1367
Cdd:TIGR02168 553 ENLNAAKKAIAFLK------------QNELGRVTFLPLDSIKG-TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1368 ELRGQLeketksqsALAHALQKAQRdcdLLREQYEEEQEVKAELHRTL---------SKVNAEMVQWRMKYENNViQKTE 1438
Cdd:TIGR02168 620 YLLGGV--------LVVDDLDNALE---LAKKLRPGYRIVTLDGDLVRpggvitggsAKTNSSILERRREIEELE-EKIE 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1439 DLEDAKKELAIRLQETAEAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQ 1518
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1519 TLLDASRKEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTL 1598
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1599 EETEGALERNESKILRFQLELLKAKAELERKLSEKDEELENfrrkqqctIDSMQSSLDSEAKSRIEATRLKKKMEEDLNE 1678
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA--------LALLRSELEELSEELRELESKRSELRRELEE 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1679 MELQLSCANRQVSEATKSLGQLQIQIKDL-QMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEqtergrrLSE 1757
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNL-------AAI 992
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 1411134203 1758 EELLEATERINLFYTQNTSLLSQKKKLEADVAQMQKEAEEVVQE 1801
Cdd:TIGR02168 993 EEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
275-760 |
2.54e-26 |
|
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: 117.92 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 275 IMQANIILEAFGNAKTLRNDNSSRFGKF--IRMHFGARG---MLSSVDIDIYFLEKSRVIFQQ------PGERNYHIFYQ 343
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 344 ILSG----------QKELH-DMLLVSA----NPSDFHFCscGAVTVESL--DDAEELLATEQAMDILGFLPDEKYGCFKL 406
Cdd:cd14894 329 MVAGvnafpfmrllAKELHlDGIDCSAltylGRSDHKLA--GFVSKEDTwkKDVERWQQVIDGLDELNVSPDEQKTIFKV 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 407 TGAIMHFGNMKFKQKPREEQL--EADGTENA-DKAAFLMGINSSE-LVKDLIHPRIKVGNEYVTRGQTIE--QVTCAVGA 480
Cdd:cd14894 407 LSAVLWLGNIELDYREVSGKLvmSSTGALNApQKVVELLELGSVEkLERMLMTKSVSLQSTSETFEVTLEkgQVNHVRDT 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 481 LSKSMYERMFKWLVARINRA--------------LDAKLSRQ---FFTGILDITGFEILEYNSLEQLCINFTNEKLqqfF 543
Cdd:cd14894 487 LARLLYQLAFNYVVFVMNEAtkmsalstdgnkhqMDSNASAPeavSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL---Y 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 544 NRHMFVLEQEEYKKESIewvsigFGLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTF-----KTKLFDNHFGKSVHL 617
Cdd:cd14894 564 AREEQVIAVAYSSRPHL------TARDSEKDVLFIyEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIYDRNSS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 618 QKPKPDKKKFEAH-----------FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYM------S 680
Cdd:cd14894 638 RLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSqlgwspN 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 681 TDSAIPFGEKKRKKGTsfQTAASLHKENLNKLMTNLKSTAPHFVRCINPNVNKMPGILDPYLVLQQLRCNGVLEGIRICR 760
Cdd:cd14894 718 TNRSMLGSAESRLSGT--KSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
901-1768 |
9.83e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 116.69 E-value: 9.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 901 EEIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSERV 980
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 981 EEEEEINSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKvVQEAHQQT 1060
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA-SLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1061 LddlhmeEEKLSSLSKANLKLEQQVVGLEGALEQERKARIncERELHKLEGDLKLNQESMENLESSQRHLAEELRKKELE 1140
Cdd:TIGR02168 405 L------EARLERLEDRRERLQQEIEELLKKLEEAELKEL--QAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1141 NSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAerttrakmEKERADLTQDLADLNE-------RLEEVGGASLA 1213
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN--------QSGLSGILGVLSELISvdegyeaAIEAALGGRLQ 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1214 QLEITKKQETK--FQKLRRDMEEATLHFEATSASLKKRHADSLAELEGQvENLQQVKQKLEKDRSDLQLEVDDLLTRIeq 1291
Cdd:TIGR02168 549 AVVVENLNAAKkaIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI-EGFLGVAKDLVKFDPKLRKALSYLLGGV-- 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1292 mtrakanaeklctLYEERLNEANAKLDKVTQLANdLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRG 1371
Cdd:TIGR02168 626 -------------LVVDDLDNALELAKKLRPGYR-IVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1372 QLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEmvqwrmkyENNVIQKTEDLEDAKKELAIRL 1451
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE--------VEQLEERIAQLSKELTELEAEI 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1452 QETAEAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIqal 1531
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL--- 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1532 stellklkhaykesivgqETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALERNESK 1611
Cdd:TIGR02168 841 ------------------EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1612 IlrfqLELLKAKAELERKLSEKDEELENFRRKQQctidsmqssldsEAKSRIEatRLKKKMEEDLnEMELQLscANRQVS 1691
Cdd:TIGR02168 903 L----RELESKRSELRRELEELREKLAQLELRLE------------GLEVRID--NLQERLSEEY-SLTLEE--AEALEN 961
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1692 EATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDL----RSLQEQTERGRRLSEEELLEATERI 1767
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLteakETLEEAIEEIDREARERFKDTFDQV 1041
|
.
gi 1411134203 1768 N 1768
Cdd:TIGR02168 1042 N 1042
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1135-1904 |
7.51e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 113.61 E-value: 7.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1135 RKKELENsQMNSKVENekglVAQLQKMVKELQTQIKDLKEKLE-AERTTRAKMEKERADL---TQDLADLNERLEEVgga 1210
Cdd:TIGR02168 173 RRKETER-KLERTREN----LDRLEDILNELERQLKSLERQAEkAERYKELKAELRELELallVLRLEELREELEEL--- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1211 slaqLEITKKQETKFQKLRRDMEEATLHFEATSASLKKRHaDSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIE 1290
Cdd:TIGR02168 245 ----QEELKEAEEELEELTAELQELEEKLEELRLEVSELE-EEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1291 QMTRAKANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELR 1370
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1371 GQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQevKAELHRTLSKVNAEMVQWRMKYENnVIQKTEDLEDAKKELAIR 1450
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELER-LEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1451 LQETAEAMGVANARNASLERARHRLQ------------------------------------LE--LGDALSDLGKVRSA 1492
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEgfsegvkallknqsglsgilgvlselisvdegyeaaIEaaLGGRLQAVVVENLN 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1493 AARLD---QKQLQSGKA----LADWK-QKHEESQTLLDASRKEIQALSTELLKLKHAYKESIVG-----------QETLR 1553
Cdd:TIGR02168 557 AAKKAiafLKQNELGRVtflpLDSIKgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvvddlDNALE 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1554 RENKNLQEEI------------------SNLTNQVREGTKN-LTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKILr 1614
Cdd:TIGR02168 637 LAKKLRPGYRivtldgdlvrpggvitggSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELE- 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1615 fqlELLKAKAELERKLSEKDEELENFRRKQQctidSMQSSLDSEAKSRIEATRLKKKMEEDLNEMELQLSCANRQVSEAT 1694
Cdd:TIGR02168 716 ---QLRKELEELSRQISALRKDLARLEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1695 KSLGQLQIQ-------IKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERI 1767
Cdd:TIGR02168 789 AQIEQLKEElkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1768 NLFYTQNTSLLSQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKaateaanLSEELKKKQDTIAHLEKTRENMEQTITDL 1847
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE-------LRRELEELREKLAQLELRLEGLEVRIDNL 941
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 1411134203 1848 QKRLAEAEQTALMGSRKQIQKLESrvrelegelegeirRSAEAQRGARRLERCIKEL 1904
Cdd:TIGR02168 942 QERLSEEYSLTLEEAEALENKIED--------------DEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
915-1768 |
3.31e-21 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 101.68 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 915 KALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEwliKSKIQLEARVKELSERVEEEEEINSELTARG 994
Cdd:TIGR02169 209 KAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELE---KLTEEISELEKRLEEIEQLLEELNKKIKDLG 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 995 rklEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLnraakvvQEAHQQTLDDLHMEEEKLSSL 1074
Cdd:TIGR02169 286 ---EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL-------LAEIEELEREIEEERKRRDKL 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1075 SKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMENLESSQRHLAEELRKKELENSQMNSKVENEKGL 1154
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1155 VAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEvggaslAQLEITKKQETkfqklRRDMEE 1234
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK------LQRELAEAEAQ-----ARASEE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1235 ATLHFEATSASLKkrhaDSLAELEGQVENLQQVKQK----LE------------KDRSDLQLEVDDL------------L 1286
Cdd:TIGR02169 505 RVRGGRAVEEVLK----ASIQGVHGTVAQLGSVGERyataIEvaagnrlnnvvvEDDAVAKEAIELLkrrkagratflpL 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1287 TRIEQMTRAK-ANAEKLCTLYEERLNEANAKLDKV-------TQLANDLAAQKT-----ELWSESGEFLrrleEKEALI- 1352
Cdd:TIGR02169 581 NKMRDERRDLsILSEDGVIGFAVDLVEFDPKYEPAfkyvfgdTLVVEDIEAARRlmgkyRMVTLEGELF----EKSGAMt 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1353 ---NQLSREKSNFTRQIEELRgQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKvNAEMVQwrmKY 1429
Cdd:TIGR02169 657 ggsRAPRGGILFSRSEPAELQ-RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK-EIEQLE---QE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1430 ENNVIQKTEDLEDAKKELAIRLQETAEAMGVANARNASLERARHRLQLELGDalsdlgkvrsaaarLDQKQLQSGkalad 1509
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND--------------LEARLSHSR----- 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1510 WKQKHEESQTLlDASRKEIQALSTELlklkhaykESIVGQETLRRENknLQEEISNLTNQVREGTKNLTEMEKVKKLIEQ 1589
Cdd:TIGR02169 793 IPEIQAELSKL-EEEVSRIEARLREI--------EQKLNRLTLEKEY--LEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1590 EKTEVQVTLEETEGALErneskilrfqlELLKAKAELERKLSEKDEELENFRRKQQctidsmQSSLDSEAKSRIEATRLK 1669
Cdd:TIGR02169 862 KKEELEEELEELEAALR-----------DLESRLGDLKKERDELEAQLRELERKIE------ELEAQIEKKRKRLSELKA 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1670 KK--MEEDLNEMElQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDL----R 1743
Cdd:TIGR02169 925 KLeaLEEELSEIE-DPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLeeerK 1003
|
890 900
....*....|....*....|....*
gi 1411134203 1744 SLQEQTERGRRLSEEELLEATERIN 1768
Cdd:TIGR02169 1004 AILERIEEYEKKKREVFMEAFEAIN 1028
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
901-1797 |
3.42e-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: 98.22 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 901 EEIAGLKEECAQLQKALEKSEFQREELKAKQvSLTQEKNDLILQLQAEQETLanveEQCEWLIKSKIQLEARVKELSERv 980
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLD-LIIDEKRQQLERLRREREKA----ERYQALLKEKREYEGYELLKEKE- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 981 eeeeeinsELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDisklnraakvVQEAHQQT 1060
Cdd:TIGR02169 234 --------ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE----------EQLRVKEK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1061 LDDLHMEEEklsslskanlkleqqvvglegaleqerkarincerelhKLEGDLKLNQESMENLESSQRHLAEELRKKELE 1140
Cdd:TIGR02169 296 IGELEAEIA--------------------------------------SLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1141 NSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVggaslaQLEITKK 1220
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL------KRELDRL 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1221 QETKFQKL--RRDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSdlqlEVDDLLTRIEQmtrakan 1298
Cdd:TIGR02169 412 QEELQRLSeeLADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ----ELYDLKEEYDR------- 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1299 aeklctlYEERLNEANAKLDKvtqlandLAAQKTELWSESGEFLRRLEEKEA-------LINQLSREKSNFTRQIEELRG 1371
Cdd:TIGR02169 481 -------VEKELSKLQRELAE-------AEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGSVGERYATAIEVAAG 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1372 Q------LEKETKSQSALAHALQ-KAQRDCDL-LREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENN---VIQKT--- 1437
Cdd:TIGR02169 547 NrlnnvvVEDDAVAKEAIELLKRrKAGRATFLpLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAfkyVFGDTlvv 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1438 EDLEDAKK--------ELAIRLQETAEAM-----------GVANARNASLERARHRLQlELGDALSDL-GKVRSAAARLD 1497
Cdd:TIGR02169 627 EDIEAARRlmgkyrmvTLEGELFEKSGAMtggsraprggiLFSRSEPAELQRLRERLE-GLKRELSSLqSELRRIENRLD 705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1498 QKQlqsgKALADWKQKHEESQTLLDASRKEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLT---NQVREGT 1574
Cdd:TIGR02169 706 ELS----QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEedlHKLEEAL 781
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1575 KNLTEMEKVKKL--IEQEKTEVQVTLEETEGALERNESKILRFQLEllkakaelERKLSEKDEELENFRRKQQCTIDSMQ 1652
Cdd:TIGR02169 782 NDLEARLSHSRIpeIQAELSKLEEEVSRIEARLREIEQKLNRLTLE--------KEYLEKEIQELQEQRIDLKEQIKSIE 853
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1653 SSLDSEAKSRIEATRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRN 1732
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1733 SLLQ----------SELEDLRSLQEQTERgrrlsEEELLEATERINLFYTQN--------TSLLSQKKKLEADVAQMQKE 1794
Cdd:TIGR02169 934 SEIEdpkgedeeipEEELSLEDVQAELQR-----VEEEIRALEPVNMLAIQEyeevlkrlDELKEKRAKLEEERKAILER 1008
|
...
gi 1411134203 1795 AEE 1797
Cdd:TIGR02169 1009 IEE 1011
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
906-1489 |
6.84e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.85 E-value: 6.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 906 LKEECAQLQKALEksefQREELKAKQVSLT-QEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSERVEeee 984
Cdd:COG1196 205 LERQAEKAERYRE----LKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE--- 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 985 einsELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDL 1064
Cdd:COG1196 278 ----ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1065 HMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMENLESSQRHLAEELRKKELENSQM 1144
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1145 NSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNER---LEEVGGASLAQLEITKKQ 1221
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARlllLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1222 ETKFQKLRRDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDL-LTRIEQMTRAKANAE 1300
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLpLDKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1301 KLCTLYEERLNEANAKLDKVTQLANDLAAQKTELWSESGEF-LRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKS 1379
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAaLRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1380 QSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQKTEDLEDAKKELAIRLQETAEAMG 1459
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
570 580 590
....*....|....*....|....*....|
gi 1411134203 1460 VANARNASLERARHRLQlELGDALSDLGKV 1489
Cdd:COG1196 754 EELPEPPDLEELERELE-RLEREIEALGPV 782
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1227-1874 |
1.33e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.08 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1227 KLRRDMEEATLHFEATSASLKkRHADSLAELEGQVENLQ-QVKQ-------KLEKDRSDLQL---EVDDLLTRIEQMTRA 1295
Cdd:COG1196 169 KYKERKEEAERKLEATEENLE-RLEDILGELERQLEPLErQAEKaeryrelKEELKELEAELlllKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1296 KANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEK 1375
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1376 ETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWrmkyennviqktedlEDAKKELAIRLQETA 1455
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---------------EEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1456 EAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALSTEL 1535
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1536 LKLKHAYKEsIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKILRF 1615
Cdd:COG1196 473 ALLEAALAE-LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1616 QLELLKAKAELERKLSEKDEELENFrrkqqctidsmqssldsEAKSRIEATRLKKKMEEDLNEMELQLSCANRQVSEAtk 1695
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATF-----------------LPLDKIRARAALAAALARGAIGAAVDLVASDLREAD-- 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1696 slGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQsELEDLRSLQEQTERGRRLSEEELLEATERInlfytqnt 1775
Cdd:COG1196 613 --ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL-EGEGGSAGGSLTGGSRRELLAALLEAEAEL-------- 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1776 sllSQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAE 1855
Cdd:COG1196 682 ---EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
650
....*....|....*....
gi 1411134203 1856 QTALMGSRKQIQKLESRVR 1874
Cdd:COG1196 759 PPDLEELERELERLEREIE 777
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
900-1643 |
1.49e-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: 92.82 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 900 GEEIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSER 979
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 980 VEEEEEINSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQ 1059
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1060 TLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQerkarinCERELHKLegdlklnQESMENLESSQRHLAEELRKKEL 1139
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR-------VEKELSKL-------QRELAEAEAQARASEERVRGGRA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1140 ENSQMNSKVENEKGLVAQLQKMVKELQTQI-------------------KDLKEKLEAERTTRA------KMEKERADLT 1194
Cdd:TIGR02169 512 VEEVLKASIQGVHGTVAQLGSVGERYATAIevaagnrlnnvvveddavaKEAIELLKRRKAGRAtflplnKMRDERRDLS 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1195 Q-----------DLADLNERLEEV-----GGASLAQ-LEITKKQETKFQ--KLRRDMEEATLHFEATSASLKKRHADSLA 1255
Cdd:TIGR02169 592 IlsedgvigfavDLVEFDPKYEPAfkyvfGDTLVVEdIEAARRLMGKYRmvTLEGELFEKSGAMTGGSRAPRGGILFSRS 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1256 ELEgQVENLQQVKQKLEKDRSDLQLEvddlLTRIEQmtrakanaeklctlyeeRLNEANAKLDKVTQLANDLAAQKTELW 1335
Cdd:TIGR02169 672 EPA-ELQRLRERLEGLKRELSSLQSE----LRRIEN-----------------RLDELSQELSDASRKIGEIEKEIEQLE 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1336 SESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSALAHALQKAQRdcDLLREQYEEEQEVKAELHRTL 1415
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEV 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1416 SKVNAEMVQWRMKyENNVIQKTEDLEDAKKELAIRLQETAEamgvanaRNASLERARHRLQLELGDALSDLGKVRSAAAR 1495
Cdd:TIGR02169 808 SRIEARLREIEQK-LNRLTLEKEYLEKEIQELQEQRIDLKE-------QIKSIEKEIENLNGKKEELEEELEELEAALRD 879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1496 LDQKqlqsgkaLADWKQKHEESQTLLDASRKEIQALSTELLKLKHAYKESIVGQETLRRENKnlqeEISNLTNQVREGTK 1575
Cdd:TIGR02169 880 LESR-------LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPE 948
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411134203 1576 NLTEMEKVKKLIeQEKTEVQVTLEETE-GALERNESKILRF-QLELLKAKAELERK-LSEKDEELENFRRK 1643
Cdd:TIGR02169 949 EELSLEDVQAEL-QRVEEEIRALEPVNmLAIQEYEEVLKRLdELKEKRAKLEEERKaILERIEEYEKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1164-1801 |
1.61e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.69 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1164 ELQTQIKDLKEklEAERTTRAKMEKERADLTQdladlnerleevggASLAQLEItKKQETKFQKLRRDMEEATLHFEATS 1243
Cdd:COG1196 197 ELERQLEPLER--QAEKAERYRELKEELKELE--------------AELLLLKL-RELEAELEELEAELEELEAELEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1244 ASLkkrhadslAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRAKAnaeklctLYEERLNEANAKLDKVTQL 1323
Cdd:COG1196 260 AEL--------AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA-------RLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1324 ANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEE 1403
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1404 EQEVKAELHRTLSKVNAEMVQWRMKyENNVIQKTEDLEDAKKELAIRLQETAEAMGVANARNASLERARHRLQLELGDAL 1483
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEA-LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1484 SDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQ-----------------------TLLDASRKEIQALSTELLKLKH 1540
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGlrglagavavligveaayeaaleAALAAALQNIVVEDDEVAAAAI 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1541 AY-KESIVGQETLRRENK-NLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKILRFQLE 1618
Cdd:COG1196 564 EYlKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1619 LLKAKAELERKLSEKDEELENFRRKQQctidsmQSSLDSEAKSRIEATRLKKKMEEDLNEMELQLSCANRQVSEATKSLG 1698
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRREL------LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1699 QLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQ-SELEDLRSLQEQTERGRR----------LSEEELLEATERI 1767
Cdd:COG1196 718 EEELEEEALEEQLEAEREELLEELLEEEELLEEEALEElPEPPDLEELERELERLEReiealgpvnlLAIEEYEELEERY 797
|
650 660 670
....*....|....*....|....*....|....
gi 1411134203 1768 NLFYTQNTSLLSQKKKLEADVAQMQKEAEEVVQE 1801
Cdd:COG1196 798 DFLSEQREDLEEARETLEEAIEEIDRETRERFLE 831
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1043-1980 |
2.85e-18 |
|
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: 92.03 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1043 ISKLNRAAKVVQEaHQQTLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMEN 1122
Cdd:TIGR00606 185 IKALETLRQVRQT-QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1123 LESSQRHLaEELRKKELENSQMNSKVEnekglvaqlQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNE 1202
Cdd:TIGR00606 264 IMKLDNEI-KALKSRKKQMEKDNSELE---------LKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1203 RleevggaslAQLEITKKQETKFQKLRRDMEEATLHFEATSASLKKRHADSLAELEGqvenlqqvkqkLEKDrSDLQLEV 1282
Cdd:TIGR00606 334 E---------RRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDG-----------FERG-PFSERQI 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1283 DDLLT-RIEQMTRAKANAEKLCTLYEERLNEANAKLDKVTQLANDLAaQKTELWSEsgeflrRLEEKEALINQLSREKSN 1361
Cdd:TIGR00606 393 KNFHTlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLG-RTIELKKE------ILEKKQEELKFVIKELQQ 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1362 FTRQIEELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEeeQEVKAELHRTLSKVNAEMVQwrMKYENNVIQKTEDLE 1441
Cdd:TIGR00606 466 LEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSL--QNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLT 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1442 DAKKE-----LAIRLQETAEAMGVAN--ARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKH 1514
Cdd:TIGR00606 542 KDKMDkdeqiRKIKSRHSDELTSLLGyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1515 -------------EESQTLLDASRKEIQALSTELLKL--KHAYKESIVGQETLRREN------------KNLQEEISNLT 1567
Cdd:TIGR00606 622 ssyedklfdvcgsQDEESDLERLKEEIEKSSKQRAMLagATAVYSQFITQLTDENQSccpvcqrvfqteAELQEFISDLQ 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1568 NQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKIlrfqlellKAKAELERKLSEKDEELENFRRKQQCT 1647
Cdd:TIGR00606 702 SKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEI--------PELRNKLQKVNRDIQRLKNDIEEQETL 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1648 IDSMQSSLDSEAKSRIEATRLKK-KMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVA 1726
Cdd:TIGR00606 774 LGTIMPEEESAKVCLTDVTIMERfQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQ 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1727 VAERRNSLLQSELEDLRS--LQEQTERGRRLS-EEELLEATERINLFYTQNTSLLSQKKKLEADVAQMQKEAEEVVQECQ 1803
Cdd:TIGR00606 854 DQQEQIQHLKSKTNELKSekLQIGTNLQRRQQfEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKE 933
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1804 NAEEKAKKAAteaanlsEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQTALMGSRKQIQKLESRVRELEGELEGE 1883
Cdd:TIGR00606 934 TSNKKAQDKV-------NDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQD 1006
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1884 IRRSAEAQR------GARRLERCIKELtyqaEEDKKNLSRMQTQMDKLQLKVHNYKQQVEVAEAQANQYLSKYKKQQHEL 1957
Cdd:TIGR00606 1007 IDTQKIQERwlqdnlTLRKRENELKEV----EEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEK 1082
|
970 980
....*....|....*....|...
gi 1411134203 1958 NEVKERAEVAESQVNKLKIKARE 1980
Cdd:TIGR00606 1083 EIKHFKKELREPQFRDAEEKYRE 1105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
888-1588 |
5.10e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 91.27 E-value: 5.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 888 FKIKPLVKSSERGEE-IAGLKEECAQLQKALEKSEFQREELKAKQVSltqekndlilqLQAEQETLANVEEqcewliksk 966
Cdd:TIGR02168 309 ERLANLERQLEELEAqLEELESKLDELAEELAELEEKLEELKEELES-----------LEAELEELEAELE--------- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 967 iQLEARVKelserveeeeeinsELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKL 1046
Cdd:TIGR02168 369 -ELESRLE--------------ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1047 NRaakvvqEAHQQTLDDLHMEEEKlssLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMENLESS 1126
Cdd:TIGR02168 434 EL------KELQAELEELEEELEE---LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1127 QRHLAEELRKKELENSQMNS-----KVEN------EKGLVAQLQKMVKELQTQIKD----LKE----------------- 1174
Cdd:TIGR02168 505 SEGVKALLKNQSGLSGILGVlseliSVDEgyeaaiEAALGGRLQAVVVENLNAAKKaiafLKQnelgrvtflpldsikgt 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1175 KLEAERTTRAKMEKERADLTQDLADLNERLEEVGGASLAQLEITKKQETKFQKLRR----------DMEEATLHFEATSA 1244
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrpgyrivtlDGDLVRPGGVITGG 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1245 SLK------------KRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRA-------KANAEKLCTL 1305
Cdd:TIGR02168 665 SAKtnssilerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQisalrkdLARLEAEVEQ 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1306 YEERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSALAH 1385
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1386 ALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMvqwrmkyennviqktEDLEDAKKELAIRLQETAEAMgvanarn 1465
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI---------------EELEELIEELESELEALLNER------- 882
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1466 ASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEES----QTLLDASRKEIQALSTELLKLKHA 1541
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLevriDNLQERLSEEYSLTLEEAEALENK 962
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1411134203 1542 YKESIvgqETLRRENKNLQEEISNLtnqvreGTKNLTEMEKVKKLIE 1588
Cdd:TIGR02168 963 IEDDE---EEARRRLKRLENKIKEL------GPVNLAAIEEYEELKE 1000
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1187-1974 |
5.29e-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: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1187 EKERAdlTQDLADLNERLEEVG------GASLAQLEITKKQETKFQKLRRDMEEatlhFEATSASLKKRHAD-SLAELEG 1259
Cdd:TIGR02169 171 KKEKA--LEELEEVEENIERLDliidekRQQLERLRREREKAERYQALLKEKRE----YEGYELLKEKEALErQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1260 QVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMtrakanAEKLCTLYEERLNEANAKLDKVTqlandlaAQKTELWSESG 1339
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEEL------NKKIKDLGEEEQLRVKEKIGELE-------AEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1340 EFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVN 1419
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1420 AEMVQwrMKYENNVIQKTED-LEDAKKELAIRLQETAEAMGVANARNASLERARHRLQLELgdalsdlgkvrsaaARLDQ 1498
Cdd:TIGR02169 392 EKLEK--LKREINELKRELDrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI--------------KKQEW 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1499 KQLQSGKALADWKQKHEESQTLLDASRKEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKnlT 1578
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS--V 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1579 EMEKVKKLIEQEKTEVQVTLEETEGALER-----NESKILRFQ---LELLKAKAELERKLSEK------------DEELE 1638
Cdd:TIGR02169 534 GERYATAIEVAAGNRLNNVVVEDDAVAKEaiellKRRKAGRATflpLNKMRDERRDLSILSEDgvigfavdlvefDPKYE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1639 N-FRRKQQCTI--DSMQS-----------SLDSE-----------AKSRIEATRLKKKMEEDLNEMelqlscaNRQVSEA 1693
Cdd:TIGR02169 614 PaFKYVFGDTLvvEDIEAarrlmgkyrmvTLEGElfeksgamtggSRAPRGGILFSRSEPAELQRL-------RERLEGL 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1694 TKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATerinlfytq 1773
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK--------- 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1774 ntsllSQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKaateaanlsEELKKKQDTIAHLEKTRENMEQTITDLQKRLaE 1853
Cdd:TIGR02169 758 -----SELKELEARIEELEEDLHKLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSRIEARLREIEQKL-N 822
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1854 AEQTALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVHNYK 1933
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 1411134203 1934 QQVEVAEAQANqylskykKQQHELNEVKERAEVAESQVNKL 1974
Cdd:TIGR02169 903 RKIEELEAQIE-------KKRKRLSELKAKLEALEEELSEI 936
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1222-1997 |
3.12e-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: 88.59 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1222 ETKFQKLRRDMEEATLHFEATSASLKkrhadslaELEGQVENLQQVKQKLEKDRsDLQLEVDD-----LLTRIEQMTRAK 1296
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIID--------EKRQQLERLRREREKAERYQ-ALLKEKREyegyeLLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1297 ANAEKlctlyeeRLNEANAKLDKVTQLANDLAAqktelwsESGEFLRRLEEKEALINQLSREKSN-FTRQIEELRGQLEK 1375
Cdd:TIGR02169 240 EAIER-------QLASLEEELEKLTEEISELEK-------RLEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1376 ETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENnviqktedLEDAKKELAIRLQETA 1455
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE--------LKEELEDLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1456 EAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALSTEL 1535
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1536 lklkhayKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEEtegaLERNESKILRF 1615
Cdd:TIGR02169 458 -------EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEV----LKASIQGVHGT 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1616 QLELLKAKAELERKLsekdeELENFRRKQQCTIDSmqsslDSEAKSRIEATRLKK----------KMEE----------- 1674
Cdd:TIGR02169 527 VAQLGSVGERYATAI-----EVAAGNRLNNVVVED-----DAVAKEAIELLKRRKagratflplnKMRDerrdlsilsed 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1675 -------DLNEMELQLSCANRQVSEATKSLGQLQIQiKDLQMQLDDSTqLNSDLKEQV------AVAERRNSLLQ-SELE 1740
Cdd:TIGR02169 597 gvigfavDLVEFDPKYEPAFKYVFGDTLVVEDIEAA-RRLMGKYRMVT-LEGELFEKSgamtggSRAPRGGILFSrSEPA 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1741 DLRSLQEQTERGRRLSEEELLEATERINLFYtqntSLLSQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLS 1820
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLD----ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1821 EELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQTALMGSRKQIQKLESRVRELEGELEGEIrRSAEAQRGARRLERC 1900
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARL-REIEQKLNRLTLEKE 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1901 -----IKELTYQAEEDKKNLSRMQTQMDKLQLKVHNYKQQVEVAEAQANQYLSKYKKQQHELNEVKERAEVAESQVNKLK 1975
Cdd:TIGR02169 830 ylekeIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
810 820
....*....|....*....|..
gi 1411134203 1976 IKArefgKKVRQAQTELLVTLQ 1997
Cdd:TIGR02169 910 AQI----EKKRKRLSELKAKLE 927
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1157-1956 |
4.71e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 88.25 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1157 QLQKMVKELQTQIKDLKEKLEAERTTRakmEKERADLTQDLADLNERLEEVGGASLAQLEItKKQETKFQKLRRDMEEAT 1236
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELH---EKQKFYLRQSVIDLQTKLQEMQMERDAMADI-RRRESQSQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1237 LHFEATSASLKKrhaDSLAELEGQVENLQQVKQKLEkdrsDLQLEVDDLLTRIEQMTRAKA-NAEKLCTLYEERLNEANA 1315
Cdd:pfam15921 151 VHELEAAKCLKE---DMLEDSNTQIEQLRKMMLSHE----GVLQEIRSILVDFEEASGKKIyEHDSMSTMHFRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1316 KLdkVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNftrQIEELRGQLEKET-----KSQSALAHAlQKA 1390
Cdd:pfam15921 224 KI--LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQD---RIEQLISEHEVEItglteKASSARSQA-NSI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1391 QRDCDLLREQYEEEQEVK----AELHRTLSKVNAEMVQWRMKYENnviqKTEDLEdakKELAIRLQETAEamgvANARNA 1466
Cdd:pfam15921 298 QSQLEIIQEQARNQNSMYmrqlSDLESTVSQLRSELREAKRMYED----KIEELE---KQLVLANSELTE----ARTERD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1467 SLERARHRLQLELGDALSDLGKvRSAAARLDQKQlqsGKALadWKQKHEESQTlLDASRKEIQALSTELLKLK---HAYK 1543
Cdd:pfam15921 367 QFSQESGNLDDQLQKLLADLHK-REKELSLEKEQ---NKRL--WDRDTGNSIT-IDHLRRELDDRNMEVQRLEallKAMK 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1544 ESIVGQ-----ETLRRENKNLqEEISNLTNQVrEGTKnltemEKVKKLIEqEKTEVQVTLEETE-------GALERNESK 1611
Cdd:pfam15921 440 SECQGQmerqmAAIQGKNESL-EKVSSLTAQL-ESTK-----EMLRKVVE-ELTAKKMTLESSErtvsdltASLQEKERA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1612 ILRFQLELLKAKAELERKLsekdEELENFRRKQQcTIDSMQSSLDSEAKSRIEATRLKKKMEEDLNEMELQLSCANRQVS 1691
Cdd:pfam15921 512 IEATNAEITKLRSRVDLKL----QELQHLKNEGD-HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAG 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1692 EATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLqsELEDLRSLQEQTERgrrlseeelLEATERINlfy 1771
Cdd:pfam15921 587 AMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL--ELEKVKLVNAGSER---------LRAVKDIK--- 652
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1772 TQNTSLLSQKKKLEADVAQMQKEAEEVVQECQNaeeKAKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDLQKrL 1851
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSEDYEVLKRNFRN---KSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMK-V 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1852 AEAEQTALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLErciKELTYQAEEDKK---NLSRMQTQMDKLQLK 1928
Cdd:pfam15921 729 AMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS---QELSTVATEKNKmagELEVLRSQERRLKEK 805
|
810 820
....*....|....*....|....*...
gi 1411134203 1929 VHNYKQQVEVAEAQANQYLSKYKKQQHE 1956
Cdd:pfam15921 806 VANMEVALDKASLQFAECQDIIQRQEQE 833
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
906-1602 |
1.85e-16 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 85.94 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 906 LKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIK-SKIQLEARVKELSERVEEEE 984
Cdd:pfam15921 108 LRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEdSNTQIEQLRKMMLSHEGVLQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 985 EINSELT----ARGRKLEDEcselkkeiDDLETMLVKSEKEkrTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQT 1060
Cdd:pfam15921 188 EIRSILVdfeeASGKKIYEH--------DSMSTMHFRSLGS--AISKILRELDTEISYLKGRIFPVEDQLEALKSESQNK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1061 LDDL-HMEEEKLSSLskanlkLEQQVVGLEGALEQERKARinceRELHKLEGDLKLNQESMENLESS-QRHLAEelrkKE 1138
Cdd:pfam15921 258 IELLlQQHQDRIEQL------ISEHEVEITGLTEKASSAR----SQANSIQSQLEIIQEQARNQNSMyMRQLSD----LE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1139 LENSQMNSKVENEKGLvaqLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDL----ADLNERLEEvggaslaq 1214
Cdd:pfam15921 324 STVSQLRSELREAKRM---YEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLqkllADLHKREKE-------- 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1215 LEITKKQETKF-----------QKLRRDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRS-DLQLEV 1282
Cdd:pfam15921 393 LSLEKEQNKRLwdrdtgnsitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSlTAQLES 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1283 DDLLTR--IEQMTRAKANAEK-------LCTLYEERLNEANAKLDKVTQLAN--DLAAQKTELWSESGEFLRRLE-EKEA 1350
Cdd:pfam15921 473 TKEMLRkvVEELTAKKMTLESsertvsdLTASLQEKERAIEATNAEITKLRSrvDLKLQELQHLKNEGDHLRNVQtECEA 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1351 LINQLSREKsnftRQIEELRGQLEKETK-----SQSALAHALQKAQRDCDLlREQYEEEQEVKA----------ELHRTL 1415
Cdd:pfam15921 553 LKLQMAEKD----KVIEILRQQIENMTQlvgqhGRTAGAMQVEKAQLEKEI-NDRRLELQEFKIlkdkkdakirELEARV 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1416 SKVNAEMVQW------RMKYENNVIQKTEDLEDAKKELAIRLQETAEAMGV--ANARNAS--LERARHRLQLELGDALSD 1485
Cdd:pfam15921 628 SDLELEKVKLvnagseRLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVlkRNFRNKSeeMETTTNKLKMQLKSAQSE 707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1486 LGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALS---TELLKLKHAYKES----------------- 1545
Cdd:pfam15921 708 LEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEeamTNANKEKHFLKEEknklsqelstvateknk 787
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1546 IVGQ-ETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQE--KTEVQVTLEETE 1602
Cdd:pfam15921 788 MAGElEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQEsvRLKLQHTLDVKE 847
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
999-1496 |
2.12e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 85.86 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 999 DECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLnraakvvqeahqqtLDDLHMEEEKLSSLSKAN 1078
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL--------------LAEAGLDDADAEAVEARR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1079 LKLEQQVVGLEGALEQERKArincereLHKLEGDLKLNQESMENLESSqrhlAEELRKK--ELEnsqmnSKVENEKGLVA 1156
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVA-------AQAHNEEAESLREDADDLEER----AEELREEaaELE-----SELEEAREAVE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1157 QLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVggaslaqleitkkqETKFQKLRRDMEEAT 1236
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL--------------EATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1237 LHFEA-----TSASLKKR-HADSLAELEGQVEnlqqvkqKLEKDRSDLQLEVDDLLTRIEQMTRAKANAEKLCTLYE--- 1307
Cdd:PRK02224 447 ALLEAgkcpeCGQPVEGSpHVETIEEDRERVE-------ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErre 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1308 ---ERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEEL---RGQLEKETKSQS 1381
Cdd:PRK02224 520 dleELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELkerIESLERIRTLLA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1382 ALAHALQKAQRdcdlLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVI----QKTEDLEDAKKELAIRLQETAE- 1456
Cdd:PRK02224 600 AIADAEDEIER----LREKREALAELNDERRERLAEKRERKRELEAEFDEARIeearEDKERAEEYLEQVEEKLDELREe 675
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1411134203 1457 ------AMGVANARNASLERARHRLQlELGDALSDLGKVRSAAARL 1496
Cdd:PRK02224 676 rddlqaEIGAVENELEELEELRERRE-ALENRVEALEALYDEAEEL 720
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1021-1852 |
1.31e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.65 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1021 EKRTTEHKVKNLTEEVEFLNEDI-----SKLNRAAKVVQ-EAHQQTLDDLHMEEEKLS----SLSKANLKLEQQVVGLEG 1090
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDIIDEDIdgnheGKAEAKAHVGQdEGLKPSYKDFDFDAKEDNradeATEEAFGKAEEAKKTETG 1109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1091 ALEQERKARincerELHKLEGDLKLNQESMENLESsqRHLAEELRKKELENSQMNSKVEN----EKGLVAQLQKMVKELQ 1166
Cdd:PTZ00121 1110 KAEEARKAE-----EAKKKAEDARKAEEARKAEDA--RKAEEARKAEDAKRVEIARKAEDarkaEEARKAEDAKKAEAAR 1182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1167 --TQIKDLKEKLEAERTTRA----KMEKERADLTQDLADLNERLEEVGGASLAQleiTKKQETKFQKLRRDMEEATLHFE 1240
Cdd:PTZ00121 1183 kaEEVRKAEELRKAEDARKAeaarKAEEERKAEEARKAEDAKKAEAVKKAEEAK---KDAEEAKKAEEERNNEEIRKFEE 1259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1241 ATSASLKKRHADSLAELEGQVENL---QQVKQKLEKDRSDLQLEVDDLLTRIEQMTRA---KANAEKLCTLYEE--RLNE 1312
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELkkaEEKKKADEAKKAEEKKKADEAKKKAEEAKKAdeaKKKAEEAKKKADAakKKAE 1339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1313 ANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSALAHAlQKAQR 1392
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA-AAAKK 1418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1393 DCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQKTEDLEDAKK--ELAIRLQETAEAMGVANARNASLER 1470
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEAKKK 1498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1471 ARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALSTELLKLKHAYKESIVGQE 1550
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1551 TLRREN--------------KNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEgalERNESKILRFQ 1616
Cdd:PTZ00121 1579 ALRKAEeakkaeearieevmKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE---EKKKAEELKKA 1655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1617 LELLKAKAELERKLSEKDEELENFRRKQQCTIDSMQSSLDSEAKSRIEATRLKKKMEEDLNEME----------LQLSCA 1686
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEelkkaeeenkIKAEEA 1735
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1687 NRQVSEATKSLGQLQI----QIKDLQMQLDDSTQLNSDLKEQVAVAERRnslLQSELEDLRSLQEQTERGRRLSEEELLE 1762
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKdeeeKKKIAHLKKEEEKKAEEIRKEKEAVIEEE---LDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1763 ATERINLFYTQNTSLLSQKKKLEADVAQMQK-EAEEVVQECQNAEEKAKKAATEAANLSEELKKKQDTIAHLEKTRENME 1841
Cdd:PTZ00121 1813 GGKEGNLVINDSKEMEDSAIKEVADSKNMQLeEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEK 1892
|
890
....*....|.
gi 1411134203 1842 QTITDLQKRLA 1852
Cdd:PTZ00121 1893 IDKDDIEREIP 1903
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1116-1791 |
1.77e-15 |
|
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: 82.46 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1116 NQESMENLESSQRHLAEELRK----KELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERa 1191
Cdd:pfam05483 72 NSEGLSRLYSKLYKEAEKIKKwkvsIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEN- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1192 DLTQDLADLNERLEEVGGASLAQLEItKKQETK--FQKLRRDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQ 1269
Cdd:pfam05483 151 NATRHLCNLLKETCARSAEKTKKYEY-EREETRqvYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1270 KLEKDRSDLQLEVDDLLTrieQMTRAKANAEKLCTLYEErlneanaKLDKVTQLandlaAQKTELWSESgeflrrleeke 1349
Cdd:pfam05483 230 EYKKEINDKEKQVSLLLI---QITEKENKMKDLTFLLEE-------SRDKANQL-----EEKTKLQDEN----------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1350 alINQLSREKSNFTRQIEELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEM------V 1423
Cdd:pfam05483 284 --LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFeattcsL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1424 QWRMKYENNVIQKTED-LEDAKKELAIRLQETAEAMGVANARNASLErarhrlqlelgdalsDLGKVRSAAARLDQKQLQ 1502
Cdd:pfam05483 362 EELLRTEQQRLEKNEDqLKIITMELQKKSSELEEMTKFKNNKEVELE---------------ELKKILAEDEKLLDEKKQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1503 SGKALADWKQKHEESQTLLDASRKEIQALSTELLKLKhaykesiVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEK 1582
Cdd:pfam05483 427 FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIK-------TSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1583 VKKLIEQEKTEVQVTLEETEGALERNESKILRfqleLLKAKAELERKLSEKDEELENFRRKQQCTIDSMQSSLDSEAKSR 1662
Cdd:pfam05483 500 ENKELTQEASDMTLELKKHQEDIINCKKQEER----MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENA 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1663 IEATRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQ-LDDSTQLNSdLKEQVAVAERRNSLLQSELED 1741
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKgSAENKQLNA-YEIKVNKLELELASAKQKFEE 654
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1411134203 1742 LRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQ-KKKLEADVAQM 1791
Cdd:pfam05483 655 IIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEiDKRCQHKIAEM 705
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
900-1804 |
2.21e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 82.79 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 900 GEEIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKnDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSER 979
Cdd:TIGR00606 199 GQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 980 VEEEEEINSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHK-VKNLTEEVEFLNEDISKLnraakVVQEAHQ 1058
Cdd:TIGR00606 278 KKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQReLEKLNKERRLLNQEKTEL-----LVEQGRL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1059 QTLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMENLESSQRHLAEELRKKE 1138
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1139 LENSQMNSKVENEKglvAQLQKMVKELQTQIKDLKeklEAERTTRAKMEKERAdLTQDLADLNERLEEvggaslAQLEIT 1218
Cdd:TIGR00606 433 DEKKGLGRTIELKK---EILEKKQEELKFVIKELQ---QLEGSSDRILELDQE-LRKAERELSKAEKN------SLTETL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1219 KKQETKFQKLRRDMEEaTLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLL-----TRIEQMT 1293
Cdd:TIGR00606 500 KKEVKSLQNEKADLDR-KLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLgyfpnKKQLEDW 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1294 RAKANAEKLCTlyEERLNEANAKLDKVTQLANDLAAQKTELWSEsgefLRRLEEKeaLINQLSREksNFTRQIEELRGQL 1373
Cdd:TIGR00606 579 LHSKSKEINQT--RDRLAKLNKELASLEQNKNHINNELESKEEQ----LSSYEDK--LFDVCGSQ--DEESDLERLKEEI 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1374 EKETKSQSALAHALQKAqrdcDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQKTEDLEDAKKELAIRLQE 1453
Cdd:TIGR00606 649 EKSSKQRAMLAGATAVY----SQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKR 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1454 TAEAMGVANARNASLErarhRLQLELGDALSDLGKVRSAAARLdQKQLQSGKALADWKQKHEESQTLLDASRKEIQALST 1533
Cdd:TIGR00606 725 RDEMLGLAPGRQSIID----LKEKEIPELRNKLQKVNRDIQRL-KNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQM 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1534 ELLKLKHAYKESIVGQET---------LRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGA 1604
Cdd:TIGR00606 800 ELKDVERKIAQQAAKLQGsdldrtvqqVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTN 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1605 LERNEsKILRFQLELLKAKAELERKLSEKDEE---LENFRRK-QQCTIDSMQSSLDSEAKSRIEATRLKKKM-------- 1672
Cdd:TIGR00606 880 LQRRQ-QFEEQLVELSTEVQSLIREIKDAKEQdspLETFLEKdQQEKEELISSKETSNKKAQDKVNDIKEKVknihgymk 958
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1673 ----------EEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDL 1742
Cdd:TIGR00606 959 dienkiqdgkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELK 1038
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411134203 1743 RSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVAQMQKEAEEvvQECQN 1804
Cdd:TIGR00606 1039 QHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE--PQFRD 1098
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1364-1980 |
3.83e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1364 RQIEELRGQ-----------LEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMvqwrmkyenn 1432
Cdd:COG1196 200 RQLEPLERQaekaeryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL---------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1433 viqktEDLEDAKKELAIRLQETAEAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQ 1512
Cdd:COG1196 270 -----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1513 KHEESQTLLDASRKEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKT 1592
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1593 EVQVTLEETEGALERNESKILRFQLELLKAKAELERKLSEKDEELENFRRKQQCTIDSMQSSLDSEAKsrieatrlkkkm 1672
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR------------ 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1673 EEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQlnsdlkEQVAVAERRNSLLQSELEDLRSLQEQTE-- 1750
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY------EAALEAALAAALQNIVVEDDEVAAAAIEyl 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1751 RGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKKKQDT- 1829
Cdd:COG1196 567 KAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRl 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1830 -IAHLEKTRENMEQTITDLQKR----LAEAEQTALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKEL 1904
Cdd:COG1196 647 rEVTLEGEGGSAGGSLTGGSRRellaALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1905 TYQAEEDKKNLSRMQTQMDKLQLKVHNYKQQVEVAEAQANQYLSKYKKQ-----------QHELNEVKERAEVAESQVNK 1973
Cdd:COG1196 727 EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREiealgpvnllaIEEYEELEERYDFLSEQRED 806
|
....*..
gi 1411134203 1974 LKiKARE 1980
Cdd:COG1196 807 LE-EARE 812
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
895-1796 |
7.42e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 80.79 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 895 KSSERGEEIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVK 974
Cdd:pfam02463 188 LIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 975 ELSERVE-EEEEINSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVV 1053
Cdd:pfam02463 268 AQVLKENkEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1054 QEAHQQTLDdlhmEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMENLESSQRHLAEE 1133
Cdd:pfam02463 348 EIKREAEEE----EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1134 LRKKELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVGGASLA 1213
Cdd:pfam02463 424 EKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKES 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1214 QLEITKKQETKFQK---LRRDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIE 1290
Cdd:pfam02463 504 KARSGLKVLLALIKdgvGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLL 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1291 QMTRAKANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELR 1370
Cdd:pfam02463 584 IPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSE 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1371 --GQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLskvnaemvQWRMKYEnnviQKTEDLEDAKKELA 1448
Cdd:pfam02463 664 vkASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE--------ELKKLKL----EAEELLADRVQEAQ 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1449 IRLQETAEAMgVANARNASLERARHRLQLELGDAlsdlgkvrsaaarlDQKQLQSGKALADWKQKHEESQTLLDASRKEI 1528
Cdd:pfam02463 732 DKINEELKLL-KQKIDEEEEEEEKSRLKKEEKEE--------------EKSELSLKEKELAEEREKTEKLKVEEEKEEKL 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1529 QALSTELLKLKHAYKESIvgqETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALERN 1608
Cdd:pfam02463 797 KAQEEELRALEEELKEEA---ELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELL 873
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1609 ESKILRFQLELLKAKAELERKLSEKDEELENFRRkqqctIDSMQSSLDSEAKSRIEATRLKKKMEEDLNEMELqLSCANR 1688
Cdd:pfam02463 874 LKEEELEEQKLKDELESKEEKEKEEKKELEEESQ-----KLNLLEEKENEIEERIKEEAEILLKYEEEPEELL-LEEADE 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1689 QVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNsllqSELEDLRSLQEQTERGRRLSEEELLEATERIN 1768
Cdd:pfam02463 948 KEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYN----KDELEKERLEEEKKKLIRAIIEETCQRLKEFL 1023
|
890 900
....*....|....*....|....*...
gi 1411134203 1769 LFYTQNTSLLSQKKKLEADVAQMQKEAE 1796
Cdd:pfam02463 1024 ELFVSINKGWNKVFFYLELGGSAELRLE 1051
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1260-1991 |
1.54e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.19 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1260 QVENLQQVKQKLEKDRSDLQLEVDDLLTR-IEQMTRAKANAEKlcTLYEERLNEANAKLDKVTQLANDLAAQKTELWSES 1338
Cdd:PTZ00121 1022 QNFNIEKIEELTEYGNNDDVLKEKDIIDEdIDGNHEGKAEAKA--HVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGK 1099
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1339 GEFLRRLEE---KEALINQLSREKSNFTRQIEELRG-----QLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAE 1410
Cdd:PTZ00121 1100 AEEAKKTETgkaEEARKAEEAKKKAEDARKAEEARKaedarKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAE 1179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1411 LHRTLSKV----------NAEMVQWRMKYEN-NVIQKTEDLEDAKKELAIRLQETAEAmGVANARNASLERARHRLQLEL 1479
Cdd:PTZ00121 1180 AARKAEEVrkaeelrkaeDARKAEAARKAEEeRKAEEARKAEDAKKAEAVKKAEEAKK-DAEEAKKAEEERNNEEIRKFE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1480 GDALSDLGKVRSA-----AARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALSTELLKLKHAYKESIVGQETLRR 1554
Cdd:PTZ00121 1259 EARMAHFARRQAAikaeeARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKA 1338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1555 ENKNLQEEISNltNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEG-ALERNESKILRFQLELLKAKAELERKLSEK 1633
Cdd:PTZ00121 1339 EEAKKAAEAAK--AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1634 DEELENFRRKQQCTIDSMQSSLDSEAKSRieATRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDD 1713
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKK--ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1714 STQLNSDLKEQVAVAERRNSLLQSE----LEDLRSLQE--QTERGRRLSE----EELLEATErinLFYTQNTSLLSQKKK 1783
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEeakkADEAKKAEEakKADEAKKAEEkkkaDELKKAEE---LKKAEEKKKAEEAKK 1571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1784 LEADVAQMQKEAEEVVQ-ECQNAEEKAKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQTALMGS 1862
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1863 RKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVHNYKQQVEVAEAQ 1942
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1411134203 1943 ANQylskYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVRQAQTE 1991
Cdd:PTZ00121 1732 AEE----AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1141-1962 |
9.18e-14 |
|
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: 77.32 E-value: 9.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1141 NSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKeKLEAERTTRAKM-------------EKERADLTQDLadlnERLEEV 1207
Cdd:TIGR00618 104 EQPEQLYLEQKKGRGRILAAKKSETEEVIHDLL-KLDYKTFTRVVLlpqgefaqflkakSKEKKELLMNL----FPLDQY 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1208 GGASLAQLEITKKQETKFQKLRRDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEvDDLLT 1287
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ-EEQLK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1288 RIEQMTRAKANAEKLCTLyEERLNEANAKLDKVTQLANDLAAQK--TELWSESGEFLRRLEEKEALINQLSREKSNFTRQ 1365
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQ-EAVLEETQERINRARKAAPLAAHIKavTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1366 IEELRGQLEketksqsalahALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNaEMVQWRMkyennviQKTEDLEDAKK 1445
Cdd:TIGR00618 337 QSSIEEQRR-----------LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQ-------QKTTLTQKLQS 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1446 ELAIRLQETAEAmgvanARNASLERARHRLQlelGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASR 1525
Cdd:TIGR00618 398 LCKELDILQREQ-----ATIDTRTSAFRDLQ---GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1526 KEIQALST-ELLKLKHAYKESIVGQETLR-RENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEG 1603
Cdd:TIGR00618 470 EREQQLQTkEQIHLQETRKKAVVLARLLElQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1604 AL--ERNESKILRFQLELLK-AKAELERKLSEKDEELENFRRKQQCTIDSMQSSLDSEAKSRIEATRLKKKMEEDLNEME 1680
Cdd:TIGR00618 550 QLtsERKQRASLKEQMQEIQqSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1681 LQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQ-VAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEE 1759
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKElLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1760 LLEATERINLFYTQNTSLLSQKKKLEAD---VAQMQKEAEEVVQE-CQNAEEKAKKAATEAANLSEELKKKQDTIAHLEK 1835
Cdd:TIGR00618 710 ETHIEEYDREFNEIENASSSLGSDLAARedaLNQSLKELMHQARTvLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQF 789
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1836 TRENMEQTITDLQKRLAEAEQTALMGSrkqiqklesrvrelegelegeirrsaeaqrgarrlerciKELTYQAEEDKKNL 1915
Cdd:TIGR00618 790 FNRLREEDTHLLKTLEAEIGQEIPSDE---------------------------------------DILNLQCETLVQEE 830
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 1411134203 1916 SRMQTQMDKLQLKVHNYKQQVEVAEAQANQYLSKYKKQQHELNEVKE 1962
Cdd:TIGR00618 831 EQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1149-1874 |
2.12e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.16 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1149 ENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVGGASLAQLEITKKQETKFQKL 1228
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1229 RRDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSDLQlEVDDLLTRIEQMTRAKANAEKLCTLYEE 1308
Cdd:TIGR00618 267 ARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQ-SKMRSRAKLLMKRAAHVKQQSSIEEQRR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1309 RLNEANAKLDKVTQLANDLAAQKTELWSESGEF--LRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSALAHA 1386
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTqhIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1387 LQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKY------ENNVIQKTEDLEDAKKELAIRLQETAEAMGV 1460
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLkereqqLQTKEQIHLQETRKKAVVLARLLELQEEPCP 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1461 ANARNASLERARHrlqlelgdALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALSTELLKLKH 1540
Cdd:TIGR00618 506 LCGSCIHPNPARQ--------DIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQ 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1541 AYKESIVGQETLRRENKNLQEEISNLTnQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKILRFQLELL 1620
Cdd:TIGR00618 578 CDNRSKEDIPNLQNITVRLQDLTEKLS-EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLT 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1621 KAKAELERKLSEKDEELENFRRkqQCTIDSMQSSLDSEAKSRIEATRLKKKMEEdLNEMELQLSCANRQVSEATKSLGQl 1700
Cdd:TIGR00618 657 QERVREHALSIRVLPKELLASR--QLALQKMQSEKEQLTYWKEMLAQCQTLLRE-LETHIEEYDREFNEIENASSSLGS- 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1701 qiqikDLQMQLDDSTQLNSDLKEQvavaeRRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATerINLFYTQNTSLLSQ 1780
Cdd:TIGR00618 733 -----DLAAREDALNQSLKELMHQ-----ARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAE--IQFFNRLREEDTHL 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1781 KKKLEadvAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKKKQDTIAH-LEKTRENMEQ--TITDLQKRLAEAEQT 1857
Cdd:TIGR00618 801 LKTLE---AEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHqLLKYEECSKQlaQLTQEQAKIIQLSDK 877
|
730
....*....|....*..
gi 1411134203 1858 ALMGSRKQIQKLESRVR 1874
Cdd:TIGR00618 878 LNGINQIKIQFDGDALI 894
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
899-1649 |
2.80e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.95 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 899 RGEEIAGLKEECAQLQKALEKSEFQR-EEL-KAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWL-----IKSKIQLEA 971
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKaEELrKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVkkaeeAKKDAEEAK 1243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 972 RVKELSERVEEEEEINSELTARGRKLEDECSELKKEIDDLETML-VKSEKEKRTTEHKVKnlTEEVEFLNEDISKLNRAA 1050
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEeKKKADEAKKAEEKKK--ADEAKKKAEEAKKADEAK 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1051 KVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMENLESSQRhl 1130
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK-- 1399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1131 AEELRKK--ELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKE----KLEAERTTRAKMEKERADLTQDLADLNERL 1204
Cdd:PTZ00121 1400 AEEDKKKadELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKadeaKKKAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1205 EEVGGASlaqlEITKKQE---TKFQKLRRDMEEATLHFEATSASlKKRHADSL--AELEGQVENLQQV--KQKLEKDRSD 1277
Cdd:PTZ00121 1480 EEAKKAD----EAKKKAEeakKKADEAKKAAEAKKKADEAKKAE-EAKKADEAkkAEEAKKADEAKKAeeKKKADELKKA 1554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1278 LQLEVDDLLTRIEQMTRAKAN-------AEKLCTLYEERLNEAnAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEA 1350
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDknmalrkAEEAKKAEEARIEEV-MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1351 LINQLSREKSNFTRQIEELRGQLEKETKSQSALAHALQKAQRDCDLLREqyEEEQEVKAELHRTLSKVNAEMVQWRMKYE 1430
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK--AEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1431 NNVIQKTEDLEDAKKELAIRLQEtAEAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADW 1510
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEE-AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1511 KQKHEESQTLLD----------ASRKEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEM 1580
Cdd:PTZ00121 1791 KRRMEVDKKIKDifdnfaniieGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADF 1870
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411134203 1581 EKVKKLIEQEKTEV-------QVTLEETEGALERNESKILRFQLELLKAKAE--LERKLSEKDEELENFRRKQQCTID 1649
Cdd:PTZ00121 1871 NKEKDLKEDDEEEIeeadeieKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDeyIKRDAEETREEIIKISKKDMCIND 1948
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
906-1557 |
5.28e-13 |
|
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: 74.37 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 906 LKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKskiqlEARVKELSERVEEEEE 985
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLK-----EDHEKIQHLEEEYKKE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 986 INSElTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLH 1065
Cdd:pfam05483 235 INDK-EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1066 MEEEKLSSLSKANLKLEQQVvglEGALEQERKAR-------INCERELHKLEGDLKLNQESMENLESSQRHLAEELRKKE 1138
Cdd:pfam05483 314 ALEEDLQIATKTICQLTEEK---EAQMEELNKAKaahsfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1139 LENSQMNSKVENEKGLVAQLQKMVKElqtqikdlKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVGGASLAQLEIT 1218
Cdd:pfam05483 391 SELEEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAI 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1219 KKQETKFQKLRRDMEEatlhfEATSASLKKrhadslAELEGQVENLQQVKQKLEKDRSDLQLEvddLLTRIEQMTRAKAN 1298
Cdd:pfam05483 463 KTSEEHYLKEVEDLKT-----ELEKEKLKN------IELTAHCDKLLLENKELTQEASDMTLE---LKKHQEDIINCKKQ 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1299 AEKLctlyeerLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETK 1378
Cdd:pfam05483 529 EERM-------LKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKK 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1379 SQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQKTEDLEDAKKELAIRLQETAEAM 1458
Cdd:pfam05483 602 QIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAK 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1459 GVANARNASLERARHRLQLELGDALSDLGKVRSaaaRLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALSTELLKL 1538
Cdd:pfam05483 682 AIADEAVKLQKEIDKRCQHKIAEMVALMEKHKH---QYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSL 758
|
650
....*....|....*....
gi 1411134203 1539 KHAYKESIVGQETLRRENK 1557
Cdd:pfam05483 759 KKQLEIEKEEKEKLKMEAK 777
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
996-1704 |
6.37e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 74.62 E-value: 6.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 996 KLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAH--QQTLDDLHMEEEKLSS 1073
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1074 ----LSKANLKLEQQVVGLEGALEQERKARINCERE----------------LHKLEGDLKLNQESMENLESSQRHLAEE 1133
Cdd:TIGR00618 275 qeavLEETQERINRARKAAPLAAHIKAVTQIEQQAQrihtelqskmrsraklLMKRAAHVKQQSSIEEQRRLLQTLHSQE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1134 LRKKELENSQMNSKVENEKGLvaQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERAdlTQDLADLNERLEEVggasla 1213
Cdd:TIGR00618 355 IHIRDAHEVATSIREISCQQH--TLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQA--TIDTRTSAFRDLQG------ 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1214 QLEITKKQEtKFQKLRRDMEEATLHFEATSASLKKRHAD----SLAELEGQVENLQQVKQKLEKdrsdlqlevddllTRI 1289
Cdd:TIGR00618 425 QLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKLEKIHLQesaqSLKEREQQLQTKEQIHLQETR-------------KKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1290 EQMTRAKANAEKLCTLyEERLNEANAKLDKVTQLAND--LAAQKTELWSESGEFLRRLE-EKEALINQLSREKSNFTRQI 1366
Cdd:TIGR00618 491 VVLARLLELQEEPCPL-CGSCIHPNPARQDIDNPGPLtrRMQRGEQTYAQLETSEEDVYhQLTSERKQRASLKEQMQEIQ 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1367 EELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQKTEDLEDAKKE 1446
Cdd:TIGR00618 570 QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1447 lairlqetaeamgvANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQsgkaLADWKQKHEESQTLLDASRK 1526
Cdd:TIGR00618 650 --------------ALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQ----LTYWKEMLAQCQTLLRELET 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1527 EIQALSTELLKLKHAykeSIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALE 1606
Cdd:TIGR00618 712 HIEEYDREFNEIENA---SSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQ 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1607 RNESKILRFQLELLKAKAELERKLSEKDEELENFRRKQQCTIDSMQSSLDSEAKSRIEATRLKKKMEEDLNEMElQLSCA 1686
Cdd:TIGR00618 789 FFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA-QLTQE 867
|
730 740
....*....|....*....|.
gi 1411134203 1687 NRQVSEATKSLG---QLQIQI 1704
Cdd:TIGR00618 868 QAKIIQLSDKLNginQIKIQF 888
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1026-1751 |
8.07e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 73.90 E-value: 8.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1026 EHKVKNLTEEVEFLNEDISKLNRAAKVVQeahqqtlDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERE 1105
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLD-------KNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1106 LHKLEGDLKLNQESMENLESSQRHLAEELRKKELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEaerttraK 1185
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELN-------L 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1186 MEKERADLTQDLADLNERLEevggASLAQLEITKKQETKFQKLRRDmeeatlhfeatsaslkkrhadsLAELEGQVENLQ 1265
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLL----KLELLLSNLKKKIQKNKSLESQ----------------------ISELKKQNNQLK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1266 QVKQKLEKDRSDLQLEVDDLLTRIEQMTRAKANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQKTELWSesgeflrrl 1345
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN--------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1346 EEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEmvqw 1425
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE---- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1426 rmkyENNVIQKTEDLEDAKKELAIRLQETAEAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGK 1505
Cdd:TIGR04523 379 ----NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1506 ALADWKQKHEESQTLLDASRKEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKK 1585
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1586 LIEQEKTEVQVTLEETEGALERN--ESKILRFQLELLKAKAE---LERKLSEKDEELENFR------RKQQCTIDSMQSS 1654
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTqksLKKKQEEKQELIDQKEkekkdlIKEIEEKEKKISS 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1655 LDSEAKSRIEATR----LKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAER 1730
Cdd:TIGR04523 615 LEKELEKAKKENEklssIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYK 694
|
730 740
....*....|....*....|.
gi 1411134203 1731 RNSLLQSELEDLRSLQEQTER 1751
Cdd:TIGR04523 695 KYITRMIRIKDLPKLEEKYKE 715
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
889-1334 |
8.94e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 8.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 889 KIKPLVKSSERGEEIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLqaeqETLANVEEQCEWLIKSKIQ 968
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 969 LEARVKELSERVeeeeeinsELTARGRKLEDECSELKK-----EIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDI 1043
Cdd:PRK03918 350 LEKRLEELEERH--------ELYEEAKAKKEELERLKKrltglTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1044 SKLNRAAKVVQEAHQQ--TLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARinceRELHKLEGDLKLNQESme 1121
Cdd:PRK03918 422 KELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLR----KELRELEKVLKKESEL-- 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1122 nleSSQRHLAEELRKKELENSQMN-SKVENEKGLVAQLQKMVKELQTQIKDLK---EKLEAERTTRAKMEKERADLTQDL 1197
Cdd:PRK03918 496 ---IKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDELEEEL 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1198 ADLNERLEEVGGASLAQLEITKKQETKFQKLRRDMEEATLHFEATSASLKKRHadslAELEGQVENLQQVKQKLEKDRSD 1277
Cdd:PRK03918 573 AELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLE----EELDKAFEELAETEKRLEELRKE 648
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1411134203 1278 L-QLEVDDLLTRIEQMTRAKANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQKTEL 1334
Cdd:PRK03918 649 LeELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
988-1591 |
1.50e-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: 73.13 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 988 SELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNraakvvqeahqQTLDDLHME 1067
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK-----------DKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1068 EEKLSSLSKAN----LKLEQQVVGLEGALEQERKARINCERELHKLEGDL-KLNQE------SMENLESSQRHLAEELRK 1136
Cdd:TIGR04523 105 LSKINSEIKNDkeqkNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELeKLNNKyndlkkQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1137 KELENSQMNSKVENEKGLVAQLQKMV---KELQTQIKDLKEKleaerttRAKMEKERADLTQDLADLNERLEEVGgaslA 1213
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLLSNLKKKIqknKSLESQISELKKQ-------NNQLKDNIEKKQQEINEKTTEISNTQ----T 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1214 QLEITKKQETKFQKlrrDMEEATLHFEATSASLKKRHaDSLAELEGQVENLQQVKQklekdrSDLQLEVDDLLTRIEqmt 1293
Cdd:TIGR04523 254 QLNQLKDEQNKIKK---QLSEKQKELEQNNKKIKELE-KQLNQLKSEISDLNNQKE------QDWNKELKSELKNQE--- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1294 rakanaEKLCTLyEERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKS-------NFTRQI 1366
Cdd:TIGR04523 321 ------KKLEEI-QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQsykqeikNLESQI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1367 EELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYEN------NVIQKTEDL 1440
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNldntreSLETQLKVL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1441 EDAKKELAIRLQETAEAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTL 1520
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411134203 1521 LDAS--RKEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEK 1591
Cdd:TIGR04523 554 LKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
912-1334 |
1.78e-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: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 912 QLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCE----WLIKSKIQLEARVKELSERVEEEEEIN 987
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNkikkQLSEKQKELEQNNKKIKELEKQLNQLK 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 988 SELTA-RGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHM 1066
Cdd:TIGR04523 295 SEISDlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1067 EEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMENLESSQRHLAEELRKKELENSQMNS 1146
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1147 KVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVGG------ASLAQLEITKK 1220
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKkisslkEKIEKLESEKK 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1221 Q-ETKFQKLRRDMEEatLHFEATSASLKKrhadSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRAKANA 1299
Cdd:TIGR04523 535 EkESKISDLEDELNK--DDFELKKENLEK----EIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEK 608
|
410 420 430
....*....|....*....|....*....|....*
gi 1411134203 1300 EKLCTLYEERLNEANAKLDKVTQLANDLAAQKTEL 1334
Cdd:TIGR04523 609 EKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
925-1611 |
1.85e-12 |
|
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: 72.95 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 925 EELKAKQVSLTQEKNDLILQLQAEQETLANVEEQcewlIKSKIQLEARVKELSER-VEEEEEINSELTARGRKLEDECSE 1003
Cdd:pfam12128 216 SRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQE----FNTLESAELRLSHLHFGyKSDETLIASRQEERQETSAELNQL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1004 LKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLD----DLHMEEEKLSSLSKANL 1079
Cdd:pfam12128 292 LRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPswqsELENLEERLKALTGKHQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1080 KLEQQVVGLEGALEQERK---ARINCERELHKLEGDLKLNQES--MENLESSQRH-LAEELRKKELENSQMNSKVENEKG 1153
Cdd:pfam12128 372 DVTAKYNRRRSKIKEQNNrdiAGIKDKLAKIREARDRQLAVAEddLQALESELREqLEAGKLEFNEEEYRLKSRLGELKL 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1154 LVAQLQkMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEvggaslaQLEITKKQETKFQKLRRDME 1233
Cdd:pfam12128 452 RLNQAT-ATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQ-------ASEALRQASRRLEERQSALD 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1234 EAT----------LHFEATSASLKKRHADSLAELE----------------GQVENLQQVKQKLEK-DRSDLQLEVDDLL 1286
Cdd:pfam12128 524 ELElqlfpqagtlLHFLRKEAPDWEQSIGKVISPEllhrtdldpevwdgsvGGELNLYGVKLDLKRiDVPEWAASEEELR 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1287 TRIEQMTRAKANAEKLCTLYEERLNEANAKLDKVtQLANDLAAQKTElwsESGEFLRRL-EEKEALINQLSREKSNFTRQ 1365
Cdd:pfam12128 604 ERLDKAEEALQSAREKQAAAEEQLVQANGELEKA-SREETFARTALK---NARLDLRRLfDEKQSEKDKKNKALAERKDS 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1366 IEELRGQLEKETKsQSALAHALQKAQRDcDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQKTEDLE-DAK 1444
Cdd:pfam12128 680 ANERLNSLEAQLK-QLDKKHQAWLEEQK-EQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALEtWYK 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1445 KELAirlqetaeAMGVANARNASLERARHrlqlELGDALSDLGKVRSAAARLDQKQLQSgkaladWKQKHEESQTLLDAS 1524
Cdd:pfam12128 758 RDLA--------SLGVDPDVIAKLKREIR----TLERKIERIAVRRQEVLRYFDWYQET------WLQRRPRLATQLSNI 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1525 RKEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVRegtknlTEMEKVKKLIE-QEKTEVQVTLEETEG 1603
Cdd:pfam12128 820 ERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLR------CEMSKLATLKEdANSEQAQGSIGERLA 893
|
....*...
gi 1411134203 1604 ALERNESK 1611
Cdd:pfam12128 894 QLEDLKLK 901
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1598-1898 |
2.39e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1598 LEETEGALERNESKI--LRFQLELLK---AKAELERKLSEKDEELE-----NFRRKQQCTIDSMQSSLDSEAKSRIEATR 1667
Cdd:COG1196 181 LEATEENLERLEDILgeLERQLEPLErqaEKAERYRELKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1668 LKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSD-------LKEQVAVAERRNSLLQSELE 1740
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREleerleeLEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1741 DLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLS 1820
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411134203 1821 EELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQTALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLE 1898
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
895-1447 |
4.39e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 895 KSSERGEEIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVK 974
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 975 ELSERVeeeeeinseltargRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQ 1054
Cdd:COG1196 362 EAEEAL--------------LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1055 EAHQQTLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKL---EGDLKLNQESMENLESSQRHLA 1131
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELleeLAEAAARLLLLLEAEADYEGFL 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1132 EELRKKELENSQmnskvENEKGLVAQLQKMVKELQTQIkdlkEKLEAERTTRAKMEKERADLTQDLADLNERLEEVGGAS 1211
Cdd:COG1196 508 EGVKAALLLAGL-----RGLAGAVAVLIGVEAAYEAAL----EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLP 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1212 LAQLEITKKQETKFQKLRRDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQ 1291
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1292 ---MTRAKANAEklctlyEERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEE 1368
Cdd:COG1196 659 ggsLTGGSRREL------LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1369 LRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEE-QEVKAELHRtLSKVN------AEMVQWRmkYENNVIQKtEDLE 1441
Cdd:COG1196 733 EREELLEELLEEEELLEEEALEELPEPPDLEELERElERLEREIEA-LGPVNllaieeYEELEER--YDFLSEQR-EDLE 808
|
....*.
gi 1411134203 1442 DAKKEL 1447
Cdd:COG1196 809 EARETL 814
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1188-1842 |
4.75e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.61 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1188 KERADLTQDLADLNeRLEE----VGGASLAQLEITKKQETKFQKLR---RDMEEATLHfeATSASLKKRhadsLAELEGQ 1260
Cdd:PRK02224 149 SDRQDMIDDLLQLG-KLEEyrerASDARLGVERVLSDQRGSLDQLKaqiEEKEEKDLH--ERLNGLESE----LAELDEE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1261 VENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRAKANAEKLctlyEERLNEANAKLDKVTQLANDLAAQKTELWSESGE 1340
Cdd:PRK02224 222 IERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDL----RETIAETEREREELAEEVRDLRERLEELEEERDD 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1341 FLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNA 1420
Cdd:PRK02224 298 LLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1421 EMVQWRmkyennviQKTEDLEDAKKELAIRLQETAEAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARlDQKQ 1500
Cdd:PRK02224 378 AVEDRR--------EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE-AEAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1501 LQSGKAlADWKQKHEESQTL--LDASRKEIQALSTELlklkhaykesivgqETLRRENKNLQEEISNLTnQVREGTKNLT 1578
Cdd:PRK02224 449 LEAGKC-PECGQPVEGSPHVetIEEDRERVEELEAEL--------------EDLEEEVEEVEERLERAE-DLVEAEDRIE 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1579 EMEKVKKLIEQEKTEVQVTLEETEGALErneskilrfqlELLKAKAELERKLSEKDEELEnfrrkqqctidsmqssldsE 1658
Cdd:PRK02224 513 RLEERREDLEELIAERRETIEEKRERAE-----------ELRERAAELEAEAEEKREAAA-------------------E 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1659 AKSRIEATRLK-KKMEEDLNEMELQLSCANRqVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQS 1737
Cdd:PRK02224 563 AEEEAEEAREEvAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEA 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1738 ELEDLRSLQEQTERGRrlSEEELLEATERInlfytqnTSLLSQKKKLEADVAQMQKEAEEVvqecqnaeekakkaateaA 1817
Cdd:PRK02224 642 EFDEARIEEAREDKER--AEEYLEQVEEKL-------DELREERDDLQAEIGAVENELEEL------------------E 694
|
650 660
....*....|....*....|....*
gi 1411134203 1818 NLSEELKKKQDTIAHLEKTRENMEQ 1842
Cdd:PRK02224 695 ELRERREALENRVEALEALYDEAEE 719
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1660-2024 |
5.20e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1660 KSRIEATRLK-KKMEEDLN-------EMELQLSCANRQVSEATKSLgQLQIQIKDLQMQLddstQLNSD--LKEQVAVAE 1729
Cdd:COG1196 171 KERKEEAERKlEATEENLErledilgELERQLEPLERQAEKAERYR-ELKEELKELEAEL----LLLKLreLEAELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1730 RRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVAQMQKEAEEvvqecqnaeeka 1809
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE------------ 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1810 kkaateaanLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQtALMGSRKQIQKLESRVRELEGELEGEIRRSAE 1889
Cdd:COG1196 314 ---------LEERLEELEEELAELEEELEELEEELEELEEELEEAEE-ELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1890 AQRGARRLERcikeltyQAEEDKKNLSRMQTQMDKLQLKVHNYKQQVEVAEAQANQYLSKYKKQQHELNEVKERAEVAES 1969
Cdd:COG1196 384 LAEELLEALR-------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1411134203 1970 QVNKLKIKAREFGKKVRQAQTELLVTLQGSKRIVSPALKGQQLEKYKEGAVSWPK 2024
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
91-136 |
5.80e-12 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 62.06 E-value: 5.80e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1411134203 91 DGKKKCWIPDGENAYIEAEVKgSEDDGTVIVETTDGKSLSIKEDKI 136
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIK-EEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
953-1593 |
1.12e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 953 ANVEEQCEWLIKSKIQLEARVKELSERVEEEEEINSELTARGRKLEdecsELKKEIDDLETMLVKSEKEKRTTEHKVKNL 1032
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1033 TEEVEFLNEDISKLNRAAKVVQEahqqtLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKariNCERELHKLEGD 1112
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKELKE-----LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN---GIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1113 LKLNQESMENLESSQRHLaEELRKKELEnsqmnskVENEKGLVAQLQKMVKELQ-TQIKDLKEKLEAERTTRAKMEKERA 1191
Cdd:PRK03918 337 EERLEELKKKLKELEKRL-EELEERHEL-------YEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1192 DLTQDLADLNERLEEVGGAslaqLEITKKQETKFQKLRRDMEeatlhfEATSASLKKRHADSLAELEGQVENLQQVKQKL 1271
Cdd:PRK03918 409 KITARIGELKKEIKELKKA----IEELKKAKGKCPVCGRELT------EEHRKELLEEYTAELKRIEKELKEIEEKERKL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1272 EKDRSdlqlEVDDLLTRIEQMTRAKANAEKLCTLyEERLNEANA-KLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEA 1350
Cdd:PRK03918 479 RKELR----ELEKVLKKESELIKLKELAEQLKEL-EEKLKKYNLeELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1351 LINQLsREKSNFTRQIEELRGQLEKETKSqsalahalqkaqRDCDLLREQYEEEQEVKAELHRTLSKVNAEmvqwrmkye 1430
Cdd:PRK03918 554 LKKKL-AELEKKLDELEEELAELLKELEE------------LGFESVEELEERLKELEPFYNEYLELKDAE--------- 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1431 nnviqktEDLEDAKKELAIRLQETAEAMGVANARNASLERARHRLQlELGDALSDlgkvrSAAARLDQKQLQSGKALADW 1510
Cdd:PRK03918 612 -------KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE-ELEKKYSE-----EEYEELREEYLELSRELAGL 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1511 KQKHEESQTLLDASRKEIQALSTELLKLKHaYKESIVGQETLRRENKNLQEEISNLTNQVREGTknLTEMEKVKKLIEQE 1590
Cdd:PRK03918 679 RAELEELEKRREEIKKTLEKLKEELEEREK-AKKELEKLEKALERVEELREKVKKYKALLKERA--LSKVGEIASEIFEE 755
|
...
gi 1411134203 1591 KTE 1593
Cdd:PRK03918 756 LTE 758
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1112-1975 |
2.91e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1112 DLKLNQESMENLESSQRHLAEELRKKELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEklEAERTTRAKMEKER- 1190
Cdd:PTZ00121 1039 DDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAE--EAKKTETGKAEEARk 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1191 ADLTQDLADLNERLEEVGGASLAQL--EITKKQETKFQKLRRDMEEATLHFEATSASLKKRHADSLAELE----GQVENL 1264
Cdd:PTZ00121 1117 AEEAKKKAEDARKAEEARKAEDARKaeEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEvrkaEELRKA 1196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1265 QQVKQ-----KLEKDRSDLQLEVDDLLTRIEQMTRA---KANAEKLCTLYEERLNEANAKLD--KVTQLANDLAAQKTEL 1334
Cdd:PTZ00121 1197 EDARKaeaarKAEEERKAEEARKAEDAKKAEAVKKAeeaKKDAEEAKKAEEERNNEEIRKFEeaRMAHFARRQAAIKAEE 1276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1335 WSESGEFLRRLEEKEALINQLSREKsnftRQIEELRGQLEKETKSQSALAHAlQKAQRDCDLLREQYEEEQEvKAELHRT 1414
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEK----KKADEAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKAEEAKK-AAEAAKA 1350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1415 LSKVNAEMVQWRMKYENNVIQKTEDledaKKELAIRLQETAEAMGVANARNASLERARHRlqlelGDALSDLGKVRSAAA 1494
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEE----AKKKADAAKKKAEEKKKADEAKKKAEEDKKK-----ADELKKAAAAKKKAD 1421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1495 RLDQKQLQSGKAlADWKQKHEESQTLLDASRKEIQALSTELLKlKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGT 1574
Cdd:PTZ00121 1422 EAKKKAEEKKKA-DEAKKKAEEAKKADEAKKKAEEAKKAEEAK-KKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1575 KNLTEMEKVKKLIEQ-EKTEVQVTLEETEGALERNESKILRFQLEllKAKAELERKLSE--KDEELENFRRKQQCTIDSM 1651
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEE--KKKADELKKAEElkKAEEKKKAEEAKKAEEDKN 1577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1652 QSSLDSEAKSRIEATRLKKKMEEDLNEMELQLSCANRQVSEATKSlgqlqiqikdlqmqlddstqlnSDLKEQVAVAERR 1731
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA----------------------EELKKAEEEKKKV 1635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1732 NSLLQSELEDLRslqeQTERGRRLSEEELLEATErinlfytqntsllsQKKKLEADvaqmQKEAEEVVQEcqnaEEKAKK 1811
Cdd:PTZ00121 1636 EQLKKKEAEEKK----KAEELKKAEEENKIKAAE--------------EAKKAEED----KKKAEEAKKA----EEDEKK 1689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1812 AATEAANLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQTALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQ 1891
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1892 RGARRLErciKELTYQAEEDKKNLSRMQTQMDKLQLKVHNYKQQVEvAEAQANQYLSKYKKQqhELNEVKERAEVAESQV 1971
Cdd:PTZ00121 1770 AEEIRKE---KEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE-GGKEGNLVINDSKEM--EDSAIKEVADSKNMQL 1843
|
....
gi 1411134203 1972 NKLK 1975
Cdd:PTZ00121 1844 EEAD 1847
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1117-1682 |
3.92e-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: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1117 QESMENLESSQRHLAEELRKKELensqmnskvenekglvaqLQKMVkELQTQIKDLKEKLEAERTTRAKM-----EKERA 1191
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIEL------------------LEPIR-ELAERYAAARERLAELEYLRAALrlwfaQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1192 DLTQDLADLNERLEEVggasLAQLEITKKQETKFQKLRRDMEEAtlhfeatsasLKKRHADSLAELEGQVENLQQVKQKL 1271
Cdd:COG4913 292 LLEAELEELRAELARL----EAELERLEARLDALREELDELEAQ----------IRGNGGDRLEQLEREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1272 EKDRSDLQlevdDLLTRIEQmtRAKANAEKLctlyEERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEAL 1351
Cdd:COG4913 358 ERRRARLE----ALLAALGL--PLPASAEEF----AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1352 INQLSREKSNFTRQIEELRgqleketksqSALAHALQKAQRD----CDLL--------------------------REQY 1401
Cdd:COG4913 428 IASLERRKSNIPARLLALR----------DALAEALGLDEAElpfvGELIevrpeeerwrgaiervlggfaltllvPPEH 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1402 EEE----------------QEVKAELHRTLSK---------------------VNAEMVQW------------------- 1425
Cdd:COG4913 498 YAAalrwvnrlhlrgrlvyERVRTGLPDPERPrldpdslagkldfkphpfrawLEAELGRRfdyvcvdspeelrrhprai 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1426 ------------------RMKYENNVIQktEDLEDAKKELAIRLQETAEAMGVANARNASLERARHRLQlELGDALSDLG 1487
Cdd:COG4913 578 tragqvkgngtrhekddrRRIRSRYVLG--FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLA 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1488 KVRSaaARLDQKQLQsgKALADWKQKHEEsqtlLDASRKEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLT 1567
Cdd:COG4913 655 EYSW--DEIDVASAE--REIAELEAELER----LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1568 NQVREGTKNLTEMEKVKKLIEQEKTEvqvtlEETEGALERNESKILRFQLEllKAKAELERKLSEKDEELEN----FRRK 1643
Cdd:COG4913 727 EELDELQDRLEAAEDLARLELRALLE-----ERFAAALGDAVERELRENLE--ERIDALRARLNRAEEELERamraFNRE 799
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1411134203 1644 QQCTIDSMQSSLDSEAK-----SRIEATRL---KKKMEEDLNEMELQ 1682
Cdd:COG4913 800 WPAETADLDADLESLPEylallDRLEEDGLpeyEERFKELLNENSIE 846
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1343-1961 |
7.17e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.84 E-value: 7.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1343 RRLEEKealiNQLSREKSNFTRQ-IEELRGQLEKETKSQSALAhalqkaqrdcDLLREQYEEEQEVKAELHRTLSKVNAE 1421
Cdd:pfam15921 92 RRLNES----NELHEKQKFYLRQsVIDLQTKLQEMQMERDAMA----------DIRRRESQSQEDLRNQLQNTVHELEAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1422 --MVQWRMKYENNVIQKTEDL----EDAKKELAIRLQETAEAMG--------VANARNASLERARHRLQLELGDALSDL- 1486
Cdd:pfam15921 158 kcLKEDMLEDSNTQIEQLRKMmlshEGVLQEIRSILVDFEEASGkkiyehdsMSTMHFRSLGSAISKILRELDTEISYLk 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1487 GKVRSAAARLDQKQLQSGKALADWKQKHEES-QTLLDASRKEIQALsTELLKLKHAYKESI-----VGQETLRRENKNLQ 1560
Cdd:pfam15921 238 GRIFPVEDQLEALKSESQNKIELLLQQHQDRiEQLISEHEVEITGL-TEKASSARSQANSIqsqleIIQEQARNQNSMYM 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1561 EEISNLTNQVREGTKNLTEMEKV--KKLIEQEKTEVQVTLEETEGALERN----ESKILRFQLE-LLKAKAELERKLS-- 1631
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMyeDKIEELEKQLVLANSELTEARTERDqfsqESGNLDDQLQkLLADLHKREKELSle 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1632 -EKDEELENFRRKQQCTIDSMQSSLDSEAK--SRIEATrLKKKMEEDLNEMELQLScANRQVSEATKSLGQLQIQIKDLQ 1708
Cdd:pfam15921 397 kEQNKRLWDRDTGNSITIDHLRRELDDRNMevQRLEAL-LKAMKSECQGQMERQMA-AIQGKNESLEKVSSLTAQLESTK 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1709 MQLDDSTQLNSDLKEQVAVAERRNSLLQSeledlrSLQEQtERGRRLSEEELLEATERINLFYTQntslLSQKKKLEADV 1788
Cdd:pfam15921 475 EMLRKVVEELTAKKMTLESSERTVSDLTA------SLQEK-ERAIEATNAEITKLRSRVDLKLQE----LQHLKNEGDHL 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1789 AQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDlqkRLAEAEQTALMGSRK--QI 1866
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIND---RRLELQEFKILKDKKdaKI 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1867 QKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQlkvHNYKQQVEVAEAQANQY 1946
Cdd:pfam15921 621 RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK---RNFRNKSEEMETTTNKL 697
|
650
....*....|....*
gi 1411134203 1947 LSKYKKQQHELNEVK 1961
Cdd:pfam15921 698 KMQLKSAQSELEQTR 712
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1254-1855 |
9.79e-11 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 67.07 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1254 LAELEGQVENLQQVKQKLEKD----RSDLQLEVDDLLTRIEQMTRAKANAEKLCTLYEERLNEANAKLDKVTQLANDLAA 1329
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEhkraRIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1330 QKTELwsesgefLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKA 1409
Cdd:pfam05557 84 YLEAL-------NKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1410 ELhRTLSKVNAEMVQwRMKYENNVIQKTED----LEDAKKELA--IRLQETAEAMGVANARNASLERARHRLQLELGDAL 1483
Cdd:pfam05557 157 NL-EKQQSSLAEAEQ-RIKELEFEIQSQEQdseiVKNSKSELAriPELEKELERLREHNKHLNENIENKLLLKEEVEDLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1484 SDLGKVRSAAARLDQKQLQSGKALADWKqkheesqtlldasrkeiqalstELLKLKHAYKESIVGQETLRRENKNLQEEI 1563
Cdd:pfam05557 235 RKLEREEKYREEAATLELEKEKLEQELQ----------------------SWVKLAQDTGLNLRSPEDLSRRIEQLQQRE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1564 SNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKILRFQLELLKAKAE--LERKLsekdeeLENFR 1641
Cdd:pfam05557 293 IVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKErdGYRAI------LESYD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1642 RKQQCTIDSMQSSLDSEaksriEATRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQlddstqlnSDL 1721
Cdd:pfam05557 367 KELTMSNYSPQLLERIE-----EAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQ--------ESL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1722 KEQVAVAERRNSLLQsELEDLRsLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVAQMQKEAEEVVQ- 1800
Cdd:pfam05557 434 ADPSYSKEEVDSLRR-KLETLE-LERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQa 511
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1411134203 1801 ECQNAEEkakkaateaanLSEELKKKQDTIAHLEKTRENM-EQTITDLQKRLAEAE 1855
Cdd:pfam05557 512 EIERLKR-----------LLKKLEDDLEQVLRLPETTSTMnFKEVLDLRKELESAE 556
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1521-1993 |
1.39e-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: 66.58 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1521 LDASRKEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEE 1600
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1601 TegaleRNESKILRFQLELLKAKAELERKLSEKDEELENFRRKQQCTIDSMQSSLD------SEAKSRIEATR-LKKKME 1673
Cdd:TIGR04523 192 I-----KNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINektteiSNTQTQLNQLKdEQNKIK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1674 EDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQldDSTQLNSDLKEQvavaerrnslLQSELEDLRSLQEQtergr 1753
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELKSE----------LKNQEKKLEEIQNQ----- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1754 rlseeeLLEATERINLFYTQNTSLLSQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKKKQDTIAHL 1833
Cdd:TIGR04523 330 ------ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1834 EKTRENMEQTITDLQKRLAEAEqtalmgsrKQIQKLESRVRELEGELEGEIRRSAEaqrgarrLERCIKELTYQAEEDKK 1913
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLE--------KEIERLKETIIKNNSEIKDLTNQDSV-------KELIIKNLDNTRESLET 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1914 NLSRMQTQMDKLQLKVHNYKQQVEVAEAQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVRQAQTELL 1993
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1125-1969 |
1.44e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.90 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1125 SSQRHLAEELRKKELENSQMNSKVENEKGLVAQLqkmvKELQTQIKDLKEKLEAERTTRAKMEK-ERADltQDLADLNER 1203
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAE----SDLEQDYQAASDHLNLVQTALRQQEKiERYQ--ADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1204 LEEvggaslaQLEITKKQETKFQKLRRDMEEAtlhfEATSASLKKRHAD---SLAELEGQVENLQQVKQKLEKDRSDLQ- 1279
Cdd:PRK04863 364 LEE-------QNEVVEEADEQQEENEARAEAA----EEEVDELKSQLADyqqALDVQQTRAIQYQQAVQALERAKQLCGl 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1280 --LEVDDLLTRIEQMT-RAKANAEKLCTLyEERLN---EANAKLDKVTQLANDLAAQ--KTELWSESGEFLRRLEEKEAL 1351
Cdd:PRK04863 433 pdLTADNAEDWLEEFQaKEQEATEELLSL-EQKLSvaqAAHSQFEQAYQLVRKIAGEvsRSEAWDVARELLRRLREQRHL 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1352 INQLSREKsnftRQIEELRGQLEKETKSQSALAHALQKAQRDCDL--LREQYEEEQEVKAElhrTLSKVNAEMVQWRMky 1429
Cdd:PRK04863 512 AEQLQQLR----MRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDedELEQLQEELEARLE---SLSESVSEARERRM-- 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1430 ennviqkteDLEDAKKELAIRLQetaeamgvanaRNASLERARHRLQlelgDALSDLGKvrsaaarldqkqlQSGKALAD 1509
Cdd:PRK04863 583 ---------ALRQQLEQLQARIQ-----------RLAARAPAWLAAQ----DALARLRE-------------QSGEEFED 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1510 WKQKHEESQTLL----------DASRKEIQALSTELLKLKHAYKESivgQETLRR--------------ENKNLQE--EI 1563
Cdd:PRK04863 626 SQDVTEYMQQLLerereltverDELAARKQALDEEIERLSQPGGSE---DPRLNAlaerfggvllseiyDDVSLEDapYF 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1564 SNLTNQ------------VREGTKNLTEMEKVKKLIEQEKT---EVQVTLEETEGALERNESKI-LRF------------ 1615
Cdd:PRK04863 703 SALYGParhaivvpdlsdAAEQLAGLEDCPEDLYLIEGDPDsfdDSVFSVEELEKAVVVKIADRqWRYsrfpevplfgra 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1616 ----QLELLKAKAELerkLSEKDEELENFRRKQQCTIdsmqssldsEAKSRIEATRLKKKMEEDlNEMELQLscANRQVS 1691
Cdd:PRK04863 783 arekRIEQLRAEREE---LAERYATLSFDVQKLQRLH---------QAFSRFIGSHLAVAFEAD-PEAELRQ--LNRRRV 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1692 EATKSLGQLQIQIKDLQMQLDdstqlnsDLKEQVavaerrnSLLQsELEDLRSLQEQTERGRRLSE-EELLEATERINLF 1770
Cdd:PRK04863 848 ELERALADHESQEQQQRSQLE-------QAKEGL-------SALN-RLLPRLNLLADETLADRVEEiREQLDEAEEAKRF 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1771 YTQNTSLLSQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKKK-----QDTIAHLEKTRENMEQtit 1845
Cdd:PRK04863 913 VQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEMLAKNSDLNEK--- 989
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1846 dLQKRLAEAEQtALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKnlSRMQTQMDKL 1925
Cdd:PRK04863 990 -LRQRLEQAEQ-ERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAE--ERARARRDEL 1065
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 1411134203 1926 QlkvhnykQQVEVAEAQANQYLSKYKKQQHELNEVKERAEVAES 1969
Cdd:PRK04863 1066 H-------ARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLER 1102
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1518-1984 |
1.46e-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: 66.58 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1518 QTLLDASRKEIQALSTELLKLK---HAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEV 1594
Cdd:TIGR04523 186 QKNIDKIKNKLLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1595 QVTLEETEGALERNESKILRFQLELLKAKAELE------------------RKLSEKDEELENFRRKQQCTIDSMQSSLD 1656
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqkeqdwnkelkselKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1657 SEAKSRIEATRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQ 1736
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1737 SELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEA 1816
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1817 ANLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQTAL-MGSRKQIQKLESRVRelegELEGEIRRSAEAQRGAR 1895
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNkDDFELKKENLEKEID----EKNKEIEELKQTQKSLK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1896 RLERCIKELTYQAEEDKKNLSRmqtQMDKLQLKVHNYKQQVEVAEAQANQYLSKYKKQQHELNEVKERAEVAESQVNKLK 1975
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIK---EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
....*....
gi 1411134203 1976 IKAREFGKK 1984
Cdd:TIGR04523 659 NKWPEIIKK 667
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
898-1424 |
1.67e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.60 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 898 ERGEEIAGLKEECAQLQKALEKSEFQREELKAKqvslTQEKNDLILQLQAEQETLAnveEQCEWLIKSKIQLEARVKels 977
Cdd:PRK02224 248 ERREELETLEAEIEDLRETIAETEREREELAEE----VRDLRERLEELEEERDDLL---AEAGLDDADAEAVEARRE--- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 978 erveeeeeinsELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISklnrAAKVVQEAH 1057
Cdd:PRK02224 318 -----------ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELE----EAREAVEDR 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1058 QQTLDDLhmeEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMENlessqrhlAEELRK- 1136
Cdd:PRK02224 383 REEIEEL---EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE--------AEALLEa 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1137 -------KELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEaERTTRAKMEKERADLTQDLADLNERLEEvgg 1209
Cdd:PRK02224 452 gkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE-RAEDLVEAEDRIERLEERREDLEELIAE--- 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1210 aslaQLEITKKQETKFQKLRRDMEEATLHFEATSASLKKRH------ADSLAELEGQVENLQQVKQKLEKDRSDLQlEVD 1283
Cdd:PRK02224 528 ----RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEeeaeeaREEVAELNSKLAELKERIESLERIRTLLA-AIA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1284 DLLTRIEQMTRAKANAEKLCTLYEERLNEanaKLDKVTQLANDL-AAQKTELWSESGEFLRRLEEKEALINQLSREKSNF 1362
Cdd:PRK02224 603 DAEDEIERLREKREALAELNDERRERLAE---KRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERDDL 679
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411134203 1363 TRQIeelrGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQevkaELHRTLSKVNAEMVQ 1424
Cdd:PRK02224 680 QAEI----GAVENELEELEELRERREALENRVEALEALYDEAE----ELESMYGDLRAELRQ 733
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1149-1614 |
1.91e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1149 ENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEK---------ERADLTQDLADLNERLEEVggasLAQLEITK 1219
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllqllplyqELEALEAELAELPERLEEL----EERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1220 KQETKFQKLRRDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRAKANA 1299
Cdd:COG4717 160 ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1300 EKLCTLYEERLneANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKS 1379
Cdd:COG4717 240 ALEERLKEARL--LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1380 QSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQKTEDLEDAKKElairlqETAEAMG 1459
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE------EELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1460 VANARNASLERARHRLQLELGDALSDLgkvrsaaarldqKQLQSGKALADWKQKHEESQTLLDASRKEIQALSTELLKLK 1539
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGEL------------EELLEALDEEELEEELEELEEELEELEEELEELREELAELE 459
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411134203 1540 HAyKESIVGQETLRRenknLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQvtlEETEGALERNESKILR 1614
Cdd:COG4717 460 AE-LEQLEEDGELAE----LLQELEELKAELRELAEEWAALKLALELLEEAREEYR---EERLPPVLERASEYFS 526
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
906-1177 |
2.67e-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: 65.81 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 906 LKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSERVEEEEE 985
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 986 INSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLH 1065
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1066 MEEEKLSSLSKANLKLEQQVVGLEGALEQ--ERKARINCERELHKLEGDLKLNQESMENLESSQRHLAEELRKKELENSQ 1143
Cdd:TIGR04523 521 SLKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1411134203 1144 MNSKVENEKGLVAQLQKMV-------KELQTQIKDLKEKLE 1177
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELekakkenEKLSSIIKNIKSKKN 641
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1624-1945 |
2.74e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.86 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1624 AELERKLSEKDEELENFRRKQ---QCTIDSMQSSLDSEAKSRIEATR---LKKKMEE--------DLNEMELQLSCANRQ 1689
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIerlDLIIDEKRQQLERLRREREKAERyqaLLKEKREyegyellkEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1690 VSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQV-AVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERIN 1768
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1769 LFYTQNTSLLSQKKKLEADVAQMQK--------------EAEEVVQECQNAEEKAKKAATEAANLSEELKKKQDTIAHLE 1834
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKrrdklteeyaelkeELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1835 KTRENMEQTITDLQKRLAEAEQtALMGSRKQIQKLESRVRelegelegeirrsaEAQRGARRLERCIKELTYQAEEDKKN 1914
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNA-AIAGIEAKINELEEEKE--------------DKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350
....*....|....*....|....*....|.
gi 1411134203 1915 LSRMQTQMDKLQLKVHNYKQQVEVAEAQANQ 1945
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQARA 501
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
897-1428 |
3.26e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 897 SERGEEIAGLKEECAQLQKALEKSEFQRE---ELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLiKSKIQLEARV 973
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEELKEeieELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL-EEKVKELKEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 974 KELSERVEEEEEINSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRttehKVKNLTEEVEFLNEDISKLNRAAKVV 1053
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKKLKELEKRLEELEERHELY 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1054 QEAhQQTLDDLHMEEEKLSSLSKAnlKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMENLESSQ------ 1127
Cdd:PRK03918 365 EEA-KAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvc 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1128 -RHLAEELRKKELENSQMN-SKVENEKglvaqlqKMVKELQTQIKDLKEKLEAERTTRAKMEKERaDLTQDLADLNERLE 1205
Cdd:PRK03918 442 gRELTEEHRKELLEEYTAElKRIEKEL-------KEIEEKERKLRKELRELEKVLKKESELIKLK-ELAEQLKELEEKLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1206 EVGgaslaqLEITKKQETKFQKLRRDMEEatlhFEATSASLKKRhADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDL 1285
Cdd:PRK03918 514 KYN------LEELEKKAEEYEKLKEKLIK----LKGEIKSLKKE-LEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1286 -LTRIEQMTRAKANAEKLCTLYEERLN---EANAKLDKVTQLANDLAAQKTELwsesGEFLRRLEEKEALINQLSREKS- 1360
Cdd:PRK03918 583 gFESVEELEERLKELEPFYNEYLELKDaekELEREEKELKKLEEELDKAFEEL----AETEKRLEELRKELEELEKKYSe 658
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411134203 1361 ----NFTRQIEELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELhRTLSKVNAEMVQWRMK 1428
Cdd:PRK03918 659 eeyeELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL-EKLEKALERVEELREK 729
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1631-1862 |
4.35e-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: 64.01 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1631 SEKDEELENFRRKQQCTIDSMQSSLDSEAKSRIEATRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQ 1710
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1711 LDdstQLNSDLKEQVAVAERRNS------LLQSE--LEDLRSLQ--EQTERGRRLSEEELLEATERINlfyTQNTSLLSQ 1780
Cdd:COG4942 99 LE---AQKEELAELLRALYRLGRqpplalLLSPEdfLDAVRRLQylKYLAPARREQAEELRADLAELA---ALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1781 KKKLEADVAQMQKEAEEVVQEcqnaeekAKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQTALM 1860
Cdd:COG4942 173 RAELEALLAELEEERAALEAL-------KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
..
gi 1411134203 1861 GS 1862
Cdd:COG4942 246 AG 247
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
897-1308 |
6.43e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 897 SERGEEIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAeqetlanVEEQCEWLIKSKIQLEARVKel 976
Cdd:PRK02224 289 EELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA-------HNEEAESLREDADDLEERAE-- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 977 sERVEEEEEINSELTARGRKLED---ECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDI----SKLNRA 1049
Cdd:PRK02224 360 -ELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREaeleATLRTA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1050 AKVVQEA--------------------HQQTLDDlhmEEEKLSSLSKANLKLEQQVVGLEGALEQERKARiNCERELHKL 1109
Cdd:PRK02224 439 RERVEEAealleagkcpecgqpvegspHVETIEE---DRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1110 EGDLKLNQESMENLESS---QRHLAEELRKK--ELENS-QMNSKVENEKGLVAQ-LQKMVKELQTQIKDLKEKLEAERTT 1182
Cdd:PRK02224 515 EERREDLEELIAERRETieeKRERAEELRERaaELEAEaEEKREAAAEAEEEAEeAREEVAELNSKLAELKERIESLERI 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1183 RAKMEkERADLTQDLADLNERLEEvggasLAQLEITKKQETKFQKLRRDMEEATLHFEATSA--SLKKRHADSLAELEGQ 1260
Cdd:PRK02224 595 RTLLA-AIADAEDEIERLREKREA-----LAELNDERRERLAEKRERKRELEAEFDEARIEEarEDKERAEEYLEQVEEK 668
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1411134203 1261 VENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRAKANAEKLCTLYEE 1308
Cdd:PRK02224 669 LDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEALYDE 716
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1340-1905 |
6.53e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1340 EFLRR--LEEKE--ALINQLsreKSNFtRQIEELRGQLEKETKSQSALAHALQKAQRdCDLLREQYEEEQEVKAEL---- 1411
Cdd:COG4913 211 DFVREymLEEPDtfEAADAL---VEHF-DDLERAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAALrlwf 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1412 -HRTLSKVNAEMVQWRMKYENNVIQKtEDLEDAKKELAIRLQETAEAM-GVANARNASLERARHRLQLELGDALSDLGKV 1489
Cdd:COG4913 286 aQRRLELLEAELEELRAELARLEAEL-ERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1490 RSAAARLDQKQLQSGKALADwkqKHEESQTLLDASRKEIQALSTELLKLKhaykesiVGQETLRRENKNLQEEISNLtnq 1569
Cdd:COG4913 365 EALLAALGLPLPASAEEFAA---LRAEAAALLEALEEELEALEEALAEAE-------AALRDLRRELRELEAEIASL--- 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1570 vREGTKNLT-EMEKVKKLIEQE--KTE---------VQVTLEET--EGALERneskILR-FQLELLkAKAELERKLSEKd 1634
Cdd:COG4913 432 -ERRKSNIPaRLLALRDALAEAlgLDEaelpfvgelIEVRPEEErwRGAIER----VLGgFALTLL-VPPEHYAAALRW- 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1635 eeLENFRRKQQCTIDSMQSSLDSEAKSRIEATRLKKKMEEDLN------EMEL-------------QLSCANRQVSEA-- 1693
Cdd:COG4913 505 --VNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHpfrawlEAELgrrfdyvcvdspeELRRHPRAITRAgq 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1694 TKSLGQLQiqikdlqmQLDDSTQLNSD-------------LKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEEL 1760
Cdd:COG4913 583 VKGNGTRH--------EKDDRRRIRSRyvlgfdnraklaaLEAELAELEEELAEAEERLEALEAELDALQERREALQRLA 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1761 LEATERINLFYTQNT--SLLSQKKKLEA---DVAQMQKEAEEVVQEcqnaeekakkaateAANLSEELKKKQDTIAHLEK 1835
Cdd:COG4913 655 EYSWDEIDVASAEREiaELEAELERLDAssdDLAALEEQLEELEAE--------------LEELEEELDELKGEIGRLEK 720
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411134203 1836 TRENMEQTITDLQKRLAEAEQtalMGSRKQIQKLESRVRELEG-ELEGEIRRSAEAQRGA--RRLERCIKELT 1905
Cdd:COG4913 721 ELEQAEEELDELQDRLEAAED---LARLELRALLEERFAAALGdAVERELRENLEERIDAlrARLNRAEEELE 790
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
901-1446 |
6.70e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.27 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 901 EEIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSERV 980
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 981 EEEEEINSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKV----------KNLTEEVEFLNEDISKLNRAA 1050
Cdd:TIGR04523 155 EKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlkkkiqknKSLESQISELKKQNNQLKDNI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1051 KVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLK-LNQESMENLESSqrh 1129
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdLNNQKEQDWNKE--- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1130 LAEELRKKELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDL-------KEKLEAERTTRAKMEKERADLTQDLADLNE 1202
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSesensekQRELEEKQNEIEKLKKENQSYKQEIKNLES 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1203 RLEEVGGASLAQLEITKKQETKFQKLRRDMEeatlhfeatsaslkkrhadslaELEGQVENLQQVKQKLEKDRSDLQLEV 1282
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLQQEKE----------------------LLEKEIERLKETIIKNNSEIKDLTNQD 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1283 DDLLTRIEQMTRAKANAEKLCTLYEERLNEANAKLDKV-------TQLANDLAAQKTELWSESGEFLRRLEEKEALINQL 1355
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKqkelkskEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1356 SREKSNFTRQIEELRGQLEK--ETKSQSALAHALQKAQRDCDLLREQYEE---EQEVKAELHRTLSKVNAEMVQWRMKYE 1430
Cdd:TIGR04523 530 ESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSlkkKQEEKQELIDQKEKEKKDLIKEIEEKE 609
|
570
....*....|....*.
gi 1411134203 1431 NNVIQKTEDLEDAKKE 1446
Cdd:TIGR04523 610 KKISSLEKELEKAKKE 625
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
897-1332 |
7.87e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 7.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 897 SERGEEIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDL--ILQLQAEQETLANVEEQCEWLIKSKIQLEARVK 974
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 975 ELserveeeeeinSELTARGRKLEDECSELKKEIDDLEtmlvksEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQ 1054
Cdd:COG4717 157 EL-----------RELEEELEELEAELAELQEELEELL------EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1055 EAHQQTLDDLHMEEEKLSSLSKAN-LKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQE----SMENLESSQRH 1129
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEErLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGllalLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1130 LAEELRKKELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEA--ERTTRAKMEKERADLTQDLADLNERLEEV 1207
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEElqELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1208 GGASLAQLEITKKQETKFQKLRRDMEEATLHFEATSASLKKRHAD-SLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLL 1286
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELREELAELE 459
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1411134203 1287 TRIEQMTRAKAnaeklctlYEERLNEANAKLDKVTQLANDLAAQKT 1332
Cdd:COG4717 460 AELEQLEEDGE--------LAELLQELEELKAELRELAEEWAALKL 497
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
888-1348 |
1.14e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 888 FKIKPLVKSSERGEEIAGLKEECAQLQKA---LEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIK 964
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERikeLEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 965 SKIQLEARVKELSERVEEEEEinsELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEE--VEFLNED 1042
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKE---EIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrKELLEEY 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1043 ISKLNRAAKVVQEAHQQ---------TLDDLHMEEEKLSSLSKA-----NLKLEQQVVGLEGALEQERKARiNCERELHK 1108
Cdd:PRK03918 458 TAELKRIEKELKEIEEKerklrkelrELEKVLKKESELIKLKELaeqlkELEEKLKKYNLEELEKKAEEYE-KLKEKLIK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1109 LEGD---LKLNQESMENLESSQRHLAEELRKKELENSQMNSKVENEK-GLVAQLQKMVKELQT------QIKDLKEKLEA 1178
Cdd:PRK03918 537 LKGEiksLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPfyneylELKDAEKELER 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1179 ERTTRAKMEKERADLTQDLADLNERLEEVGGaSLAQLEiTKKQETKFQKLRRDMEEatlhfeatsasLKKRHADSLAELE 1258
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRK-ELEELE-KKYSEEEYEELREEYLE-----------LSRELAGLRAELE 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1259 GQVENLQQVKQKLEKDRSDLQlEVDDLLTRIEQMTRAKANAEKLCTLYEERLNEAN-AKLDKVTQLANDLAAQKTElWSE 1337
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEELREKVKKYKALLKeRALSKVGEIASEIFEELTE-GKY 761
|
490
....*....|.
gi 1411134203 1338 SGEFLRRLEEK 1348
Cdd:PRK03918 762 SGVRVKAEENK 772
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1553-1910 |
1.52e-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: 63.22 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1553 RRENKNLQEEISNLTNQ--VREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKILRFQLELLKAKAELERKL 1630
Cdd:pfam17380 239 RKESFNLAEDVTTMTPEytVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1631 SEKdEELENFRRKQQCTIDSMQSSLDSEAKSRIEATRL--KKKMEEDLNEMELQLSCanrqvsEATKSLGQLQIQIKDLQ 1708
Cdd:pfam17380 319 EEA-EKARQAEMDRQAAIYAEQERMAMERERELERIRQeeRKRELERIRQEEIAMEI------SRMRELERLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1709 MQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQT-ERGRRLSEEELLEATERINLfytQNTSLLSQKKKLEAD 1787
Cdd:pfam17380 392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAREMERVRL---EEQERQQQVERLRQQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1788 VAQMQKEAEEVVQECQNAEEKAKKAATEaanLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQ--TALMGSRKQ 1865
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKI---LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERrrEAEEERRKQ 545
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1411134203 1866 IQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEE 1910
Cdd:pfam17380 546 QEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1048-1413 |
1.58e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1048 RAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQER--KARINCERELHKLEG---DLKLNQESMEN 1122
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPErleELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1123 LESSQRHLAEELRKKELE-NSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDL--AD 1199
Cdd:COG4717 161 LEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1200 LNERLEE----------------------------------VGGASLAQLEITKKQETKFQKLRRDMEEATLHFEATSAS 1245
Cdd:COG4717 241 LEERLKEarlllliaaallallglggsllsliltiagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1246 LKK----------RHADSLAELEGQVENLQQVKQKLEKDRSDLQLEvdDLLTRIEQMtRAKANAEKLCTLYE--ERLNEA 1313
Cdd:COG4717 321 LEEllaalglppdLSPEELLELLDRIEELQELLREAEELEEELQLE--ELEQEIAAL-LAEAGVEDEEELRAalEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1314 NAKLDKVTQLANDLAAQKTELWSESGEFlrrleEKEALINQLSREKsnftRQIEELRGQLEKETKSQSALAHALQKAQRD 1393
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEAL-----DEEELEEELEELE----EELEELEEELEELREELAELEAELEQLEED 468
|
410 420
....*....|....*....|
gi 1411134203 1394 cDLLREQYEEEQEVKAELHR 1413
Cdd:COG4717 469 -GELAELLQELEELKAELRE 487
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1498-1991 |
2.67e-09 |
|
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: 62.83 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1498 QKQLQSGKALADwKQKHEESQTLLDASRKeIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNL 1577
Cdd:pfam15921 91 QRRLNESNELHE-KQKFYLRQSVIDLQTK-LQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1578 -TEMEKVKKL------IEQEKTEVQVTLEETEGA--LERNESKILRFQlellKAKAELERKLSEKDEELeNFRRKQQCTI 1648
Cdd:pfam15921 169 nTQIEQLRKMmlshegVLQEIRSILVDFEEASGKkiYEHDSMSTMHFR----SLGSAISKILRELDTEI-SYLKGRIFPV 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1649 DSMQSSLDSEAKSRIEA--TRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDStqlNSDLKEQVA 1726
Cdd:pfam15921 244 EDQLEALKSESQNKIELllQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ---NSMYMRQLS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1727 VAERRNSLLQSELEDLRSLQE----QTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVAQMQKEAEevVQEC 1802
Cdd:pfam15921 321 DLESTVSQLRSELREAKRMYEdkieELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS--LEKE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1803 QNAeekakkaateaaNLSEELKKKQDTIAHLEKTRE--NMEqtitdlqkrlaeaeqtalmgsrkqIQKLESRVRELEGEL 1880
Cdd:pfam15921 399 QNK------------RLWDRDTGNSITIDHLRRELDdrNME------------------------VQRLEALLKAMKSEC 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1881 EGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVHNYKQQVEVAEAQANQYLSKYKKQQHELNEV 1960
Cdd:pfam15921 443 QGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKL 522
|
490 500 510
....*....|....*....|....*....|.
gi 1411134203 1961 KERAEVAESQVNKLKIKarefGKKVRQAQTE 1991
Cdd:pfam15921 523 RSRVDLKLQELQHLKNE----GDHLRNVQTE 549
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
995-1643 |
2.79e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 995 RKLEDECSELKKEIDDLETMlvksEKEKRTTEHKVKNLTEEVEfLNEDISKLnRAAKVVQEAHQQTLDDLHmEEEKLSSL 1074
Cdd:COG4913 221 PDTFEAADALVEHFDDLERA----HEALEDAREQIELLEPIRE-LAERYAAA-RERLAELEYLRAALRLWF-AQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1075 SKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQ-ESMENLESSQRHLAEELRKKELENSQMNSKVENEKG 1153
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1154 LVAQLQKMVKELQTQIKDLKEKLEAERttrAKMEKERADLTQDLADLNERLEEVggasLAQLEITKKQET----KFQKLR 1229
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEEL---EALEEALAEAEAALRDLRRELREL----EAEIASLERRKSnipaRLLALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1230 RDMEEATlhfeatsaSLKKRHADSLAEL----------EGQVE---------------NLQQVKQKLE--KDRSDLQLEV 1282
Cdd:COG4913 447 DALAEAL--------GLDEAELPFVGELievrpeeerwRGAIErvlggfaltllvppeHYAAALRWVNrlHLRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1283 DDLLTRIEQMTRAKAN--AEKL----CTLY---EERLNEAN--AKLDKVTQLAN-DLAAQKTELWSESGEF--------- 1341
Cdd:COG4913 519 VRTGLPDPERPRLDPDslAGKLdfkpHPFRawlEAELGRRFdyVCVDSPEELRRhPRAITRAGQVKGNGTRhekddrrri 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1342 ----------LRRLEEKEALINQLSREKSNFTRQIEELRGQLEketksqsalahALQKAQRDCDLLREQYEEEQEVkAEL 1411
Cdd:COG4913 599 rsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELD-----------ALQERREALQRLAEYSWDEIDV-ASA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1412 HRTLSKVNAEMvqwrmkyennviqktEDLEDAKKELairlqetaeamgvanarnASLERARHRLQLELGDALSDLGKVRS 1491
Cdd:COG4913 667 EREIAELEAEL---------------ERLDASSDDL------------------AALEEQLEELEAELEELEEELDELKG 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1492 AAARLDQKqlqsgkaLADWKQKHEESQTLLDASRKEIQALSTELLKlkhAYKESIVGQETLRRENKNLQEEISNLTNQVR 1571
Cdd:COG4913 714 EIGRLEKE-------LEQAEEELDELQDRLEAAEDLARLELRALLE---ERFAAALGDAVERELRENLEERIDALRARLN 783
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411134203 1572 EGTKNLTE-MEKVKKLIEQEKTEVQVTLEETEGALERNESkiLRfQLELLKAKAELERKLSE-KDEELENFRRK 1643
Cdd:COG4913 784 RAEEELERaMRAFNREWPAETADLDADLESLPEYLALLDR--LE-EDGLPEYEERFKELLNEnSIEFVADLLSK 854
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
903-1257 |
3.57e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 903 IAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDL--ILQLQAEQETLANVEEQCEwlikskiQLEARVKELSERv 980
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIA-------ELEAELERLDAS- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 981 eeeeeiNSELtargRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEdisKLNRAAKVVQEAHQQT 1060
Cdd:COG4913 684 ------SDDL----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD---RLEAAEDLARLELRAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1061 LDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERE-LHKLEGDLKLNQESMENLESSQRHLAeelrkkEL 1139
Cdd:COG4913 751 LEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLD------RL 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1140 ENSqmnskvenekGLVAQLQKMVKELQTQIKDLKEKLeaerttRAKMEKERADLTQDLADLNERLEEV--GGASLAQLEI 1217
Cdd:COG4913 825 EED----------GLPEYEERFKELLNENSIEFVADL------LSKLRRAIREIKERIDPLNDSLKRIpfGPGRYLRLEA 888
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1411134203 1218 TKKQETKFQKLRRDMEEATLHFEATSASLKKRHADSLAEL 1257
Cdd:COG4913 889 RPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRL 928
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
899-1259 |
4.14e-09 |
|
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: 62.06 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 899 RGEEIAGLKEECAQLQKALEKSEFQREELKAKQVSLT-------------QEKN-----------------DLILQ---- 944
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLEssertvsdltaslQEKEraieatnaeitklrsrvDLKLQelqh 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 945 LQAEQETLANVEEQCEWLiksKIQLEARVKELSERVEEEEEINSELTARGRK---LEDECSELKKEIDD--LETMLVKSE 1019
Cdd:pfam15921 536 LKNEGDHLRNVQTECEAL---KLQMAEKDKVIEILRQQIENMTQLVGQHGRTagaMQVEKAQLEKEINDrrLELQEFKIL 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1020 KEK-----RTTEHKVKNLT-EEVEFLNEDISKLnRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQvvgLEGALE 1093
Cdd:pfam15921 613 KDKkdakiRELEARVSDLElEKVKLVNAGSERL-RAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN---FRNKSE 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1094 QERKARINCERELHKLEGDLKLNQESMENLESSQRHlaeelrkkelensQMNSKVENEKGLVAQlQKMVKELQTQIKDLK 1173
Cdd:pfam15921 689 EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH-------------AMKVAMGMQKQITAK-RGQIDALQSKIQFLE 754
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1174 EKLEAERTTRAKMEKERADLTQDLADLNERLEEVGGaslaQLEITKKQETKFQKLRRDME----EATLHF---------- 1239
Cdd:pfam15921 755 EAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAG----ELEVLRSQERRLKEKVANMEvaldKASLQFaecqdiiqrq 830
|
410 420
....*....|....*....|
gi 1411134203 1240 EATSASLKKRHADSLAELEG 1259
Cdd:pfam15921 831 EQESVRLKLQHTLDVKELQG 850
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1103-1344 |
4.88e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1103 ERELHKLEGDLKLNQESMENLESSQRHLAEELRKKELEnsqmnskvenekglVAQLQKMVKELQTQIKDLKEKLEAERTT 1182
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR--------------IAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1183 RAKMEKERADLTQDLADLNERLEEVGGASlaQLEITKKQETKFQKLRRDMeeatlHFEATSASLKKRhadsLAELEGQVE 1262
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQP--PLALLLSPEDFLDAVRRLQ-----YLKYLAPARREQ----AEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1263 NLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRAKANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQKTELWSESGEFL 1342
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
..
gi 1411134203 1343 RR 1344
Cdd:COG4942 241 ER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
914-1593 |
6.57e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 61.28 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 914 QKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEwlikskiQLEARVKELSERVEEEEEINSELTar 993
Cdd:pfam05483 119 RKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCA-------RSAEKTKKYEYEREETRQVYMDLN-- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 994 grkledecSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKlnraakvvqeahqqtldDLHMEEEKLSS 1073
Cdd:pfam05483 190 --------NNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKK-----------------EINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1074 LSKANLKLEQQVVGLEGALEQERKarincerELHKLEGDLKLNQESMENLESSQRHLAEEL-------------RKKELE 1140
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLLEESRD-------KANQLEEKTKLQDENLKELIEKKDHLTKELedikmslqrsmstQKALEE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1141 NSQMNSK-----VENEKGLVAQLQK-------MVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVg 1208
Cdd:pfam05483 318 DLQIATKticqlTEEKEAQMEELNKakaahsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEM- 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1209 gaslaqLEITKKQETKFQKLRRDM-EEATLHFEatsaslKKRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDdlLT 1287
Cdd:pfam05483 397 ------TKFKNNKEVELEELKKILaEDEKLLDE------KKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLT--AI 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1288 RIEQMTRAKANAEKLCTLYEERLneanaKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIE 1367
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEKEKL-----KNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIE 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1368 ELRgqlEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYEN---NVIQKTEDLEDAK 1444
Cdd:pfam05483 538 NLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNlkkQIENKNKNIEELH 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1445 KE-LAIRLQETAEamgvaNARNASLERARHRLQLELGDALSDLGKVRSAAAR-LDQKQLQSGKALADWKQKH---EESQT 1519
Cdd:pfam05483 615 QEnKALKKKGSAE-----NKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKeIEDKKISEEKLLEEVEKAKaiaDEAVK 689
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411134203 1520 LLDASRKEIQALSTELLKL----KHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNL-TEMEKVKKLIEQEKTE 1593
Cdd:pfam05483 690 LQKEIDKRCQHKIAEMVALmekhKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIkAELLSLKKQLEIEKEE 768
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
907-1649 |
1.07e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 60.75 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 907 KEECAQLQKALEK--SEFQREELKAKQVSLTQEKNDLILQLQAEQETLanveeqcEWLIKSKIQLEARvkelserveeee 984
Cdd:TIGR00618 195 KAELLTLRSQLLTlcTPCMPDTYHERKQVLEKELKHLREALQQTQQSH-------AYLTQKREAQEEQ------------ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 985 einseltargRKLEDECSELKKEIDDLETMLVKSEK--EKRTTEHKVKNLTEEVEFLNEdiskLNRAAKVVQEAHQQTLD 1062
Cdd:TIGR00618 256 ----------LKKQQLLKQLRARIEELRAQEAVLEEtqERINRARKAAPLAAHIKAVTQ----IEQQAQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1063 DLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCEREL---------HKLEGDLKLNQESMENLESSQRHLAEE 1133
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATsireiscqqHTLTQHIHTLQQQKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1134 LRKKELENSQMNSKVENEKGLVAQLQKMVKELQTQIK--DLKEKLEAERTTRAKME-----------KERADLTQDLADL 1200
Cdd:TIGR00618 402 LDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRyaELCAAAITCTAQCEKLEkihlqesaqslKEREQQLQTKEQI 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1201 NERLEEVGGASLAQLEITKKQEtkfqklrRDMEEATLHFEAtsaslKKRHADSLAELEGQVENLQQVKQKLEKDRSDLQL 1280
Cdd:TIGR00618 482 HLQETRKKAVVLARLLELQEEP-------CPLCGSCIHPNP-----ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1281 EVDDLLTRI----EQMTRAKANAEKLCTLYeerlNEANAKLDKVTQLANDLaaqktelwSESGEFLRRLEEKEALINQLS 1356
Cdd:TIGR00618 550 QLTSERKQRaslkEQMQEIQQSFSILTQCD----NRSKEDIPNLQNITVRL--------QDLTEKLSEAEDMLACEQHAL 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1357 REKSNftRQIEELRGQLEKETKSQSALAHALQKAQRDCDLLreqyEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQK 1436
Cdd:TIGR00618 618 LRKLQ--PEQDLQDVRLHLQQCSQELALKLTALHALQLTLT----QERVREHALSIRVLPKELLASRQLALQKMQSEKEQ 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1437 -TEDLED-AKKELAIRLQETAEamgvanarnASLERARHRLQLELGDALSDLGKVRSAAARLdqkqLQSGKALADWKQKH 1514
Cdd:TIGR00618 692 lTYWKEMlAQCQTLLRELETHI---------EEYDREFNEIENASSSLGSDLAAREDALNQS----LKELMHQARTVLKA 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1515 EEsqtlLDASRKEIQALSteLLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKN-LTEMEKVKKLIEQEKTE 1593
Cdd:TIGR00618 759 RT----EAHFNNNEEVTA--ALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdEDILNLQCETLVQEEEQ 832
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1411134203 1594 VQVTLEETEGALERNESKILRFQlELLKAKAELERKLSEKDEELENFRRKQQCTID 1649
Cdd:TIGR00618 833 FLSRLEEKSATLGEITHQLLKYE-ECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQ 887
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1156-1392 |
1.25e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1156 AQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLeevggaslaqleitKKQETKFQKLRRDMEEA 1235
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI--------------RALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1236 TLHFEATSASLKKRHADsLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRA-KANAEKLctlyEERLNEAN 1314
Cdd:COG4942 89 EKEIAELRAELEAQKEE-LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPArREQAEEL----RADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411134203 1315 AKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSALAHALQKAQR 1392
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1061-1659 |
1.48e-08 |
|
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: 60.15 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1061 LDDLHMEEEKLSSLSKANL----KLEQQVVGLEGALEQERKARINCErelhKLEGDLKLNQESMENLESSQRHLAEELRK 1136
Cdd:pfam07111 72 LQELRRLEEEVRLLRETSLqqkmRLEAQAMELDALAVAEKAGQAEAE----GLRAALAGAEMVRKNLEEGSQRELEEIQR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1137 keLENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEevggaslaqle 1216
Cdd:pfam07111 148 --LHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELE----------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1217 itkKQETKFQKLRRDMEEATLhfeatsaslKKRHADslaELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRAK 1296
Cdd:pfam07111 215 ---AQVTLVESLRKYVGEQVP---------PEVHSQ---TWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHML 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1297 ANAEKLCT--------LYEERLNEANAKL----DKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTR 1364
Cdd:pfam07111 280 ALQEEELTrkiqpsdsLEPEFPKKCRSLLnrwrEKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1365 QIEELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQE-----------VKAELHRTLSKVNAEMVQW-----RMK 1428
Cdd:pfam07111 360 ALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEqlkfvvnamssTQIWLETTMTRVEQAVARIpslsnRLS 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1429 YENNVIQKTEDLEDAKKELAIRLQETAEAMGVA------------------NARNASLERARHRLQLELGDAL----SDL 1486
Cdd:pfam07111 440 YAVRKVHTIKGLMARKVALAQLRQESCPPPPPAppvdadlsleleqlreerNRLDAELQLSAHLIQQEVGRAReqgeAER 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1487 GKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALSTELLKLKHAYKESIvgQETLRRENKNLQEEISN- 1565
Cdd:pfam07111 520 QQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQAL--QEKVAEVETRLREQLSDt 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1566 ---LTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKILRFQLELLKAKAELerkLSEKDEELENFRR 1642
Cdd:pfam07111 598 krrLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNLM---LATLQQEGLLSRY 674
|
650
....*....|....*..
gi 1411134203 1643 KQQCTIDSMQSSLDSEA 1659
Cdd:pfam07111 675 KQQRLLAVLPSGLDKKS 691
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1308-1937 |
2.00e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1308 ERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKetksqsalahaL 1387
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK-----------L 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1388 QKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRmKYENNVIQKTEDLEDAKKELAiRLQETAEAMGVANARNAS 1467
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE-ERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1468 LERARHRLQLELGD----------ALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTL------LDASRKEIQAL 1531
Cdd:PRK03918 305 YLDELREIEKRLSRleeeingieeRIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAkakkeeLERLKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1532 STEllKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVqvTLEETEGALERNESK 1611
Cdd:PRK03918 385 TPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL--TEEHRKELLEEYTAE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1612 ILRFQLELLKAKaELERKLSEKDEELENFRRKQQcTIDSMQSSLDseaksrieatrLKKKMEEDLNEMELQ-LSCANRQV 1690
Cdd:PRK03918 461 LKRIEKELKEIE-EKERKLRKELRELEKVLKKES-ELIKLKELAE-----------QLKELEEKLKKYNLEeLEKKAEEY 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1691 SEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEqvavAERRNSLLQSELEDLrsLQEQTERGRRlSEEELLEATERINLF 1770
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELAEL--LKELEELGFE-SVEELEERLKELEPF 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1771 YTQNTSLLSQKKKLEAdvaqmqkeaeevvqecqnaeekakkaateaanLSEELKKKQDTiahLEKTRENMEQTITDLQ-- 1848
Cdd:PRK03918 601 YNEYLELKDAEKELER--------------------------------EEKELKKLEEE---LDKAFEELAETEKRLEel 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1849 -KRLAEAEQT----ALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTyQAEEDKKNLSRMQTQMD 1923
Cdd:PRK03918 646 rKELEELEKKyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE-KAKKELEKLEKALERVE 724
|
650
....*....|....
gi 1411134203 1924 KLQLKVHNYKQQVE 1937
Cdd:PRK03918 725 ELREKVKKYKALLK 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1665-1895 |
2.08e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1665 ATRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLR- 1743
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1744 SLQEQTER-GRRLSEEELLEATERINLFYTQNTSLLSQK--KKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLS 1820
Cdd:COG4942 98 ELEAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411134203 1821 EELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQ--TALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGAR 1895
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAelAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
995-1587 |
2.10e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.53 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 995 RKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNraakvvqeahqqtlddlhmeeeklssl 1074
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELS--------------------------- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1075 skanlkleqqvvglegALEQERKariNCERELHKLEGDLKLNQESMENLESSqrhlaeELRKKELENSQMNSKVE----- 1149
Cdd:PRK01156 246 ----------------SLEDMKN---RYESEIKTAESDLSMELEKNNYYKEL------EERHMKIINDPVYKNRNyindy 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1150 -NEKGLVAQLQKMVKELQTQIKDLKE------KLEAERTTRAKMEKERADLTQDLADLNERLEEVGGA--SLAQLEITKK 1220
Cdd:PRK01156 301 fKYKNDIENKKQILSNIDAEINKYHAiikklsVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYlkSIESLKKKIE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1221 QETKFQKLRRDMEEATLHF-EATSASLKKRHAD---SLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTR----IEQM 1292
Cdd:PRK01156 381 EYSKNIERMSAFISEILKIqEIDPDAIKKELNEinvKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpVCGT 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1293 TRAKANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQKTELWSesgeFLRRLEEKEAlinqlsREKSNFTRQIEELRGQ 1372
Cdd:PRK01156 461 TLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKK----RKEYLESEEI------NKSINEYNKIESARAD 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1373 LEKETKSQSALAHALQKAQR--------DCDLLREQYEEEQEVKAElhrtLSKVNAEMVQWRmkyENNVIQKTEDLEDAK 1444
Cdd:PRK01156 531 LEDIKIKINELKDKHDKYEEiknrykslKLEDLDSKRTSWLNALAV----ISLIDIETNRSR---SNEIKKQLNDLESRL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1445 KELAIRLQETaeamgvanarNASLERARHRLQLELGDALSDLGKVRSAAARLD--QKQLQSGKALADWKQKHEESQTLLD 1522
Cdd:PRK01156 604 QEIEIGFPDD----------KSYIDKSIREIENEANNLNNKYNEIQENKILIEklRGKIDNYKKQIAEIDSIIPDLKEIT 673
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411134203 1523 ASRKEIQalsTELLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLI 1587
Cdd:PRK01156 674 SRINDIE---DNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1166-1967 |
3.06e-08 |
|
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: 59.20 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1166 QTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVGGASLAQLEITKKQEtkfqklrrDMEEATLHFEATSAS 1245
Cdd:COG3096 298 RRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQE--------DLEELTERLEEQEEV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1246 LKKRHaDSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTR---IEQMTRAKANAEKLCTL-------YEERLNEANA 1315
Cdd:COG3096 370 VEEAA-EQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRaiqYQQAVQALEKARALCGLpdltpenAEDYLAAFRA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1316 KLDKVTQLANDLAaQKTELWSES-GEFLRRLEEKEALINQLSREKSNFTRQieelrgQLEKETKSQSALAHALQKAQRDC 1394
Cdd:COG3096 449 KEQQATEEVLELE-QKLSVADAArRQFEKAYELVCKIAGEVERSQAWQTAR------ELLRRYRSQQALAQRLQQLRAQL 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1395 DLLREQYEEEQEVKAELHRtLSKvnaemvqwRMKYEnnvIQKTEDLEDAKKELAIRLQETAEAmgvanARNASLERARHR 1474
Cdd:COG3096 522 AELEQRLRQQQNAERLLEE-FCQ--------RIGQQ---LDAAEELEELLAELEAQLEELEEQ-----AAEAVEQRSELR 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1475 LQLE-LGDALSDLGKV----RSAAARLDQKQLQSGKALADWKQKHEESQTLLDASR-----------------KEIQALS 1532
Cdd:COG3096 585 QQLEqLRARIKELAARapawLAAQDALERLREQSGEALADSQEVTAAMQQLLEREReatverdelaarkqaleSQIERLS 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1533 -------TELLKLKHAykesiVGQETLRR--ENKNLQE--EISNL------------TNQVREGTKNLTEMEKVKKLIEQ 1589
Cdd:COG3096 665 qpggaedPRLLALAER-----LGGVLLSEiyDDVTLEDapYFSALygparhaivvpdLSAVKEQLAGLEDCPEDLYLIEG 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1590 EKT----EVQVTLEETEGALERNESKILRF----------------QLELLKAKAELerkLSEKDEELENFRRKQQCTid 1649
Cdd:COG3096 740 DPDsfddSVFDAEELEDAVVVKLSDRQWRYsrfpevplfgraarekRLEELRAERDE---LAEQYAKASFDVQKLQRL-- 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1650 smqssldSEAKSRIEATRLKKKMEEDlNEMELQLscANRQVSEATKSLGQLQIQIKDLQMQLDdstqlnsDLKEQVavae 1729
Cdd:COG3096 815 -------HQAFSQFVGGHLAVAFAPD-PEAELAA--LRQRRSELERELAQHRAQEQQLRQQLD-------QLKEQL---- 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1730 rrnSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQkkkLEADVAQMQK---EAEEVVQECQNAE 1806
Cdd:COG3096 874 ---QLLNKLLPQANLLADETLADRLEELREELDAAQEAQAFIQQHGKALAQ---LEPLVAVLQSdpeQFEQLQADYLQAK 947
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1807 EKAKKAATEAANLSEELKKK-----QDTIAHLEKTRENMEQtitdLQKRLAEAEQtALMGSRKQIQKLESRVrelegELE 1881
Cdd:COG3096 948 EQQRRLKQQIFALSEVVQRRphfsyEDAVGLLGENSDLNEK----LRARLEQAEE-ARREAREQLRQAQAQY-----SQY 1017
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1882 GEIRRSAEAQRGARR-----LERCIKELTYQAEEDKKNlsRMQTQMDKLQLKVHNYKQ-------QVEVAEAQANQYLSK 1949
Cdd:COG3096 1018 NQVLASLKSSRDAKQqtlqeLEQELEELGVQADAEAEE--RARIRRDELHEELSQNRSrrsqlekQLTRCEAEMDSLQKR 1095
|
890
....*....|....*...
gi 1411134203 1950 YKKQQHELNEVKERAEVA 1967
Cdd:COG3096 1096 LRKAERDYKQEREQVVQA 1113
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1166-1384 |
3.83e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1166 QTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVggasLAQLEITKKQEtkfQKLRRDMEEATLHFEATSAS 1245
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNEL----QAELEALQAEI---DKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1246 LKKRhADSLAELEGQVENLQQVkqkLEKDrsdlqlEVDDLLTRIEQMTRAKANAEKLCTLYEERLNEANAKLDKVTQLAN 1325
Cdd:COG3883 88 LGER-ARALYRSGGSVSYLDVL---LGSE------SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1411134203 1326 DLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSALA 1384
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1366-1760 |
5.05e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1366 IEELRGQLEKETKsqsalahaLQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEmvqwRMKYENNVIQKTEDLEDAKK 1445
Cdd:TIGR02169 159 IDEIAGVAEFDRK--------KEKALEELEEVEENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1446 ELAIRLQETAEAMGVANARNASLERARHRLQLELgdalSDLGKvRSAAARLDQKQLQsgkalADWKQKHEESQTLLdasR 1525
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEI----SELEK-RLEEIEQLLEELN-----KKIKDLGEEEQLRV---K 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1526 KEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLtnqvregtknLTEMEKVKKLIEQEKTEVQVTLEETEGAL 1605
Cdd:TIGR02169 294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL----------LAEIEELEREIEEERKRRDKLTEEYAELK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1606 ERNESKILRFQlELLKAKAELERKLSEKDEELENFRRKQQCTIDSMQSSLDSEAKSRIEATRLKKKM---EEDLNEMELQ 1682
Cdd:TIGR02169 364 EELEDLRAELE-EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIagiEAKINELEEE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1683 LSCANRQVSEATKSLGQLQIQIKDLQMQLddstqlnSDLKEQVAVAERRNSLLQSELEDL---RSLQEQTERGRRLSEEE 1759
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQEL-------YDLKEEYDRVEKELSKLQRELAEAeaqARASEERVRGGRAVEEV 515
|
.
gi 1411134203 1760 L 1760
Cdd:TIGR02169 516 L 516
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
894-1601 |
6.12e-08 |
|
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: 58.26 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 894 VKSSERGEEIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLanveeqcewlikskiQLEARV 973
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL---------------QEETRQ 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 974 KELserveeeeeinseLTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVV 1053
Cdd:pfam01576 484 KLN-------------LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1054 QEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKlNQESMENLESSQRHLAE- 1132
Cdd:pfam01576 551 QRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLA-EEKAISARYAEERDRAEa 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1133 ELRKKELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVGGASL 1212
Cdd:pfam01576 630 EAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQ 709
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1213 AQLEITKKQETKFQKLRRDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQM 1292
Cdd:pfam01576 710 ATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAA 789
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1293 TRAKANAEKlctlyeeRLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKS---NFTRQIEEL 1369
Cdd:pfam01576 790 NKGREEAVK-------QLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAaseRARRQAQQE 862
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1370 RGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAElhrtlskvNAEMVQWRMKyennviQKTEDLEDAKKELAi 1449
Cdd:pfam01576 863 RDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQS--------NTELLNDRLR------KSTLQVEQLTTELA- 927
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1450 rlQETAEAMGVANARNaSLERARHRLQLELGDALSDL-GKVRSAAARLDQKQLQSgkaladwkqkheESQtlLDASRKEI 1528
Cdd:pfam01576 928 --AERSTSQKSESARQ-QLERQNKELKAKLQEMEGTVkSKFKSSIAALEAKIAQL------------EEQ--LEQESRER 990
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411134203 1529 QALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEET 1601
Cdd:pfam01576 991 QAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDA 1063
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1298-1997 |
6.22e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.81 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1298 NAEKLCTLYEERLNEAnaklDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKET 1377
Cdd:pfam05483 72 NSEGLSRLYSKLYKEA----EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1378 KSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQKtedlEDAKKELAIRLQETAEA 1457
Cdd:pfam05483 148 KENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQA----ENARLEMHFKLKEDHEK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1458 MG-VANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQlqsgkalaDWKQKHEESQTLLDASRKEI----QALS 1532
Cdd:pfam05483 224 IQhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESR--------DKANQLEEKTKLQDENLKELiekkDHLT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1533 TELLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEE----TEGALERN 1608
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEllrtEQQRLEKN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1609 ESKILRFQLELLKAKAELErklsekdeELENFRRKQQCTIDSMQSSLdSEAKSRIEATRLKKKMEEDLNEMELQLscanr 1688
Cdd:pfam05483 376 EDQLKIITMELQKKSSELE--------EMTKFKNNKEVELEELKKIL-AEDEKLLDEKKQFEKIAEELKGKEQEL----- 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1689 qvseatksLGQLQIQIKDLQmqlddstqlnsDLKEQVAVAERRNSLLQSELEDLRSLQEQtergRRLSEEELLEATERI- 1767
Cdd:pfam05483 442 --------IFLLQAREKEIH-----------DLEIQLTAIKTSEEHYLKEVEDLKTELEK----EKLKNIELTAHCDKLl 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1768 --NLFYTQNTS-LLSQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKKKQDTI-AHLEKTRENMEQT 1843
Cdd:pfam05483 499 leNKELTQEASdMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVkCKLDKSEENARSI 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1844 ITDLQKRLAEAEQTALMGS--RKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRM--- 1918
Cdd:pfam05483 579 EYEVLKKEKQMKILENKCNnlKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIidn 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1919 -QTQMDKLQLKVHNYKQQVEVAEAQANQYLSKYK----KQQHELNEVKERAEVAESQVNKL-KIKAREFG--KKVRQAQT 1990
Cdd:pfam05483 659 yQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKeidkRCQHKIAEMVALMEKHKHQYDKIiEERDSELGlyKNKEQEQS 738
|
....*..
gi 1411134203 1991 ELLVTLQ 1997
Cdd:pfam05483 739 SAKAALE 745
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1254-1869 |
1.06e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1254 LAELEGQVENLQQVK---QKLEKDRSDLQlEVDDLLTRIEQMTRAKANAeklctLYEERLNEANAKLDKVTQLANDLAAQ 1330
Cdd:COG4913 244 LEDAREQIELLEPIRelaERYAAARERLA-ELEYLRAALRLWFAQRRLE-----LLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1331 KTELwsesgeflrrLEEKEALINQLSrekSNFTRQIEELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAE 1410
Cdd:COG4913 318 LDAL----------REELDELEAQIR---GNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1411 LHRTLSKVNAEMVQWRMKYENNVIQKTEDLEDAKKELAIRLQETAEAMGVANARNASLERARHRLQLELGDALSDL---- 1486
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELpfvg 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1487 -----------------GKVRSAAARL--DQKQLqsgKALADW----KQKH-------EESQTLLDASRKEIQALSTELL 1536
Cdd:COG4913 465 elievrpeeerwrgaieRVLGGFALTLlvPPEHY---AAALRWvnrlHLRGrlvyervRTGLPDPERPRLDPDSLAGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1537 KLKHAYK---ESIVGQ----------ETLRRENKNLQEE--IS--------NLTNQVRE----GTKNLtemEKVKKLiEQ 1589
Cdd:COG4913 542 FKPHPFRawlEAELGRrfdyvcvdspEELRRHPRAITRAgqVKgngtrhekDDRRRIRSryvlGFDNR---AKLAAL-EA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1590 EKTEVQVTLEETEGALERNESkilrfQLELLKAKAELERKLSEKDEELENFRRKQQcTIDSMQSSLDSEAKSRIEATRLK 1669
Cdd:COG4913 618 ELAELEEELAEAEERLEALEA-----ELDALQERREALQRLAEYSWDEIDVASAER-EIAELEAELERLDASSDDLAALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1670 KKMEE---DLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDD-----STQLNSDLKEQVAVAERRNSlLQSELED 1741
Cdd:COG4913 692 EQLEEleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedlaRLELRALLEERFAAALGDAV-ERELREN 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1742 LRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSqkkkleADVAqmqkEAEEVVQECQNAEekakkaateaanlSE 1821
Cdd:COG4913 771 LEERIDALRARLNRAEEELERAMRAFNREWPAETADLD------ADLE----SLPEYLALLDRLE-------------ED 827
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1411134203 1822 ELKKKQDTIAHLEKtrENMEQTITDLQKRLAEAEQTAlmgsRKQIQKL 1869
Cdd:COG4913 828 GLPEYEERFKELLN--ENSIEFVADLLSKLRRAIREI----KERIDPL 869
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1133-1340 |
1.07e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1133 ELRKKELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEE------ 1206
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1207 VGGASLAQLE--------------------ITKKQETKFQKLRRDMEEAtlhfeatsASLKKRHADSLAELEGQVENLQQ 1266
Cdd:COG3883 97 RSGGSVSYLDvllgsesfsdfldrlsalskIADADADLLEELKADKAEL--------EAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411134203 1267 VKQKLEKDRSDLQLEVDDLLTRIEQMTRAKANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQKTELWSESGE 1340
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
862-1283 |
1.27e-07 |
|
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: 57.36 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 862 RDALILIQWNIRAFMAVKNWAWMRLFFKIKPLVKSSERGEEIAGLKEE---CAQLQKALEKSEFQREELKAKQVSLTQek 938
Cdd:TIGR00606 590 RDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEesdLERLKEEIEKSSKQRAMLAGATAVYSQ-- 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 939 ndLILQLQAEQETLANVeeqCEWLIKSKIQLEARVKELSERVEEEEEINSELTARGRKLEDECSELKKEIDDLETMLVKS 1018
Cdd:TIGR00606 668 --FITQLTDENQSCCPV---CQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLK 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1019 EKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVV---QEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVVGLEG----- 1090
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpeEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGsdldr 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1091 ALEQERKARINCERELHKLEGDLKLNQESMENLESSQRHLAEELRKKELENSQMNSKVENEKGLVAQLQKMVKELQ---T 1167
Cdd:TIGR00606 823 TVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQsliR 902
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1168 QIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEvggaslaQLEITKKQETKFQKLRRDMEEatlHFEATSASLK 1247
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD-------KVNDIKEKVKNIHGYMKDIEN---KIQDGKDDYL 972
|
410 420 430
....*....|....*....|....*....|....*.
gi 1411134203 1248 KRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEVD 1283
Cdd:TIGR00606 973 KQKETELNTVNAQLEECEKHQEKINEDMRLMRQDID 1008
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1026-1965 |
1.42e-07 |
|
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: 57.37 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1026 EHKVKNLTEEVEFLNEDIskLNRAAKVV--QEAHQQTLDDLHMEEEKLSSLSKANLKLEQ-----QVVGLEGALEQERKA 1098
Cdd:TIGR01612 827 EDEIFKIINEMKFMKDDF--LNKVDKFInfENNCKEKIDSEHEQFAELTNKIKAEISDDKlndyeKKFNDSKSLINEINK 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1099 RINCERE----LHKLEGDLKL---NQESMENLESSQRHLAEELRKK----------------ELENSQMNSKVENEKGL- 1154
Cdd:TIGR01612 905 SIEEEYQnintLKKVDEYIKIcenTKESIEKFHNKQNILKEILNKNidtikesnlieksykdKFDNTLIDKINELDKAFk 984
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1155 ---VAQLQKMVKELQTQIKDLKEKLEAERTTRAKM---EKERA--DLTQDLADLNERLEEVGGASLAQL---------EI 1217
Cdd:TIGR01612 985 dasLNDYEAKNNELIKYFNDLKANLGKNKENMLYHqfdEKEKAtnDIEQKIEDANKNIPNIEIAIHTSIyniideiekEI 1064
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1218 TKKQETKFQKLRRDMEEATLHFEATSASLKKRHADSLAElEGQVENLQQVkQKLEKDRSDLQLEVDDLLTRIEQMTRAKA 1297
Cdd:TIGR01612 1065 GKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGK-EENIKYADEI-NKIKDDIKNLDQKIDHHIKALEEIKKKSE 1142
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1298 NaeklctlyeeRLNEANAKLDKVTQLANDlaaqktelwSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKET 1377
Cdd:TIGR01612 1143 N----------YIDEIKAQINDLEDVADK---------AISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIE 1203
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1378 KSQSALAHA----LQKAQRDCDLLREQYEEEQEVKAELHRTLSKVnaemvqwrMKYENNVIQKTEDLEDakkELAIRLQE 1453
Cdd:TIGR01612 1204 KDKTSLEEVkginLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAY--------IEDLDEIKEKSPEIEN---EMGIEMDI 1272
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1454 TAEaMGVANARNaSLERARHRLQLELGDALSDlgkVRSAAARLDQKQLQSgkalADWKQKHEESQTLLDASRKEIQALST 1533
Cdd:TIGR01612 1273 KAE-METFNISH-DDDKDHHIISKKHDENISD---IREKSLKIIEDFSEE----SDINDIKKELQKNLLDAQKHNSDINL 1343
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1534 ELLKLKHAYKesivgqeTLRREN-KNLQEEISNLTNQVREGTKNL-TEMEKVKKLIEQEKTEVqvTLEEtegalernesk 1611
Cdd:TIGR01612 1344 YLNEIANIYN-------ILKLNKiKKIIDEVKEYTKEIEENNKNIkDELDKSEKLIKKIKDDI--NLEE----------- 1403
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1612 ilrfqlellkAKAELERKLSEKD--EELENFRRKQQcTIDSMQSSLDSEAKSrieATRLKKKMEEDLNEMELqlscANRQ 1689
Cdd:TIGR01612 1404 ----------CKSKIESTLDDKDidECIKKIKELKN-HILSEESNIDTYFKN---ADENNENVLLLFKNIEM----ADNK 1465
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1690 VseatkslgQLQIQIKDLQMQLDDSTQLNsDLKEQVAVAERRNSLLQSEledlrslQEQTERGRRLSEEELLEATERINL 1769
Cdd:TIGR01612 1466 S--------QHILKIKKDNATNDHDFNIN-ELKEHIDKSKGCKDEADKN-------AKAIEKNKELFEQYKKDVTELLNK 1529
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1770 FYtqntsllsqKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDLQK 1849
Cdd:TIGR01612 1530 YS---------ALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQL 1600
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1850 RLAEAEQTALMGSR---------KQIQKLESRVRELE-GELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQ 1919
Cdd:TIGR01612 1601 SLENFENKFLKISDikkkindclKETESIEKKISSFSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELD 1680
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*.
gi 1411134203 1920 TQMDKLQLKVHNYKQQVEVAEAQANQYLSKYKKQqhELNEVKERAE 1965
Cdd:TIGR01612 1681 SEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKE--EIESIKELIE 1724
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1488-2009 |
2.19e-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: 56.52 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1488 KVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALSTELLKLKHAyKESIVGQETLRRENKNLQEEISNLT 1567
Cdd:TIGR00618 188 KKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQS-HAYLTQKREAQEEQLKKQQLLKQLR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1568 NQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETegALERNESKILRFQLELLKAKAELERKLSEKDEELENfRRKQQCT 1647
Cdd:TIGR00618 267 ARIEELRAQEAVLEETQERINRARKAAPLAAHIK--AVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ-QSSIEEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1648 IDSMQSSLDSEAKSRIEATRLKKKMEEDLNEMEL-----QLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLK 1722
Cdd:TIGR00618 344 RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLtqhihTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1723 EQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEAT----ERINLFYTQNTSLL--SQKKKLEADVAQMQKEAE 1796
Cdd:TIGR00618 424 GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAqslkEREQQLQTKEQIHLqeTRKKAVVLARLLELQEEP 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1797 EVVQECQNAEEKAKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQtalmgsrkqiqKLESRVREL 1876
Cdd:TIGR00618 504 CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE-----------QMQEIQQSF 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1877 EGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVHNYKQQVEVAEAQANQYLSKYKKQQHE 1956
Cdd:TIGR00618 573 SILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQ 652
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1411134203 1957 LNEVKERAEVAESQVnklkikaREFGKKVRQAQTELLVTLQGSKRIVSPALKG 2009
Cdd:TIGR00618 653 LTLTQERVREHALSI-------RVLPKELLASRQLALQKMQSEKEQLTYWKEM 698
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1156-1292 |
2.29e-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: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1156 AQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEV-----GGASLAQLEITKKQETKFQKLRR 1230
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgNVRNNKEYEALQKEIESLKRRIS 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411134203 1231 DMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQM 1292
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
895-1265 |
2.84e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 895 KSSERGEEIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVK 974
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 975 ELSERVEEeeeiNSELTARGRKLE-----------DECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDI 1043
Cdd:PRK02224 437 TARERVEE----AEALLEAGKCPEcgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1044 SKLNRAAKVVQ--EAHQQTLDDlhmEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESME 1121
Cdd:PRK02224 513 RLEERREDLEEliAERRETIEE---KRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1122 NLESSqRHLAEELRKKELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERA-----DLTQD 1196
Cdd:PRK02224 590 SLERI-RTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAeeyleQVEEK 668
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411134203 1197 LADLNER----LEEVGGA--SLAQLEITKKQETKFQKLRRDMEeaTLHFEATsaSLKKRHADSLAELEGQ-VENLQ 1265
Cdd:PRK02224 669 LDELREErddlQAEIGAVenELEELEELRERREALENRVEALE--ALYDEAE--ELESMYGDLRAELRQRnVETLE 740
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1045-1856 |
5.33e-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: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1045 KLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKanlKLEQQVvGLEGALEQERKArinCERELHKLEGDLKLnQESMENLE 1124
Cdd:COG3096 282 ELSERALELRRELFGARRQLAEEQYRLVEMAR---ELEELS-ARESDLEQDYQA---ASDHLNLVQTALRQ-QEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1125 SSQRHLAEELRKKELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERT-----TRAKMEKERADLTQDLAD 1199
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTraiqyQQAVQALEKARALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1200 LN-ERLEEVGGASLAQL-EITKKQETKFQKLRrDMEEATLHFEATSASLKKrhadslaeLEGQVENLQ--QVKQKLEKDR 1275
Cdd:COG3096 434 LTpENAEDYLAAFRAKEqQATEEVLELEQKLS-VADAARRQFEKAYELVCK--------IAGEVERSQawQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1276 SDLQLevddLLTRIEQMTRAKANAEKLctlyEERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQL 1355
Cdd:COG3096 505 RSQQA----LAQRLQQLRAQLAELEQR----LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEA 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1356 SREKSNFTRQIEELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQwrmkyENNVIQ 1435
Cdd:COG3096 577 VEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVE-----RDELAA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1436 KTEDLEDAKKELA-------IRLQETAEAMG----------------------VANARNA----SLERARHRLQlELGDA 1482
Cdd:COG3096 652 RKQALESQIERLSqpggaedPRLLALAERLGgvllseiyddvtledapyfsalYGPARHAivvpDLSAVKEQLA-GLEDC 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1483 LSDL----GKVRSAAARLDQKQLQSGKALADWKQ------KHEESQTLLDASR-KEIQALSTELLKLKHAYKESIVGQET 1551
Cdd:COG3096 731 PEDLylieGDPDSFDDSVFDAEELEDAVVVKLSDrqwrysRFPEVPLFGRAAReKRLEELRAERDELAEQYAKASFDVQK 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1552 LRRENKNLQEEISNLTNQVREGtknltEMEKVKKLIEQEKTEVQVTLEETEGALERneskiLRFQLELLKAKAELERKLS 1631
Cdd:COG3096 811 LQRLHQAFSQFVGGHLAVAFAP-----DPEAELAALRQRRSELERELAQHRAQEQQ-----LRQQLDQLKEQLQLLNKLL 880
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1632 E-----KDEELENFRRkqqctidsmqsSLDSEAKSRIEATRLKKKMEEDLNEMELQLSCANR---QVSEATKSLGQLQIQ 1703
Cdd:COG3096 881 PqanllADETLADRLE-----------ELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSdpeQFEQLQADYLQAKEQ 949
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1704 IKDLQMQLDDSTQlnsdlkeqvaVAERR--------NSLL--QSEL-EDLRSLQEQTERGRRLSEEELLEATERinlfYT 1772
Cdd:COG3096 950 QRRLKQQIFALSE----------VVQRRphfsyedaVGLLgeNSDLnEKLRARLEQAEEARREAREQLRQAQAQ----YS 1015
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1773 QNTSLLSQKKKLEADVAQMQKEAEEVVQE--CQNAEEKAKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDLQKR 1850
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQQTLQELEQELEElgVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKR 1095
|
....*.
gi 1411134203 1851 LAEAEQ 1856
Cdd:COG3096 1096 LRKAER 1101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1591-1965 |
7.02e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1591 KTEVQVTLEETEGALERNESKILRF-QLELLKAKAELERKLSEKDEELENF---RRKQQCTIDSMQSSLDSEAKSRIEAT 1666
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKeEKDLHERLNGLESELAELDEEIERYeeqREQARETRDEADEVLEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1667 RLK---KKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDL--QMQLDDStqlnsdlkEQVAVAERRnsllqselED 1741
Cdd:PRK02224 255 TLEaeiEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDA--------DAEAVEARR--------EE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1742 LRSLQEQTErgrrlseEELLEATERINLFYTQNTSLLSQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSE 1821
Cdd:PRK02224 319 LEDRDEELR-------DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1822 ELKKKQDTIA-----------HLEKTREN----------MEQTITDLQKRLAEAEQ--------------------TALM 1860
Cdd:PRK02224 392 EIEELRERFGdapvdlgnaedFLEELREErdelrereaeLEATLRTARERVEEAEAlleagkcpecgqpvegsphvETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1861 GSRKQIQKLESR---VRELEGELEGEIRRSAEAQRGARRLERC----------IKELTYQAEEDKKNLSRMQTQMDKLQL 1927
Cdd:PRK02224 472 EDRERVEELEAEledLEEEVEEVEERLERAEDLVEAEDRIERLeerredleelIAERRETIEEKRERAEELRERAAELEA 551
|
410 420 430
....*....|....*....|....*....|....*...
gi 1411134203 1928 KVHNYKQQVEVAEAQANQYLSKYKKQQHELNEVKERAE 1965
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1779-2010 |
7.37e-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: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1779 SQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAE----- 1853
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElrael 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1854 AEQTALMGsrKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVHNYK 1933
Cdd:COG4942 100 EAQKEELA--ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411134203 1934 QQVEVAEAQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVRQAQTELLVTLQGSKRIVSPALKGQ 2010
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1369-1769 |
7.78e-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: 54.57 E-value: 7.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1369 LRGQLEKETKSQSALAhaLQKAQRDCdllREQYEEEQEVKAELHRTLSKVNA----------------EMVQWRMKYENN 1432
Cdd:COG3096 274 MRHANERRELSERALE--LRRELFGA---RRQLAEEQYRLVEMARELEELSAresdleqdyqaasdhlNLVQTALRQQEK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1433 VIQKTEDLEdakkELAIRLqetAEAMGVANARNASLERARHRLQlelgdalsdlgkvrsaAARLDQKQLQSGkaLADWKQ 1512
Cdd:COG3096 349 IERYQEDLE----ELTERL---EEQEEVVEEAAEQLAEAEARLE----------------AAEEEVDSLKSQ--LADYQQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1513 KHEESQTLLDASRKEIQAL--STELLKLKHAYKESIVG-QETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQ 1589
Cdd:COG3096 404 ALDVQQTRAIQYQQAVQALekARALCGLPDLTPENAEDyLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1590 EKTEVqvtleETEGALERNESKILRF-QLELLKAKAE-LERKLSEKDEELENFRRKQQcTIDSMQSSLDSEAKSRIEATR 1667
Cdd:COG3096 484 IAGEV-----ERSQAWQTARELLRRYrSQQALAQRLQqLRAQLAELEQRLRQQQNAER-LLEEFCQRIGQQLDAAEELEE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1668 LKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQ----LDDSTQLNSdLKEQVAVAerrnsllqseLEDLR 1743
Cdd:COG3096 558 LLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawLAAQDALER-LREQSGEA----------LADSQ 626
|
410 420 430
....*....|....*....|....*....|..
gi 1411134203 1744 SLQE------QTERGRRLSEEELLEATERINL 1769
Cdd:COG3096 627 EVTAamqqllEREREATVERDELAARKQALES 658
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1576-1790 |
1.01e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1576 NLTEMEKVKKLIEQEKTEVQVTLEETEGALE--RNESKILRFQLE---LLKAKAELERKLSEKDEELENFRRKqqctIDS 1650
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEaklLLQQLSELESQLAEARAELAEAEAR----LAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1651 MQSSLDS--EAKSRIEATRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQ-LNSDLKEQVAV 1727
Cdd:COG3206 245 LRAQLGSgpDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQrILASLEAELEA 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411134203 1728 AERRNSLLQSELEDLRS-LQEQTERGRRLSE-EELLEATERInlfYTQntsLLSQKKKLEADVAQ 1790
Cdd:COG3206 325 LQAREASLQAQLAQLEArLAELPELEAELRRlEREVEVAREL---YES---LLQRLEEARLAEAL 383
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1188-1421 |
1.26e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1188 KERADLTQDLADLNERLEEVggasLAQLEITKKQETKFQKLRRDMEEATLHFEATSASLKKRhadsLAELEGQVENLQQV 1267
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRIRALEQE----LAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1268 KQKLEKDRSDLQLEVDDLLTRIEQMTRakaNAEKLCTLYEERLNEANAKLDKVTQLANDLAAQKTELWSEsgefLRRLEE 1347
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGR---QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411134203 1348 KEALINQLSREKSNFTRQIEELRGQLEKETKSQSALahaLQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAE 1421
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1367-1748 |
1.28e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.76 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1367 EELRGQLEKETKS------QSALAHALQKAQRDCDLLREQYEEEQEVKAELH---RTLSKVNAEMVqwRMKYENNVIQKT 1437
Cdd:PRK11281 39 ADVQAQLDALNKQklleaeDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAqapAKLRQAQAELE--ALKDDNDEETRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1438 -------EDLEDAKKELAIRLQETAEAMGVANARNASLERARHRLQLELGdalsdlgkvrSAAARLDQ--KQLQSGKA-- 1506
Cdd:PRK11281 117 tlstlslRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALY----------ANSQRLQQirNLLKGGKVgg 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1507 ---LADWKQKHEESQTLLDAS----RKEIQALS--TELLKLKHAYKESIVGQetLRRENKNLQEEISNltnqvregtKNL 1577
Cdd:PRK11281 187 kalRPSQRVLLQAEQALLNAQndlqRKSLEGNTqlQDLLQKQRDYLTARIQR--LEHQLQLLQEAINS---------KRL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1578 TEMEK-VKKLIEQEKTevqvtleeteGALERNEskilrfqleLLKAKAELERKLSEKdeelenfrrkqqctidsmqssld 1656
Cdd:PRK11281 256 TLSEKtVQEAQSQDEA----------ARIQANP---------LVAQELEINLQLSQR----------------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1657 seaksRIEATrlkkkmeEDLNEmelqlscanrqvseatksLGQLQIQIKDlqmQLDDSTQLNSDLKEQVAVAerRNSLLQ 1736
Cdd:PRK11281 294 -----LLKAT-------EKLNT------------------LTQQNLRVKN---WLDRLTQSERNIKEQISVL--KGSLLL 338
|
410
....*....|..
gi 1411134203 1737 SeledlRSLQEQ 1748
Cdd:PRK11281 339 S-----RILYQQ 345
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1016-1222 |
1.32e-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: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1016 VKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQE 1095
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1096 RKARINCERELHKLE--------GDLKLNQESMENLESSQRHLAEELRKKELENSQMNSKVENEKglvAQLQKMVKELQT 1167
Cdd:COG3883 92 ARALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL---AELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1411134203 1168 QIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVGGASLAQLEITKKQE 1222
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1252-1645 |
1.41e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1252 DSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRAKANAEklctlYEERLNEANAKLDkvtqlandlaaqk 1331
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-----LYQELEALEAELA------------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1332 telwsESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSALAH-ALQKAQRDCDLLREQYEEEQEVKAE 1410
Cdd:COG4717 143 -----ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1411 LHRTLSKVNAEMVQWRMKYENNVIQKTED--------------LEDAKKELAIRLQETAEAMGVANA---------RNAS 1467
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKearlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGllallflllAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1468 LERARHRLQLELGDALSDLG--KVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRK-----EIQALSTELLKLKH 1540
Cdd:COG4717 298 ASLGKEAEELQALPALEELEeeELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEleeelQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1541 AYK----ESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMekvkkLIEQEKTEVQVTLEETEGALERNESKILRFQ 1616
Cdd:COG4717 378 EAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL-----LEALDEEELEEELEELEEELEELEEELEELR 452
|
410 420
....*....|....*....|....*....
gi 1411134203 1617 LELLKAKAELERKlsEKDEELENFRRKQQ 1645
Cdd:COG4717 453 EELAELEAELEQL--EEDGELAELLQELE 479
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
907-1540 |
1.61e-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: 53.43 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 907 KEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQcEWLIKSKIQLEARVKELSERVEEEEEI 986
Cdd:TIGR00618 292 AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-RRLLQTLHSQEIHIRDAHEVATSIREI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 987 NS---ELTARGRKLEDEcselkKEIDDLETMLVKSEKEKRTTE-HKVKNLTEEVEFLNEDISKLN-------RAAKVVQE 1055
Cdd:TIGR00618 371 SCqqhTLTQHIHTLQQQ-----KTTLTQKLQSLCKELDILQREqATIDTRTSAFRDLQGQLAHAKkqqelqqRYAELCAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1056 AHQQTLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQerkarincERELHKLEGDLKLNQESMEN-LESSQRHLAEEL 1134
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ--------ETRKKAVVLARLLELQEEPCpLCGSCIHPNPAR 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1135 rkKELENSQMNSKvenekgLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVGgaslAQ 1214
Cdd:TIGR00618 518 --QDIDNPGPLTR------RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK----ED 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1215 LEITKKQETKFQKL--RRDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEvddlLTRIEQM 1292
Cdd:TIGR00618 586 IPNLQNITVRLQDLteKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT----LTQERVR 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1293 TRAKANAEKLCTLYEERLNEANAKLDKVTQLANDLaaqktELWSESGEFLRRLEEKEALINQLSREKSNFTR-QIEELRG 1371
Cdd:TIGR00618 662 EHALSIRVLPKELLASRQLALQKMQSEKEQLTYWK-----EMLAQCQTLLRELETHIEEYDREFNEIENASSsLGSDLAA 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1372 QLEketksqsALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQKTEDLEDAKKELAIRL 1451
Cdd:TIGR00618 737 RED-------ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIG 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1452 QETAEAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQAL 1531
Cdd:TIGR00618 810 QEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFD 889
|
....*....
gi 1411134203 1532 STELLKLKH 1540
Cdd:TIGR00618 890 GDALIKFLH 898
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1241-1471 |
2.21e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1241 ATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRAKANAEKLCTLYEERLNEANAKLDKV 1320
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1321 TQLA--NDLAAQKTELWSES---GEFLRRLEekeaLINQLSREKSNFTRQIEELRGQLEKEtksQSALAHALQKAQRDCD 1395
Cdd:COG3883 92 ARALyrSGGSVSYLDVLLGSesfSDFLDRLS----ALSKIADADADLLEELKADKAELEAK---KAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411134203 1396 LLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQKTEDLEDAKKELAIRLQETAEAMGVANARNASLERA 1471
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1268-1847 |
3.27e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1268 KQKLEKDRSDLQLEVDDLLTRIEQMTRAKANAEKLctlyEERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEE 1347
Cdd:TIGR04523 95 KDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKL----EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1348 KEALINQLSREKSNFTRQIEELRGQLEKETKSQSALahalQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRM 1427
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNL----KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1428 KYeNNVIQKTEDLEDAKKELAIRLQETAEAMGVANARNASLERARHRLQLELGD----ALSDLGK-VRSAAARLDQKQLQ 1502
Cdd:TIGR04523 247 EI-SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlnnqKEQDWNKeLKSELKNQEKKLEE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1503 SGKALADWKQKHEESQTLLDASRKEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEK 1582
Cdd:TIGR04523 326 IQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1583 VKKLIEQEktevqvtLEETEGALERNESKILRFQLELLKAKAELERkLSEKDEELENFRRKQQCTIDSMQSSLdseaksr 1662
Cdd:TIGR04523 406 LNQQKDEQ-------IKKLQQEKELLEKEIERLKETIIKNNSEIKD-LTNQDSVKELIIKNLDNTRESLETQL------- 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1663 ieatrlkKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDL 1742
Cdd:TIGR04523 471 -------KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1743 RS--LQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVAQMQ---------------------------- 1792
Cdd:TIGR04523 544 EDelNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEkekkdlikeieekekkisslekelekak 623
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1411134203 1793 KEAEEVVQECQNaeekakkAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDL 1847
Cdd:TIGR04523 624 KENEKLSSIIKN-------IKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1251-1495 |
4.56e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1251 ADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRAKANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQ 1330
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1331 KTELWSESGEFLR---RLEEKEALINQLSREKSNftrQIEELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEV 1407
Cdd:COG4942 99 LEAQKEELAELLRalyRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1408 KAELhrtlskvnaemvqwrmkyENNVIQKTEDLEDAKKELAIRLQETAEAMGVANARNASLERARHRLQlelgDALSDLG 1487
Cdd:COG4942 176 LEAL------------------LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE----ALIARLE 233
|
....*...
gi 1411134203 1488 KVRSAAAR 1495
Cdd:COG4942 234 AEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1342-1797 |
4.94e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1342 LRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSALAHALQKAQRDCDL--LREQYEEEQEVKAELHRTLSKVN 1419
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1420 AEMVQWRMKyENNVIQKTEDLEDAKKELAI----RLQETAEAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAAR 1495
Cdd:COG4717 160 ELEEELEEL-EAELAELQEELEELLEQLSLateeELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1496 LDQKQlqsgkaladwKQKHEESQTLLDASRKEIQALSTELLKLKHAYKESIVGQETLrrenknLQEEISNLTNQVREGTK 1575
Cdd:COG4717 239 AALEE----------RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL------LALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1576 NLTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKILRFqLELLKAKAELERKLSEKDEEL--ENFRRKQQCTIDSMQS 1653
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLEL-LDRIEELQELLREAEELEEELqlEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1654 SLDSEAKSRIEATRLKKKMEEDLNEMELQLSCANRQVSE--ATKSLGQLQIQIKDLQMQLDdstqlnsdlkeqvAVAERR 1731
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELE-------------ELEEEL 448
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411134203 1732 NSLLQsELEDLRSLQEQTERGRRLSE--EELLEATERINLFYTQNTSLlsqkKKLEADVAQMQKEAEE 1797
Cdd:COG4717 449 EELRE-ELAELEAELEQLEEDGELAEllQELEELKAELRELAEEWAAL----KLALELLEEAREEYRE 511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1447-1666 |
5.16e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1447 LAIRLQETAEAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRK 1526
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1527 EIQALSTELLKLKHAYKESIVGQETLRREN------------------KNLQEEISNLTNQVREGTKNLTEMEKVKKLIE 1588
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPplalllspedfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411134203 1589 QEKTEVQVTLEETEGALERNESKILRFQLELlkakAELERKLSEKDEELENFRRKQQcTIDSMQSSLDSEAKSRIEAT 1666
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLL----ARLEKELAELAAELAELQQEAE-ELEALIARLEAEAAAAAERT 243
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1365-1974 |
6.84e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1365 QIEELRGQLE-KETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRmkyennviQKTEDLEDA 1443
Cdd:PRK02224 188 SLDQLKAQIEeKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR--------EELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1444 KKELAIRLQETAEAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQlqsgkalADWKQKHEESQTLLDA 1523
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARR-------EELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1524 SRKEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEG 1603
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1604 ALE--RNESKILRFQLELLKAKAELERKLSEKDEELENFRRKQQCTidsmQSSLDSEAKSRIEATRLKK-KMEEDLNEME 1680
Cdd:PRK02224 413 FLEelREERDELREREAELEATLRTARERVEEAEALLEAGKCPECG----QPVEGSPHVETIEEDRERVeELEAELEDLE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1681 LQLSCANRQVSEAtKSLGQLQIQIKDLQMQLDDSTQLnsdlkeqvaVAERRNSLlqseledlrslQEQTERGRRLSEEel 1760
Cdd:PRK02224 489 EEVEEVEERLERA-EDLVEAEDRIERLEERREDLEEL---------IAERRETI-----------EEKRERAEELRER-- 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1761 leaterinlfytqntsllsqKKKLEADVAQMQKEAEEvvqecqnaeekakkAATEAANLSEELKKKQDTIAHLEKTRENM 1840
Cdd:PRK02224 546 --------------------AAELEAEAEEKREAAAE--------------AEEEAEEAREEVAELNSKLAELKERIESL 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1841 EqTITDLQKRLAEAEQT--ALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGAR----RLERCIKElTYQAEEDKKn 1914
Cdd:PRK02224 592 E-RIRTLLAAIADAEDEieRLREKREALAELNDERRERLAEKRERKRELEAEFDEARieeaREDKERAE-EYLEQVEEK- 668
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1915 LSRMQTQMDKLQLKVHNYKQQVEvaeaqanqylskykkqqhELNEVKERAEVAESQVNKL 1974
Cdd:PRK02224 669 LDELREERDDLQAEIGAVENELE------------------ELEELRERREALENRVEAL 710
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
941-1185 |
7.76e-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: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 941 LILQLQAEQETLANVEEQcewLIKSKIQLEARVKELSERVEEEEEINSELtargRKLEDECSELKKEIDDLETMLVKSEK 1020
Cdd:COG4942 11 LALAAAAQADAAAEAEAE---LEQLQQEIAELEKELAALKKEEKALLKQL----AALERRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1021 EKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEA-------HQQTLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALE 1093
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1094 QERKARINCERELHKLEGDLKLNQESMENLESSQRHLAEELRKKELENSQMNSKVENEKglvAQLQKMVKELQTQIKDLK 1173
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA---EELEALIARLEAEAAAAA 240
|
250
....*....|..
gi 1411134203 1174 EKLEAERTTRAK 1185
Cdd:COG4942 241 ERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1291-1524 |
8.32e-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: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1291 QMTRAKANAEKLCTLyEERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELR 1370
Cdd:COG4942 18 QADAAAEAEAELEQL-QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1371 GQLEKETKSQSALAHALQKAQRDCD---LLREQYEEEQEVKAELHRTLSKVNAEMVQwrmkyenNVIQKTEDLEDAKKEL 1447
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPlalLLSPEDFLDAVRRLQYLKYLAPARREQAE-------ELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411134203 1448 AIRLQETAEAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDAS 1524
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1307-1530 |
9.16e-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: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1307 EERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSALAHA 1386
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1387 LQKaqrdcdLLREQYEEEQEVKAELhrTLSKVNAEMVQWRMKYENNVIQ----KTEDLEDAKKELAIRLQETAEAMGVAN 1462
Cdd:COG4942 106 LAE------LLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAParreQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411134203 1463 ARNASLERARHRLQlelgdalSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQA 1530
Cdd:COG4942 178 ALLAELEEERAALE-------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
995-1318 |
9.77e-06 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 50.62 E-value: 9.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 995 RKLEDECSELKKEIDDLETMLVKS---------EKEKRTTEHKVKN------LTEEVEFLNEDISKLNRAAKVVQEAHQQ 1059
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPselalnemiEKLKKEIDLEYTEaviamgLQERLENLREEFSKANSQDQLMHPVLME 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1060 TLDDLHMEEEKLSSLSKANLKLEQQVvgleGALEQERKARINCERELHKLEGDLKLNQESMENLESSQRHLAEELRKKEL 1139
Cdd:PLN03229 512 KIEKLKDEFNKRLSRAPNYLSLKYKL----DMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIKEKMEALKAEV 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1140 ENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEK--LEAERTTRAKMEKERADLTQDLADLNERLEEvggaslaqlEI 1217
Cdd:PLN03229 588 ASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSmgLEVIGVTKKNKDTAEQTPPPNLQEKIESLNE---------EI 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1218 TKKQE--TKFQKLRRDMEEATLHFEATSASLKKRHADSLAELEgqvenlQQVKQKLEK--DRSDLQLEVDDLltRIEQMT 1293
Cdd:PLN03229 659 NKKIErvIRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALE------QQIKQKIAEalNSSELKEKFEEL--EAELAA 730
|
330 340
....*....|....*....|....*
gi 1411134203 1294 RAKANAEKLCTLYEERLNEANAKLD 1318
Cdd:PLN03229 731 ARETAAESNGSLKNDDDKEEDSKED 755
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
902-1236 |
1.02e-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: 50.88 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 902 EIAGLKEECAQLQKAL-EKSEFQR--EELKAKQvsltqekNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSE 978
Cdd:pfam05483 406 ELEELKKILAEDEKLLdEKKQFEKiaEELKGKE-------QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKT 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 979 RVEEEEEINSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQ 1058
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFI 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1059 QTLDD----LHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEG-------------------DLKL 1115
Cdd:pfam05483 559 QKGDEvkckLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQenkalkkkgsaenkqlnayEIKV 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1116 NQESMEnLESSQRHLAE-------ELRKKELENSQMNSKVENEKGLVAQLQKMVKEL----QTQIKDLKEKLEAERTTRA 1184
Cdd:pfam05483 639 NKLELE-LASAKQKFEEiidnyqkEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIdkrcQHKIAEMVALMEKHKHQYD 717
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1185 KMEKER------------------ADLTQDLADLNERLEEVGgaslAQLEITKKQEtkfQKLRRDMEEAT 1236
Cdd:pfam05483 718 KIIEERdselglyknkeqeqssakAALEIELSNIKAELLSLK----KQLEIEKEEK---EKLKMEAKENT 780
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1155-1476 |
1.18e-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: 50.51 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1155 VAQLQKMVKELQTQIKdlKEKLEAERTTRAKMEKERAdltqdlADLNERLEEVGGASLAQLEitkKQETKFQKLRRDMEE 1234
Cdd:pfam17380 277 IVQHQKAVSERQQQEK--FEKMEQERLRQEKEEKARE------VERRRKLEEAEKARQAEMD---RQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1235 ATLHFEATSASLKKRHADSLAELEGQVEnlqqVKQKLEKDRsdLQLEVDDLLTRIEQMTRAkanAEKLCTLYEERLNean 1314
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEIAME----ISRMRELER--LQMERQQKNERVRQELEA---ARKVKILEEERQR--- 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1315 akldKVTQLANDLAAQKTELWSESGEFLRRLEEKEAL-INQLSREKSNFTRQIEELRGQLEKETKSQSalahALQKAQRD 1393
Cdd:pfam17380 414 ----KIQQQKVEMEQIRAEQEEARQREVRRLEEERAReMERVRLEEQERQQQVERLRQQEEERKRKKL----ELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1394 CDLLREQYEE--EQEVKAELHRTLSKVNA-EMVQWRMKYENNVI----QKTEDLEDAKKELAI----RLQETAEAMGVAN 1462
Cdd:pfam17380 486 RKRAEEQRRKilEKELEERKQAMIEEERKrKLLEKEMEERQKAIyeeeRRREAEEERRKQQEMeerrRIQEQMRKATEER 565
|
330
....*....|....
gi 1411134203 1463 ARNASLERARHRLQ 1476
Cdd:pfam17380 566 SRLEAMEREREMMR 579
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1072-1369 |
1.31e-05 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 50.24 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1072 SSLSKANLKLEQQVVGLEGAleQERKARINCerelhkLEGDLKLNQESMENLESSQRHLAEEL---RKKELE-NSQMNSK 1147
Cdd:pfam09726 357 SSSSSKNSKKQKGPGGKSGA--RHKDPAENC------IPNNQLSKPDALVRLEQDIKKLKAELqasRQTEQElRSQISSL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1148 VENEKGL---VAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEvggaslaqleitkkqetk 1224
Cdd:pfam09726 429 TSLERSLkseLGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQEARASAEKQLAE------------------ 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1225 fQKLRRDMEEATL-HFEATSASLKKRHADSLAELEGQVENlqqVKQKLEKDRSDLQLEVDDLLTRIEQMTRAKANAEKLC 1303
Cdd:pfam09726 491 -EKKRKKEEEATAaRAVALAAASRGECTESLKQRKRELES---EIKKLTHDIKLKEEQIRELEIKVQELRKYKESEKDTE 566
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411134203 1304 TLyeerLNEANAKLDKVTQLANDLAAQ---KTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEEL 1369
Cdd:pfam09726 567 VL----MSALSAMQDKNQHLENSLSAEtriKLDLFSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEV 631
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1466-1967 |
1.41e-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: 50.21 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1466 ASLERARHRLQLELgDALSDLGKVRSAAARLDQKQLQSGKALADW-KQKHEESQTLLDASRKEIQALSTELLKLKHAY-- 1542
Cdd:pfam10174 243 SSLERNIRDLEDEV-QMLKTNGLLHTEDREEEIKQMEVYKSHSKFmKNKIDQLKQELSKKESELLALQTKLETLTNQNsd 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1543 --------KESIVGQEtlRRENKnLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKILR 1614
Cdd:pfam10174 322 ckqhievlKESLTAKE--QRAAI-LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1615 FQlellKAKAELERKLSEKDEELENFRRKQQctidSMQSslDSEAKSRIEATrlkkkMEEDLNEMElqlscanrQVSEAT 1694
Cdd:pfam10174 399 LQ----KKIENLQEQLRDKDKQLAGLKERVK----SLQT--DSSNTDTALTT-----LEEALSEKE--------RIIERL 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1695 KSlgQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSlQEQTERGRRLSEEELLEATErINLfytqn 1774
Cdd:pfam10174 456 KE--QREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKE-HASSLASSGLKKDSKLKSLE-IAV----- 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1775 tsllsQKKKLEAD--VAQMQK--EAEEVVQECQNAEEKAKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDLQKR 1850
Cdd:pfam10174 527 -----EQKKEECSklENQLKKahNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKK 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1851 LAEAEQTALmgsrKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKE--LTYQAEEDKKNLSRMQTQMDKLQLK 1928
Cdd:pfam10174 602 IAELESLTL----RQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADnsQQLQLEELMGALEKTRQELDATKAR 677
|
490 500 510
....*....|....*....|....*....|....*....
gi 1411134203 1929 VHNYKQQVEVAEAQANQYLSKYKKQQHELNEVKERAEVA 1967
Cdd:pfam10174 678 LSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLA 716
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1520-1968 |
1.50e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1520 LLDASRKEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLE 1599
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1600 etegalerneskilrfQLELLKAKAELERKLSEKDEELENFRRKQQctidsmqssldseakSRIEATRLKKKMEEDLNEM 1679
Cdd:COG4717 127 ----------------LLPLYQELEALEAELAELPERLEELEERLE---------------ELRELEEELEELEAELAEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1680 ELQLSCANRQVSEATKSlgqlqiQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEE 1759
Cdd:COG4717 176 QEELEELLEQLSLATEE------ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEAR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1760 -LLEATERINLFYTQNTSLLSQKKKLEA-----------DVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKK-- 1825
Cdd:COG4717 250 lLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlg 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1826 --KQDTIAHLEKTRENMEQTITDLQKRLAEAEQTALMGSRKQIQKLesrVRELEGELEGEIRRSAEAQRGARRLERCIKE 1903
Cdd:COG4717 330 lpPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEE 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411134203 1904 LTYQAEEDKKNLSRMQTQMDK--LQLKVHNYKQQVEVAEAQANQYLSKYKKQQHELNEVKERAEVAE 1968
Cdd:COG4717 407 LEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1512-1731 |
1.53e-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: 49.38 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1512 QKHEESQTLLDASRKEIQALSTELLKLKHAykesivgQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEK 1591
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1592 TEVQVTLEETEGALERNESKILRF----QLELLKAKAELER--KLSEKDEELENFRRKQqctIDSMQSSLDSEAKSRIEA 1665
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLgrqpPLALLLSPEDFLDavRRLQYLKYLAPARREQ---AEELRADLAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411134203 1666 TRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERR 1731
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1273-1989 |
1.67e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.05 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1273 KDRSDLQLEVDDLLTRIEQMTRAKANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALI 1352
Cdd:TIGR00606 172 KQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1353 NQLSREKSNFTRQIEelrgqLEKETKSQSALAHALQKAQRDCDLLREQY-----EEEQEVKAELHRTLSKVNAEMVQWRM 1427
Cdd:TIGR00606 252 NRLKEIEHNLSKIMK-----LDNEIKALKSRKKQMEKDNSELELKMEKVfqgtdEQLNDLYHNHQRTVREKERELVDCQR 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1428 KYENNViQKTEDLEDAKKELAI---RLQETAEAMGvANARNASLERARHRLQLELG----DALSDL---GKVRSAAARLD 1497
Cdd:TIGR00606 327 ELEKLN-KERRLLNQEKTELLVeqgRLQLQADRHQ-EHIRARDSLIQSLATRLELDgferGPFSERqikNFHTLVIERQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1498 QKQLQSGKALADWKQKHEESQTLLDASRKEIQALStellklkhaykesivgqETLRRENKNLQEEISNLTNQVREGTKNL 1577
Cdd:TIGR00606 405 DEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLG-----------------RTIELKKEILEKKQEELKFVIKELQQLE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1578 TEMEKVKKLIEQ-EKTEVQVTLEETEGALE---RNESKILRFQLELLKAKAELERKLSEKDEELENFRRKQQCTIDSM-- 1651
Cdd:TIGR00606 468 GSSDRILELDQElRKAERELSKAEKNSLTEtlkKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMdk 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1652 -QSSLDSEAKSRIEATRL------KKKMEE-------DLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLddsTQL 1717
Cdd:TIGR00606 548 dEQIRKIKSRHSDELTSLlgyfpnKKQLEDwlhskskEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQL---SSY 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1718 NSDLKEQVAVaerrnsllQSELEDLRSLQEQTERGRRlSEEELLEATERINLFYTQNTSLLSQKKKLEADVAQMQKEAEE 1797
Cdd:TIGR00606 625 EDKLFDVCGS--------QDEESDLERLKEEIEKSSK-QRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQE 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1798 VVQECQNAEEKAKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQTAlmgsRKQIQKLESRVrELE 1877
Cdd:TIGR00606 696 FISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV----NRDIQRLKNDI-EEQ 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1878 GELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMD--KLQLKVHNYKQQVEVAEAQANQYLSKYKKQQH 1955
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
730 740 750
....*....|....*....|....*....|....
gi 1411134203 1956 ELNEVKERAEVAESQVNKLKIKAREFGKKVRQAQ 1989
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQ 884
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1665-1858 |
1.68e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1665 ATRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELED-LR 1743
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1744 SLQEQterGRRLSE-EELLEAT---------ERINLFYTQNTSLL-----------SQKKKLEADVAQMQKEAEEVVQEC 1802
Cdd:COG3883 94 ALYRS---GGSVSYlDVLLGSEsfsdfldrlSALSKIADADADLLeelkadkaeleAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1411134203 1803 QNAEEKAKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQTA 1858
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1055-1227 |
1.78e-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: 48.38 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1055 EAHQQTLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMENLESsqrhlaeel 1134
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1135 RKKELENSQMNskVENEKGL------VAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVG 1208
Cdd:COG1579 74 RIKKYEEQLGN--VRNNKEYealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170
....*....|....*....
gi 1411134203 1209 GASLAQLEITKKQETKFQK 1227
Cdd:COG1579 152 AELEAELEELEAEREELAA 170
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1557-1974 |
1.91e-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: 49.82 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1557 KNLQEEISNLTNQVREGTKNLTEMEKvkkLIEQEKTEVQVTLEE----TEGALERNESKILRFQLELLKAK-AELERKLS 1631
Cdd:pfam10174 174 KKSGEEDWERTRRIAEAEMQLGHLEV---LLDQKEKENIHLREElhrrNQLQPDPAKTKALQTVIEMKDTKiSSLERNIR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1632 EKDEELENFRRKQQCTIDSMQSSLDSEAKSRIEATRLKKKMEEDLNEMelqlscaNRQVSEatksLGQLQIQIKDLQMQL 1711
Cdd:pfam10174 251 DLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQEL-------SKKESE----LLALQTKLETLTNQN 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1712 DDSTQLNSDLKEQVAVAERRNSLLQSELEDLRS--------LQEQTERGRRLSEE------------ELLEATER-INLF 1770
Cdd:pfam10174 320 SDCKQHIEVLKESLTAKEQRAAILQTEVDALRLrleekesfLNKKTKQLQDLTEEkstlageirdlkDMLDVKERkINVL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1771 YTQNTSLLSQKKKLEADVAQMQKEAEEVVQECQNaeekakkAATEAANLSEELKKKQDTIAHLEKTRENMEQT----ITD 1846
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSN-------TDTALTTLEEALSEKERIIERLKEQREREDRErleeLES 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1847 LQKRLAEAEQTaLMGSRKQIQKLESRVRELEGelegeiRRSAEAQRGARRLERcIKELTYQAEEDKKNLSRMQTQMDKlq 1926
Cdd:pfam10174 473 LKKENKDLKEK-VSALQPELTEKESSLIDLKE------HASSLASSGLKKDSK-LKSLEIAVEQKKEECSKLENQLKK-- 542
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1411134203 1927 lkvhnyKQQVEVAEAQANQYLSKYKKQQHELNEVKERAEVAESQVNKL 1974
Cdd:pfam10174 543 ------AHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERL 584
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1624-1858 |
2.08e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1624 AELERKLSEKDEELENFRRKQQctidsmQSSLDSEAKSRIEatrlkkkmeedlnemelQLSCANRQVSEATKSLGQLQIQ 1703
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNG------LVDLSEEAKLLLQ-----------------QLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1704 IKDLQMQLDDSTQLNSDLKEQVAVAERRNSL--LQSELEDLRS-----------LQEQTERGRRLSEEELLEATERINlf 1770
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQLRAQLaeLEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRILASLE-- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1771 yTQNTSLLSQKKKLEADVAQMQKEAeevvqecqnaeekakkaateaanlsEELKKKQDTIAHLEKTRENMEQTITDLQKR 1850
Cdd:COG3206 320 -AELEALQAREASLQAQLAQLEARL-------------------------AELPELEAELRRLEREVEVARELYESLLQR 373
|
....*...
gi 1411134203 1851 LAEAEQTA 1858
Cdd:COG3206 374 LEEARLAE 381
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1549-1784 |
2.24e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1549 QETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKILRFQLELlkakAELER 1628
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI----AELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1629 KLSEKDEELEN-----FRRKQQCTIDSMQSSLDSEAKSRIEA--TRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQ 1701
Cdd:COG4942 98 ELEAQKEELAEllralYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1702 IQIKDLQMQLddsTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEelLEATERINLFYTQNTSLLSQK 1781
Cdd:COG4942 178 ALLAELEEER---AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR--LEAEAAAAAERTPAAGFAALK 252
|
...
gi 1411134203 1782 KKL 1784
Cdd:COG4942 253 GKL 255
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
638-729 |
2.58e-05 |
|
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: 46.57 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 638 GVVPY---NISGWLEKNKDLLNETVVAVFQKSSNRLLAslfenymstdsAIPFGEKKRKKGTSFQTAAS----------- 703
Cdd:cd01363 71 GVIPYlasVAFNGINKGETEGWVYLTEITVTLEDQILQ-----------ANPILEAFGNAKTTRNENSSrfgkfieilld 139
|
90 100 110
....*....|....*....|....*....|.
gi 1411134203 704 -----LHKENLNKLMTNLKSTAPHFVRCINP 729
Cdd:cd01363 140 iagfeIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
826-1179 |
2.93e-05 |
|
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: 49.28 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 826 QLEAMRDERLSKVFTLFQARAQGKLMRIKFQKILEER----DALILIQWNIRAFMAVKNWAWMRLffkIKPLVKSSERGE 901
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqleERIAQLSKELTELEAEIEELEERL---EEAEEELAEAEA 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 902 EIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSERVe 981
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI- 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 982 eeeeinSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTL 1061
Cdd:TIGR02168 862 ------EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1062 DDLHMEEEKLSSLSKANLK-LEQQVVGLEGALEQerkarinCERELHKLEGDLK----LNQESMENLEssqrhlAEELRK 1136
Cdd:TIGR02168 936 VRIDNLQERLSEEYSLTLEeAEALENKIEDDEEE-------ARRRLKRLENKIKelgpVNLAAIEEYE------ELKERY 1002
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1411134203 1137 KELeNSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAE 1179
Cdd:TIGR02168 1003 DFL-TAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNEN 1044
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1123-1534 |
3.12e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1123 LESSQRHLAEELRKKELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERadltQDLADLNE 1202
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKY----KELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1203 RLEEVGGASLAQleitkkQETKFQKLRrdmeeatlHFEATSASLKKRHADSLAELE---GQVENLQQVKQKLEKDRSDLQ 1279
Cdd:pfam07888 112 ELSEEKDALLAQ------RAAHEARIR--------ELEEDIKTLTQRVLERETELErmkERAKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1280 LevdDLLTRIEQMTRAKANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQKtelwsesgeflRRLEEKEALINQLS--R 1357
Cdd:pfam07888 178 A---KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH-----------RKEAENEALLEELRslQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1358 EKSNFTRQIEELRGQLEKETKSQSALAHA------LQKAQRDCDL--LREQYEEEQEVKAELHRTLSKvNAEMVQWRMKY 1429
Cdd:pfam07888 244 ERLNASERKVEGLGEELSSMAAQRDRTQAelhqarLQAAQLTLQLadASLALREGRARWAQERETLQQ-SAEADKDRIEK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1430 ENNVIQKTEDledakkelaiRLQEtaeamgvanarnaslERA-RHRLQLELGDAlSDLGKVRSAAARLDQKQLQSGKALA 1508
Cdd:pfam07888 323 LSAELQRLEE----------RLQE---------------ERMeREKLEVELGRE-KDCNRVQLSESRRELQELKASLRVA 376
|
410 420
....*....|....*....|....*...
gi 1411134203 1509 DWKQKH--EESQTLLDASRKEIQALSTE 1534
Cdd:pfam07888 377 QKEKEQlqAEKQELLEYIRQLEQRLETV 404
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
898-1347 |
3.32e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 898 ERGEEIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQL-QAEQETLANVEEQCEWLIKskiQLEARVKEL 976
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLER---ELEERERRR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 977 SERVEEEEEINSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEA 1056
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1057 HQQTLDDLhmeEEKLSsLSKANLKleqqVVG---------------LEGAL-----------EQERKAR--INCERELHK 1108
Cdd:COG4913 442 LLALRDAL---AEALG-LDEAELP----FVGelievrpeeerwrgaIERVLggfaltllvppEHYAAALrwVNRLHLRGR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1109 LEGD-LKLNQESMENLESSQRHLAEELR----------KKELENSQMNSKVENEKGLvAQLQK------MVKELQT---- 1167
Cdd:COG4913 514 LVYErVRTGLPDPERPRLDPDSLAGKLDfkphpfrawlEAELGRRFDYVCVDSPEEL-RRHPRaitragQVKGNGTrhek 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1168 ------------------QIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEevggaSLAQLEITKKQETKFQKLR 1229
Cdd:COG4913 593 ddrrrirsryvlgfdnraKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-----ALQRLAEYSWDEIDVASAE 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1230 RDMEEAT---LHFEATSASLkKRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRAKANAEKLCTLY 1306
Cdd:COG4913 668 REIAELEaelERLDASSDDL-AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1411134203 1307 -----EERLNEANAKL---DKVTQLANDLAAQKTELWSESGEFLRRLEE 1347
Cdd:COG4913 747 lrallEERFAAALGDAverELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1132-1856 |
3.57e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1132 EELRKKELENSQMNSKVENEKGLVAQLQKMVKELQtqiKDLKEKLeaeRTTRAKMEKERADLTQDLADLNERLEevggAS 1211
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETS---AELNQLL---RTLDDQWKEKRDELNGELSAADAAVA----KD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1212 LAQLEITKKQETKFQKLrrDMEEATLHFEaTSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEq 1291
Cdd:pfam12128 321 RSELEALEDQHGAFLDA--DIETAAADQE-QLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIK- 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1292 mtrakanaEKLCTLYEERLNEANAKLDKVTQLANdlaaqktelwsesgeFLRrlEEKEALINQLSREKSNFTRQIEELRG 1371
Cdd:pfam12128 397 --------DKLAKIREARDRQLAVAEDDLQALES---------------ELR--EQLEAGKLEFNEEEYRLKSRLGELKL 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1372 QLEKETKSQSALahaLQKAQRDCDLLREQYEEEQEVKAelhrtLSKVNAEMVQWRMKYEnnviQKTEDLEDAKKELAIRL 1451
Cdd:pfam12128 452 RLNQATATPELL---LQLENFDERIERAREEQEAANAE-----VERLQSELRQARKRRD----QASEALRQASRRLEERQ 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1452 QETAEAMGVANARNASLeraRHRLQLELGDALSDLGKVrSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIqal 1531
Cdd:pfam12128 520 SALDELELQLFPQAGTL---LHFLRKEAPDWEQSIGKV-ISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDV--- 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1532 stellklkhayKESIVGQETLRRENKNLQEEIsnltnqvregtknltemekvkklieQEKTEVQVTLEETEGALERnesk 1611
Cdd:pfam12128 593 -----------PEWAASEEELRERLDKAEEAL-------------------------QSAREKQAAAEEQLVQANG---- 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1612 ilrfqlELLKAKAELERKLSEkdeeLENFRRKQQCTIDSMQSSLDSEAKSRIEATRLK----KKMEEDLNEMELQLSCA- 1686
Cdd:pfam12128 633 ------ELEKASREETFARTA----LKNARLDLRRLFDEKQSEKDKKNKALAERKDSAnerlNSLEAQLKQLDKKHQAWl 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1687 ---NRQVSEA-TKSLGQLQIQIKDLQMQLDDSTQlnSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEE--EL 1760
Cdd:pfam12128 703 eeqKEQKREArTEKQAYWQVVEGALDAQLALLKA--AIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREirTL 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1761 LEATERINLFYT--------QNTSLLSQKKKLEADVAQMQKEAEEVVQEC-----------QNAEEKAKKAATEAANLSE 1821
Cdd:pfam12128 781 ERKIERIAVRRQevlryfdwYQETWLQRRPRLATQLSNIERAISELQQQLarliadtklrrAKLEMERKASEKQQVRLSE 860
|
730 740 750
....*....|....*....|....*....|....*..
gi 1411134203 1822 ELKKKQDTIAHLEKTRE--NMEQTITDLQKRLAEAEQ 1856
Cdd:pfam12128 861 NLRGLRCEMSKLATLKEdaNSEQAQGSIGERLAQLED 897
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
897-1105 |
3.77e-05 |
|
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: 48.91 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 897 SERGEEIAGLKEECA------------QLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIK 964
Cdd:TIGR02169 768 EELEEDLHKLEEALNdlearlshsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 965 SKIQLEARVKELSERVEEEEEINSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTE-------HKVKNLTEEVE 1037
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiekkrKRLSELKAKLE 927
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411134203 1038 FLNEDISKLNRAAKVVQEAHQQTLD--DLHME----EEKLSSLSKANLKLEQQVVGLEGALE--QERKARINCERE 1105
Cdd:TIGR02169 928 ALEEELSEIEDPKGEDEEIPEEELSleDVQAElqrvEEEIRALEPVNMLAIQEYEEVLKRLDelKEKRAKLEEERK 1003
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
924-1606 |
3.92e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 924 REELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKS-KIQLEARVKELSERVEEEEEINSELTARGRKLEDECS 1002
Cdd:pfam12128 321 RSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERlKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLA 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1003 ELKKEIDDL----ETMLVKSEKEKRTT-EHKVKNLTEEVEFLNEDISKLnraaKVVQEAHQQTLDDLHMEEEKLSSLSKA 1077
Cdd:pfam12128 401 KIREARDRQlavaEDDLQALESELREQlEAGKLEFNEEEYRLKSRLGEL----KLRLNQATATPELLLQLENFDERIERA 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1078 NLKLEQQVVGLEGALEQERKARI----------NCERELHKLEGDLklnQESMENLESSQRHLAEELRKKELENSQMNSK 1147
Cdd:pfam12128 477 REEQEAANAEVERLQSELRQARKrrdqasealrQASRRLEERQSAL---DELELQLFPQAGTLLHFLRKEAPDWEQSIGK 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1148 V-------------ENEKGLVAQLQKMVK-ELQTQIKDLKEKLEAERTTRAKMEKERADLtQDLADLNERLEEVGGASLA 1213
Cdd:pfam12128 554 VispellhrtdldpEVWDGSVGGELNLYGvKLDLKRIDVPEWAASEEELRERLDKAEEAL-QSAREKQAAAEEQLVQANG 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1214 QLEITKKQETK----FQKLRRDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSD-LQLEVDDLLTR 1288
Cdd:pfam12128 633 ELEKASREETFartaLKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAwLEEQKEQKREA 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1289 IEQMTRAKANAEKLCTLYEERLNEANAKLDkvTQLANDLAAQKTELWSEsgefLRRLEEKEALINQLSREKSNFTRQIEE 1368
Cdd:pfam12128 713 RTEKQAYWQVVEGALDAQLALLKAAIAARR--SGAKAELKALETWYKRD----LASLGVDPDVIAKLKREIRTLERKIER 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1369 LRGQLEKETKSQSALAHA-LQKAQRDCDLLREQYEEEQEVKAELHRTLSKV---NAEMVQWRMKYENNVIQKTEDLEDAK 1444
Cdd:pfam12128 787 IAVRRQEVLRYFDWYQETwLQRRPRLATQLSNIERAISELQQQLARLIADTklrRAKLEMERKASEKQQVRLSENLRGLR 866
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1445 KELA----IRL-QETAEAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARLdqkqlqSGKALAD-WKQKHEES- 1517
Cdd:pfam12128 867 CEMSklatLKEdANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADH------SGSGLAEtWESLREEDh 940
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1518 -----QTLLDASRKEIQALStELLKLKHAYKESIVGQetLRRENKNLQEE----ISNLTNQV----REGTKNLTEMEKVK 1584
Cdd:pfam12128 941 yqndkGIRLLDYRKLVPYLE-QWFDVRVPQSIMVLRE--QVSILGVDLTEfydvLADFDRRIasfsRELQREVGEEAFFE 1017
|
730 740
....*....|....*....|..
gi 1411134203 1585 KLieqekTEVQVTLEETEGALE 1606
Cdd:pfam12128 1018 GV-----SESAVRIRSKVSELE 1034
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
889-1249 |
4.11e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 889 KIKPLVKSSERGEEIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQ 968
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE 1501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 969 LEARVKELSERVEEEEEINSELTARGRKLED--ECSELKKEIDDLETMLVKSEKEKRTTEHKVKnlTEEVEFLNEDISKL 1046
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEakKADEAKKAEEKKKADELKKAEELKKAEEKKK--AEEAKKAEEDKNMA 1579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1047 NRAAKVVQEAHQQTLDDL--------HMEEEKLSSLSKANLKLEQ---------QVVGLEGALEQERKArincERELHKL 1109
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVmklyeeekKMKAEEAKKAEEAKIKAEElkkaeeekkKVEQLKKKEAEEKKK----AEELKKA 1655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1110 EGDLKLNQESMENLESSQRHLAEELRKKELEN---SQMNSKVENEKGLVAQLQKMVKELQTQIKDLKeKLEAERTTRAKM 1186
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEkkaAEALKKEAEEAKKAEELKKKEAEEKKKAEELK-KAEEENKIKAEE 1734
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411134203 1187 EKERADLTQDLADlNERLEEVGGASLAQLeitKKQETKFQKLRRDMEEATLHFEATSASLKKR 1249
Cdd:PTZ00121 1735 AKKEAEEDKKKAE-EAKKDEEEKKKIAHL---KKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1120-1301 |
4.52e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1120 MENLESSQRHLAEELRKKELENSQMnsKVENEKglvaqlQKMVKELQTQIKDLKEKLEAERTTRakmEKERADLTQDLAD 1199
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKK--EAEAIK------KEALLEAKEEIHKLRNEFEKELRER---RNELQKLEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1200 LNERLEEvggaslaQLEITKKQETKFQKLRRDMEEATLHFEATSASLKKRHADSLAELEgQVENLQQ---VKQKLEKDRS 1276
Cdd:PRK12704 94 KEENLDR-------KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE-RISGLTAeeaKEILLEKVEE 165
|
170 180
....*....|....*....|....*
gi 1411134203 1277 DLQLEVDDLLTRIEQmtRAKANAEK 1301
Cdd:PRK12704 166 EARHEAAVLIKEIEE--EAKEEADK 188
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1519-1991 |
4.72e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.68 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1519 TLLDASRKEIQALSTELLKLKHAYKESIVGQETLRRE----NKNLQEEISNLTNQVREGTKNLTemekvkklieQEKTEV 1594
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEErqetSAELNQLLRTLDDQWKEKRDELN----------GELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1595 QVTLEETEGALERNESKILRFQLE-LLKAKAELER------KLSEKDEELENFRRKQQ---CTIDSMQSSLDSE------ 1658
Cdd:pfam12128 314 DAAVAKDRSELEALEDQHGAFLDAdIETAAADQEQlpswqsELENLEERLKALTGKHQdvtAKYNRRRSKIKEQnnrdia 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1659 ------AKSRIEATRLKKKMEEDL----NEMELQLSCANRQVSEATKslgQLQIQIKDLQMQLDDSTqLNSDLKEQVAV- 1727
Cdd:pfam12128 394 gikdklAKIREARDRQLAVAEDDLqaleSELREQLEAGKLEFNEEEY---RLKSRLGELKLRLNQAT-ATPELLLQLENf 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1728 -------------AERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERIN----LFYTQNTSLLSQKKKLEADVAQ 1790
Cdd:pfam12128 470 derierareeqeaANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDelelQLFPQAGTLLHFLRKEAPDWEQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1791 MQKE--AEEVVQECQNAEEKAKKAATEAANL-SEELKKKQ----DTIAHLEKTRENMEQTITDLQ--KRLAEAEQTALMG 1861
Cdd:pfam12128 550 SIGKviSPELLHRTDLDPEVWDGSVGGELNLyGVKLDLKRidvpEWAASEEELRERLDKAEEALQsaREKQAAAEEQLVQ 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1862 SRKQIQKL---ESRVRELEGELEGEIRR-SAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDklqlkvhnyKQQVE 1937
Cdd:pfam12128 630 ANGELEKAsreETFARTALKNARLDLRRlFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD---------KKHQA 700
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1411134203 1938 VAEAQANQYLSKYKKQQHELNEVKERAEVAESQVnKLKIKAREFGKKVRQAQTE 1991
Cdd:pfam12128 701 WLEEQKEQKREARTEKQAYWQVVEGALDAQLALL-KAAIAARRSGAKAELKALE 753
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1105-1296 |
5.14e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1105 ELHKLegDLKLNQesmenLESSQRHLAEELRKKELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEA--ERTT 1182
Cdd:COG1579 11 DLQEL--DSELDR-----LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1183 RAKMEKERADLTQDLADLNERLEEvggASLAQLEITKKQETKfqklrrdmEEATLHFEATSASLKKRHADSLAELEGQVE 1262
Cdd:COG1579 84 NVRNNKEYEALQKEIESLKRRISD---LEDEILELMERIEEL--------EEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1411134203 1263 NLQQVKQKLEKDRSDLQLEVD-DLLTRIEQMTRAK 1296
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPpELLALYERIRKRK 187
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
889-1300 |
5.15e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 889 KIKPLVKSSERGEEIAGLKEECAQLQKALEKSEFQR--EEL-KAKQVSLTQEKNDlILQLQAEQETLANVEEQCEWLIKS 965
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKkaDELkKAEELKKAEEKKK-AEEAKKAEEDKNMALRKAEEAKKA 1589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 966 KiqlEARVKELSERVEEEEEINSELTARGRKLEDECSELKKEiddletmlvksEKEKRTTEHKVKNLTEEVEfLNEDISK 1045
Cdd:PTZ00121 1590 E---EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----------EEEKKKVEQLKKKEAEEKK-KAEELKK 1654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1046 LNRAAKVVQEAHQQTLDDlhmEEEKLSSLSKANLKLEQQVVGLEGALEQERKARincerELHKLEGDLKLNQESMENLES 1125
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEE---DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE-----ELKKKEAEEKKKAEELKKAEE 1726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1126 SQRHLAEELRKKELEN---SQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAE----RTTRAKMEKERAdlTQDLA 1198
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDkkkAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeldeEDEKRRMEVDKK--IKDIF 1804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1199 DLNERLEEVGgaslaqleitkKQETKFQKLRRDMEEATLHFEATSASLKKRHADslaELEGQVENLQQVKQKLEKDRSDL 1278
Cdd:PTZ00121 1805 DNFANIIEGG-----------KEGNLVINDSKEMEDSAIKEVADSKNMQLEEAD---AFEKHKFNKNNENGEDGNKEADF 1870
|
410 420
....*....|....*....|..
gi 1411134203 1279 QLEVDDLLTRIEQMTRAKANAE 1300
Cdd:PTZ00121 1871 NKEKDLKEDDEEEIEEADEIEK 1892
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
996-1954 |
5.43e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 996 KLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKN-----LTEEVEFLNEDISK-LNRaakvvqeahqqTLDDLHMEEE 1069
Cdd:TIGR01612 697 KLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNelldiIVEIKKHIHGEINKdLNK-----------ILEDFKNKEK 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1070 KLSSLSKANLKLEQQVVGLEGALeQERKARINCERELHKLEgdlklNQESMENLESSQRHLaEELRKKELENSQMNSKVE 1149
Cdd:TIGR01612 766 ELSNKINDYAKEKDELNKYKSKI-SEIKNHYNDQINIDNIK-----DEDAKQNYDKSKEYI-KTISIKEDEIFKIINEMK 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1150 NEKGLVaqLQKMVKELQTQiKDLKEKLEAERTTRAKM-EKERADLTQDlaDLNERLEEVGGASLAQLEITKKQETKFQKL 1228
Cdd:TIGR01612 839 FMKDDF--LNKVDKFINFE-NNCKEKIDSEHEQFAELtNKIKAEISDD--KLNDYEKKFNDSKSLINEINKSIEEEYQNI 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1229 R--RDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQK--LEKDRSDlQLEvDDLLTRIEQMTRAkanaeklct 1304
Cdd:TIGR01612 914 NtlKKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESnlIEKSYKD-KFD-NTLIDKINELDKA--------- 982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1305 LYEERLNEANAKLDKVTQLANDLaaqKTELWSESGEFL-RRLEEKEALINQLSREKSNFTRQIEELrgQLEKETKSQSAL 1383
Cdd:TIGR01612 983 FKDASLNDYEAKNNELIKYFNDL---KANLGKNKENMLyHQFDEKEKATNDIEQKIEDANKNIPNI--EIAIHTSIYNII 1057
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1384 AHALQKAQRDCDLLREQYEEEQEVkaelhrtlSKVNAEMVQWRMKYENnviqktedLEDAKKELAIRLQEtaeamgvana 1463
Cdd:TIGR01612 1058 DEIEKEIGKNIELLNKEILEEAEI--------NITNFNEIKEKLKHYN--------FDDFGKEENIKYAD---------- 1111
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1464 rnaslerarhrlqlelgdalsDLGKVRSAAARLDQKQLQSGKALADWKQKheeSQTLLDASRKEIQALstELLKLKHAYK 1543
Cdd:TIGR01612 1112 ---------------------EINKIKDDIKNLDQKIDHHIKALEEIKKK---SENYIDEIKAQINDL--EDVADKAISN 1165
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1544 ESIVGQETlRREN--------KNLQEEISNLTNQVREGTKNLTEMEKVKKL-IEQEKTEVQVTLEETEGALERNESKIlr 1614
Cdd:TIGR01612 1166 DDPEEIEK-KIENivtkidkkKNIYDEIKKLLNEIAEIEKDKTSLEEVKGInLSYGKNLGKLFLEKIDEEKKKSEHMI-- 1242
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1615 fqlELLKAKAELERKLSEKDEELENFRRKQQCTIDSMQSSLDSEAKSRIEATRLKKKME--EDLNEMELQLSCANRQVSE 1692
Cdd:TIGR01612 1243 ---KAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDEniSDIREKSLKIIEDFSEESD 1319
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1693 ATkslgqlQIQiKDLQMQLDDSTQLNSDLKEQVA-VAERRNSL----LQSELEDLRSLQEQTERGRRLSEEElLEATERI 1767
Cdd:TIGR01612 1320 IN------DIK-KELQKNLLDAQKHNSDINLYLNeIANIYNILklnkIKKIIDEVKEYTKEIEENNKNIKDE-LDKSEKL 1391
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1768 NLFYTQNTSLLSQKKKLEADVaqmqkeAEEVVQEC-QNAEEKAKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITD 1846
Cdd:TIGR01612 1392 IKKIKDDINLEECKSKIESTL------DDKDIDECiKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNK 1465
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1847 LQKRLAEAEQTALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELT-----YQAEEDKKNLSRMQTQ 1921
Cdd:TIGR01612 1466 SQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTellnkYSALAIKNKFAKTKKD 1545
|
970 980 990
....*....|....*....|....*....|...
gi 1411134203 1922 MDKLQLKVHNYKQQVEVAEAQANQYLSKYKKQQ 1954
Cdd:TIGR01612 1546 SEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEK 1578
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
995-1800 |
6.47e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 995 RKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTlddlHMEEEKLSSL 1074
Cdd:PRK04863 282 RVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQ----EKIERYQADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1075 SKANLKLEQQVVGLEGALEQ----ERKARINcERELHKLEGDLKLNQESMENLE--SSQRHLAEE-LRKKELENSQMNSK 1147
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQqeenEARAEAA-EEEVDELKSQLADYQQALDVQQtrAIQYQQAVQaLERAKQLCGLPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1148 VENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKErADLTQDLADLNERLE--EVGGASLAQLEITKKQETKF 1225
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQA-YQLVRKIAGEVSRSEawDVARELLRRLREQRHLAEQL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1226 QKLRRDMEEA--TLHFEATS----ASLKKRHADSL----------AELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRI 1289
Cdd:PRK04863 516 QQLRMRLSELeqRLRQQQRAerllAEFCKRLGKNLddedeleqlqEELEARLESLSESVSEARERRMALRQQLEQLQARI 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1290 EQMTR-------AKANAEKLCTLYEERLNEANAkldkVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLS-REKSN 1361
Cdd:PRK04863 596 QRLAArapawlaAQDALARLREQSGEEFEDSQD----VTEYMQQLLERERELTVERDELAARKQALDEEIERLSqPGGSE 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1362 FTRQI---EELRGQLEKETKSQ---------SAL----AHALqkAQRDCDLLREQYEEEQEVKAELHRTL--------SK 1417
Cdd:PRK04863 672 DPRLNalaERFGGVLLSEIYDDvsledapyfSALygpaRHAI--VVPDLSDAAEQLAGLEDCPEDLYLIEgdpdsfddSV 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1418 VNAEmvqwrmKYENNVIQKTEDLE-------------DAKKE-----LAIRLQETAEAMGVANARNASLERARHRLQLEL 1479
Cdd:PRK04863 750 FSVE------ELEKAVVVKIADRQwrysrfpevplfgRAAREkrieqLRAEREELAERYATLSFDVQKLQRLHQAFSRFI 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1480 GD--ALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALStellklKHAYKESIVGQETLRRENK 1557
Cdd:PRK04863 824 GShlAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALN------RLLPRLNLLADETLADRVE 897
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1558 NLQEEISNLTNQ---VREGTKNLTEMEKVKKLIEQEKTEvqvtLEETEGALERNESkilrfQLELLKAKAeleRKLSEKD 1634
Cdd:PRK04863 898 EIREQLDEAEEAkrfVQQHGNALAQLEPIVSVLQSDPEQ----FEQLKQDYQQAQQ-----TQRDAKQQA---FALTEVV 965
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1635 EELENFRRKQQCTIDSMQSSLDSEAKSRIEatrlkkKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDS 1714
Cdd:PRK04863 966 QRRAHFSYEDAAEMLAKNSDLNEKLRQRLE------QAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1715 TQLNSDLKEQV-----AVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELleaterinlfytqnTSLLSQKKKLEADVA 1789
Cdd:PRK04863 1040 KQELQDLGVPAdsgaeERARARRDELHARLSANRSRRNQLEKQLTFCEAEM--------------DNLTKKLRKLERDYH 1105
|
890
....*....|.
gi 1411134203 1790 QMQkeaEEVVQ 1800
Cdd:PRK04863 1106 EMR---EQVVN 1113
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
912-1205 |
8.13e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.81 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 912 QLQKALEKSEFQREELKAKQVSLTQEKNDLILQL-------------QAEQETLANVEEQCEWLIKSKIQLEARVKELSE 978
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVerrrkleeaekarQAEMDRQAAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 979 RVEEEEEINSELT---ARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEveflnedISKLNRAAKVVQE 1055
Cdd:pfam17380 359 KRELERIRQEEIAmeiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQ-------KVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1056 AHQQTLDDLHMEEEK-LSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMEN-LESSQRHLAEE 1133
Cdd:pfam17380 432 ARQREVRRLEEERAReMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKeLEERKQAMIEE 511
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411134203 1134 LRK-----KELENSQMNSKVENEKGLVAQLQKMVKELQT--QIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLE 1205
Cdd:pfam17380 512 ERKrklleKEMEERQKAIYEEERRREAEEERRKQQEMEErrRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1343-1978 |
8.17e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.91 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1343 RRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSAlahALQKAQRDCDLLREQ-----------YEEEQEVKAEL 1411
Cdd:pfam12128 276 SRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADA---AVAKDRSELEALEDQhgafldadietAAADQEQLPSW 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1412 HRTLSKVNAEM-----------------VQWRMKYENNVIQKTEDLEDAKKELAIRLQETAEAM--GVANARNASLERAR 1472
Cdd:pfam12128 353 QSELENLEERLkaltgkhqdvtakynrrRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDlqALESELREQLEAGK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1473 HRL---QLELGDALSDLgKVRSAAARLDQKQLQSGKALADWKQKHEESQTlldASRKEIQALSTELLKLKHAYKESivgQ 1549
Cdd:pfam12128 433 LEFneeEYRLKSRLGEL-KLRLNQATATPELLLQLENFDERIERAREEQE---AANAEVERLQSELRQARKRRDQA---S 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1550 ETLRRENKNLQEeisnltnqvregtknltemekvkklIEQEKTEVQVTLEETEGALE---RNESKILRFQLELLKAKAEL 1626
Cdd:pfam12128 506 EALRQASRRLEE-------------------------RQSALDELELQLFPQAGTLLhflRKEAPDWEQSIGKVISPELL 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1627 ERklSEKDEELENFRRKQQCTIDSMQssLDSEAKSRIEATRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKD 1706
Cdd:pfam12128 561 HR--TDLDPEVWDGSVGGELNLYGVK--LDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEK 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1707 LQMQLDDSTQL--NSDLKEQVAVAERRNSLLQseledlrsLQEQTERGRRLSEEEL--LEATERINLFYTQNTSLLSQKK 1782
Cdd:pfam12128 637 ASREETFARTAlkNARLDLRRLFDEKQSEKDK--------KNKALAERKDSANERLnsLEAQLKQLDKKHQAWLEEQKEQ 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1783 KLEADVaQMQKEAEEVVQECQNAEEK-AKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQTAlmg 1861
Cdd:pfam12128 709 KREART-EKQAYWQVVEGALDAQLALlKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKI--- 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1862 srKQIQKLESRVRELEGELegeirRSAEAQRGARRLERCikeltyqaEEDKKNLSRMQTQMDKLQlkvhnykQQVEVAEA 1941
Cdd:pfam12128 785 --ERIAVRRQEVLRYFDWY-----QETWLQRRPRLATQL--------SNIERAISELQQQLARLI-------ADTKLRRA 842
|
650 660 670
....*....|....*....|....*....|....*..
gi 1411134203 1942 QANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKA 1978
Cdd:pfam12128 843 KLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDA 879
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1821-1930 |
8.27e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1821 EELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQTalmgsrkqIQKLESRVRELEGELEGEIRRSAEAQRGARRLERC 1900
Cdd:COG2433 406 RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDER--------IERLERELSEARSEERREIRKDREISRLDREIERL 477
|
90 100 110
....*....|....*....|....*....|
gi 1411134203 1901 IKELtYQAEEDKKNLSRMQTQMDKLQLKVH 1930
Cdd:COG2433 478 EREL-EEERERIEELKRKLERLKELWKLEH 506
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1515-1693 |
8.71e-05 |
|
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: 46.67 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1515 EESQTLLDASRKEIQALSTELLKLKhaykesivgQETLRRENKnLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEktev 1594
Cdd:pfam09787 50 EELRQERDLLREEIQKLRGQIQQLR---------TELQELEAQ-QQEEAESSREQLQELEEQLATERSARREAEAE---- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1595 qvtleetegaLERNESKILRFQLELLKAKAELERKLSEKDEELEnfRRKQQCTIDSMQSSLDSEAKSRI----EATRLKK 1670
Cdd:pfam09787 116 ----------LERLQEELRYLEEELRRSKATLQSRIKDREAEIE--KLRNQLTSKSQSSSSQSELENRLhqltETLIQKQ 183
|
170 180
....*....|....*....|....*..
gi 1411134203 1671 KMEEDL----NEMELQLSCANRQVSEA 1693
Cdd:pfam09787 184 TMLEALstekNSLVLQLERMEQQIKEL 210
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1455-1645 |
9.78e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1455 AEAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALSTE 1534
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1535 LLKLKHAYKESIVG-QETLRREN--------KNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQektevqvtLEETEGAL 1605
Cdd:COG3883 81 IEERREELGERARAlYRSGGSVSyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAE--------LEAKKAEL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1411134203 1606 ERNESKILRFQLELLKAKAELERKLSEKDEELENFRRKQQ 1645
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1337-1700 |
1.07e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 47.33 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1337 ESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEketKSQSALAHALQK----------------------AQRDC 1394
Cdd:pfam05701 50 EIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLE---RAQTEEAQAKQDselaklrveemeqgiadeasvaAKAQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1395 DLLREQYE----EEQEVKAELhRTLSKVNAEMVQWR---MKYENNVIQKTEDLEDAKKELAIRLQETAEAMGVANArnAS 1467
Cdd:pfam05701 127 EVAKARHAaavaELKSVKEEL-ESLRKEYASLVSERdiaIKRAEEAVSASKEIEKTVEELTIELIATKESLESAHA--AH 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1468 LERARHRLqlelgdalsdlgkvrSAAARLDQKQLQSGKALadwKQKHEESQTLLD--ASRKEIQ----ALSTELLKLK-- 1539
Cdd:pfam05701 204 LEAEEHRI---------------GAALAREQDKLNWEKEL---KQAEEELQRLNQqlLSAKDLKskleTASALLLDLKae 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1540 -HAYKESIVGQETLRRENKnlqEEISNLTNQVREGTKNltEMEKVKKLIEQEKTEVqvtleetegalernesKILRFQLE 1618
Cdd:pfam05701 266 lAAYMESKLKEEADGEGNE---KKTSTSIQAALASAKK--ELEEVKANIEKAKDEV----------------NCLRVAAA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1619 LLkaKAELERklsEKdEELENFRRKQ---QCTIDSMQSSLDSeAKSRIEATRLK-KKMEEDLNEMELQLSCANRQVSEAt 1694
Cdd:pfam05701 325 SL--RSELEK---EK-AELASLRQREgmaSIAVSSLEAELNR-TKSEIALVQAKeKEAREKMVELPKQLQQAAQEAEEA- 396
|
....*.
gi 1411134203 1695 KSLGQL 1700
Cdd:pfam05701 397 KSLAQA 402
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1507-1703 |
1.08e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1507 LADWKQKHEESQTLLDASRKEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKL 1586
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1587 IEQEKTEVQVTL--EETEGALERNE--SKILRFQLELLKAKAELERKLSEKDEELENFRRKQQCTIDSMQSSLDSEAKSR 1662
Cdd:COG3883 98 SGGSVSYLDVLLgsESFSDFLDRLSalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1411134203 1663 IEATRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQ 1703
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1280-1856 |
1.17e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1280 LEVDDLLTRIEQMtraKANAEKLcTLYEERLNEANAKLDKVTQLAndlaaqktELWSESGEFLRRLEEKEALINQLSREK 1359
Cdd:COG4913 218 LEEPDTFEAADAL---VEHFDDL-ERAHEALEDAREQIELLEPIR--------ELAERYAAARERLAELEYLRAALRLWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1360 SnfTRQIEELRGQLEketksqsALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKvnaemvqwrmkyennviQKTED 1439
Cdd:COG4913 286 A--QRRLELLEAELE-------ELRAELARLEAELERLEARLDALREELDELEAQIRG-----------------NGGDR 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1440 LEDAKKELAiRLQETAEAmgVANARnASLERARHRLQLELGDALSDLGKVRSAAARL------DQKQLQsgKALADWKQK 1513
Cdd:COG4913 340 LEQLEREIE-RLERELEE--RERRR-ARLEALLAALGLPLPASAEEFAALRAEAAALlealeeELEALE--EALAEAEAA 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1514 HEESQTLLDASRKEIQALST-------ELLKLKHAYKESIVGQETlrrENKNLQEEIsnltnQVRE-------------G 1573
Cdd:COG4913 414 LRDLRRELRELEAEIASLERrksnipaRLLALRDALAEALGLDEA---ELPFVGELI-----EVRPeeerwrgaiervlG 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1574 TKNLTEM------EKVKKLIEQEKTEVQVTLEETEGALERNESKILRFQ--LELLKAK-----AELERKLS--------E 1632
Cdd:COG4913 486 GFALTLLvppehyAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDslAGKLDFKphpfrAWLEAELGrrfdyvcvD 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1633 KDEELENFRRK--QQCTIDSMQSSLDSEAKSRI--------EATRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQI 1702
Cdd:COG4913 566 SPEELRRHPRAitRAGQVKGNGTRHEKDDRRRIrsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1703 QIKDLQMQLD-DSTQLNSD-LKEQVAVAERRNSLLQSELEDLRSLQEQTERgrrlSEEELLEATERINLFYTQNTSLLSQ 1780
Cdd:COG4913 646 RREALQRLAEySWDEIDVAsAEREIAELEAELERLDASSDDLAALEEQLEE----LEAELEELEEELDELKGEIGRLEKE 721
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411134203 1781 KKKLEADVAQMQKEAEEVVQECQNAEEKAKkaateaanlsEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQ 1856
Cdd:COG4913 722 LEQAEEELDELQDRLEAAEDLARLELRALL----------EERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
895-1380 |
1.32e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 895 KSSERGEEIAGLKEECAQLQKALEKSEFQREElKAKQVSLTQEKNDLILQLQAE----QETLANVEEQCEWLIKSKIQLE 970
Cdd:TIGR00618 484 QETRKKAVVLARLLELQEEPCPLCGSCIHPNP-ARQDIDNPGPLTRRMQRGEQTyaqlETSEEDVYHQLTSERKQRASLK 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 971 ARVKELSERVEEEEEINSELTARGRKLEDECSELKKEIDdletMLVKSEKEKRTTEHkvknltEEVEFLNEDISKLNRAA 1050
Cdd:TIGR00618 563 EQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE----KLSEAEDMLACEQH------ALLRKLQPEQDLQDVRL 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1051 KVVQEAHQQTLDDLHMEEEKLSslskanlkLEQQvvglegalEQERKARINCERELHKLEgdlkLNQESMENLESSQRHL 1130
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLT--------LTQE--------RVREHALSIRVLPKELLA----SRQLALQKMQSEKEQL 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1131 AEELRKKELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVGGA 1210
Cdd:TIGR00618 693 TYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTA 772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1211 SLAQLEITKKQETKFQKLRRDMEEATLHFEATSASLKKRHADSLAELEGQVE----NLQQVKQKLEKdRSDLQLEVDDLL 1286
Cdd:TIGR00618 773 ALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCEtlvqEEEQFLSRLEE-KSATLGEITHQL 851
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1287 TRIEQMTRakanaeklctlyeeRLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQI 1366
Cdd:TIGR00618 852 LKYEECSK--------------QLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFH 917
|
490
....*....|....
gi 1411134203 1367 EELRGQLEKETKSQ 1380
Cdd:TIGR00618 918 GRYADSHVNARKYQ 931
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
897-1191 |
1.63e-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: 46.43 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 897 SERGEEIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEA----- 971
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETelerm 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 972 --RVKELSERVEEEEEINSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEeveflnedisKLNRA 1049
Cdd:pfam07888 156 keRAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQ----------KLTTA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1050 AKVVQEaHQQTLDDLHMEEEKLSSlskanlkLEQQVVGLEGALEQERKARINCERELHKL-----EGDLKLNQESMENLE 1124
Cdd:pfam07888 226 HRKEAE-NEALLEELRSLQERLNA-------SERKVEGLGEELSSMAAQRDRTQAELHQArlqaaQLTLQLADASLALRE 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411134203 1125 SSQRHlaeelrKKELENSQMNSKVENEKglvaqlqkmVKELQTQIKDLKEKLEAERTTRAKMEKERA 1191
Cdd:pfam07888 298 GRARW------AQERETLQQSAEADKDR---------IEKLSAELQRLEERLQEERMEREKLEVELG 349
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1405-1643 |
1.85e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1405 QEVKAELHRTLSKVNAEMVQWRMKYENNvIQKTEDLEDAKKELAIRLQETAEAMGVANARNASLERARHRLQLELGDALS 1484
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1485 DLGKVRSAAARLDQKQLQSGKAladwkqkheeSQTLLDASRKEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEEIS 1564
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQ----------PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411134203 1565 NLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKIlrfqLELLKAKAELERKLSEKDEELENFRRK 1643
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL----AELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1481-1671 |
2.11e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1481 DALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALSTELLKLKHAYKESivgqETLRRENKNLQ 1560
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV----EARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1561 EEISNlTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKILRFQLELLKAKAELERKLSEKDEELENF 1640
Cdd:COG1579 83 GNVRN-NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170 180 190
....*....|....*....|....*....|.
gi 1411134203 1641 RRKqqctIDSMQSSLDSEAKSRIEATRLKKK 1671
Cdd:COG1579 162 EAE----REELAAKIPPELLALYERIRKRKN 188
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1482-1742 |
2.73e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.98 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1482 ALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALSTELLKLKHAYKESIvgqETLRRENKNLQE 1561
Cdd:PRK04778 103 AKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPAL---DELEKQLENLEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1562 EIS---NLTN------------QVREGTKNLTE-MEKVKKLIEQEKTEVQVTLEETEGA----LERN--------ESKIL 1613
Cdd:PRK04778 180 EFSqfvELTEsgdyveareildQLEEELAALEQiMEEIPELLKELQTELPDQLQELKAGyrelVEEGyhldhldiEKEIQ 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1614 RFQLELLKAKAELER----KLSEKDEELENfrrkqqcTIDSMQSSLDSEAKSRIEATRLKKKMEEDLNEMELQlscaNRQ 1689
Cdd:PRK04778 260 DLKEQIDENLALLEEldldEAEEKNEEIQE-------RIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQ----NKE 328
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411134203 1690 VSEATKSLGQ--------LQIQiKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDL 1742
Cdd:PRK04778 329 LKEEIDRVKQsytlneseLESV-RQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEI 388
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
989-1673 |
2.77e-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: 46.20 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 989 ELTARGRKLEDECSELKKEIDDLETMLVKS-------EKEKR-----TTEHKVKNLTEEVEFLNEDISKLNRAAKVVQE- 1055
Cdd:TIGR01612 1133 ALEEIKKKSENYIDEIKAQINDLEDVADKAisnddpeEIEKKienivTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEv 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1056 -----AHQQTLDDLHME---EEKLSS--LSKA---------NLKLEQQVVGLEGALEQERKARINC-------ERELHKL 1109
Cdd:TIGR01612 1213 kginlSYGKNLGKLFLEkidEEKKKSehMIKAmeayiedldEIKEKSPEIENEMGIEMDIKAEMETfnishddDKDHHII 1292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1110 ------------EGDLKLNQESMEnlESSQRHLAEELRKKELENSQMNS----------------KVENEKGLVAQLQKM 1161
Cdd:TIGR01612 1293 skkhdenisdirEKSLKIIEDFSE--ESDINDIKKELQKNLLDAQKHNSdinlylneianiynilKLNKIKKIIDEVKEY 1370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1162 VKELQTQIKDLKEKLEAERTTRAKME--------KERADLTQDLADLNERLEEVGGASLAQLEITKKQETKFQKLRRDME 1233
Cdd:TIGR01612 1371 TKEIEENNKNIKDELDKSEKLIKKIKddinleecKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNE 1450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1234 EATLHFEATSASlkkrhadslaelegqvENLQQVKQKLEKDR--SDLQLEVDDLLTRIEQMTRAKANAEKlctlyeerln 1311
Cdd:TIGR01612 1451 NVLLLFKNIEMA----------------DNKSQHILKIKKDNatNDHDFNINELKEHIDKSKGCKDEADK---------- 1504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1312 eaNAK-LDKVTQLANDLAAQKTELWSESGEFlrrleekeALINQLSREKSNFTRQIEELrgqleKETKSQSALaHALQKA 1390
Cdd:TIGR01612 1505 --NAKaIEKNKELFEQYKKDVTELLNKYSAL--------AIKNKFAKTKKDSEIIIKEI-----KDAHKKFIL-EAEKSE 1568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1391 QRDCDLLREQYEEEQEV-------KAELHRTLSKVNAEMVQWRM----KYENNVIQKTEDLEDAKKELAIRLQETAEAmg 1459
Cdd:TIGR01612 1569 QKIKEIKKEKFRIEDDAakndksnKAAIDIQLSLENFENKFLKIsdikKKINDCLKETESIEKKISSFSIDSQDTELK-- 1646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1460 vanarnaslerarhrlqlELGDALSDLgkvrsaaarldQKQLQSgkaLADWKQKHEESQTLLDASRKEIQALSTELLKLK 1539
Cdd:TIGR01612 1647 ------------------ENGDNLNSL-----------QEFLES---LKDQKKNIEDKKKELDELDSEIEKIEIDVDQHK 1694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1540 HAYKESIVgqetlrrenknlqeeisnltnqvregtknltemEKVKKLIEQEKTEVQVTLEETEGALERNESKILRFQLEL 1619
Cdd:TIGR01612 1695 KNYEIGII---------------------------------EKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEG 1741
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1411134203 1620 LKAKAELERKLSEKDEELENFRRKQQCTIDSMQS-SLDSEAKSRIEATRLKKKME 1673
Cdd:TIGR01612 1742 IDPNEKLEEYNTEIGDIYEEFIELYNIIAGCLETvSKEPITYDEIKNTRINAQNE 1796
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1186-1403 |
2.82e-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: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1186 MEKERADLTQDLADLNERLEEVGgaslAQLEitkKQETKFQKLRR-----DMEEATLHFEATSASLKKRHADSLAELEGQ 1260
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELR----KELE---EAEAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1261 VENLQQVKQKLEKDRSDLQLEVDDllTRIEQMTRAKANAEKLCTLYEERLNEANAKldkVTQLANDLAAQKTELWSESGe 1340
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTPNHPD---VIALRAQIAALRAQLQQEAQ- 312
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411134203 1341 flRRLEEKEALINQLSREKSNFTRQIEELRGQLeketKSQSALAHALQKAQRDCDLLREQYEE 1403
Cdd:COG3206 313 --RILASLEAELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYES 369
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1081-1235 |
2.91e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1081 LEQQVVGLEGALEqerkaRINceRELHKLEGDLKLNQESMENLESSQRHLAEELRKKELENSQMnskveneKGLVAQLQK 1160
Cdd:PRK09039 44 LSREISGKDSALD-----RLN--SQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRL-------QALLAELAG 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411134203 1161 MVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVGGASLAQLEITKKQETKFQKLRRDMEEA 1235
Cdd:PRK09039 110 AGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVA 184
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1048-1281 |
2.95e-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: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1048 RAAKVVQEAHQQTLDDLhmEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERE--LHKLEGDLKLNQESMENLES 1125
Cdd:COG3206 149 LAAAVANALAEAYLEQN--LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1126 SQRHLAEELR---------KKELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQD 1196
Cdd:COG3206 227 QLAEARAELAeaearlaalRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1197 LAdlnERLEEVGGASLAQLEITKKQEtkfQKLRRDMEEAtlhfEATSASLKKRHADsLAELEGQVENLQQVKQKLEKDRS 1276
Cdd:COG3206 307 LQ---QEAQRILASLEAELEALQARE---ASLQAQLAQL----EARLAELPELEAE-LRRLEREVEVARELYESLLQRLE 375
|
....*
gi 1411134203 1277 DLQLE 1281
Cdd:COG3206 376 EARLA 380
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
895-1128 |
3.05e-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: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 895 KSSERGEEIAGLKEECAQLQKALEKSEFQREELKAKQ--VSLTQEKNDLILQLQAEQETLANVEEQcewliksKIQLEAR 972
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAE-------LAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 973 VKELSERVEEEEEINSELTArgrklEDECSELKKEIDDLETMLvkSEKEKRTTE-H-KVKNLTEEVEFLNEDISKlnRAA 1050
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAEL--AELSARYTPnHpDVIALRAQIAALRAQLQQ--EAQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411134203 1051 KVVQEAHQQtlddlhmeeekLSSLSKANLKLEQQVVGLEGALEQERKArincERELHKLEGDLKLNQESMENLESSQR 1128
Cdd:COG3206 313 RILASLEAE-----------LEALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYESLLQRLE 375
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
998-1164 |
3.27e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 45.79 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 998 EDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVvqeaHQQTLDDLHMEEEKLSSLSKA 1077
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKV----KKKTLDLLPDAEENIAKLQAL 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1078 NLKLEQQVVGLEGALEQERKARINCEREL------HKLEGDLKLnqESMENLESSQRHLAEELRKKELENSQmnskvene 1151
Cdd:pfam05667 410 VDASAQRLVELAGQWEKHRVPLIEEYRALkeaksnKEDESQRKL--EEIKELREKIKEVAEEAKQKEELYKQ-------- 479
|
170
....*....|...
gi 1411134203 1152 kgLVAQLQKMVKE 1164
Cdd:pfam05667 480 --LVAEYERLPKD 490
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1117-1273 |
3.67e-04 |
|
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: 45.60 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1117 QESMENLESSQRHLA--EELRKKELENSQMNSKVENEKGLVAQLQKMVKELQTQ----------IKDLKEKLEAERTTRA 1184
Cdd:pfam15066 301 EQSFESLQPLEEDMAlnEVLQKLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKitkqqvfvdiINKLKENVEELIEDKY 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1185 KMEKERADLTQDLADLNE-------RLEEVGGASLA-QLEItKKQETKFQKLR-RDMEEatLHFEATSASLKKRHADSLA 1255
Cdd:pfam15066 381 NVILEKNDINKTLQNLQEilantqkHLQESRKEKETlQLEL-KKIKVNYVHLQeRYITE--MQQKNKSVSQCLEMDKTLS 457
|
170
....*....|....*...
gi 1411134203 1256 ELEGQVENLQQVKQKLEK 1273
Cdd:pfam15066 458 KKEEEVERLQQLKGELEK 475
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
908-1361 |
3.77e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 908 EECAQLQKALEKSEFqreeLKAKQVSLTQE---KNDLILQLQAEQETLANVEEQCEWLIK-------SKIQ----LEARV 973
Cdd:pfam10174 272 EEIKQMEVYKSHSKF----MKNKIDQLKQElskKESELLALQTKLETLTNQNSDCKQHIEvlkesltAKEQraaiLQTEV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 974 KELSERVEEEEEINSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVV 1053
Cdd:pfam10174 348 DALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSL 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1054 QEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVvglegalEQERKARincereLHKLEGDLKLNQESMENLESSQRHLAEE 1133
Cdd:pfam10174 428 QTDSSNTDTALTTLEEALSEKERIIERLKEQR-------EREDRER------LEELESLKKENKDLKEKVSALQPELTEK 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1134 ----LRKKELENSQMNSKVENE---KGLVAQLQKMVKE---LQTQIKDLKEKLEAERttrakMEKERADLTQDLADLNER 1203
Cdd:pfam10174 495 esslIDLKEHASSLASSGLKKDsklKSLEIAVEQKKEEcskLENQLKKAHNAEEAVR-----TNPEINDRIRLLEQEVAR 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1204 LEEVGGASLAQLEitkkqetKFQKLRRDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSDlqlEVD 1283
Cdd:pfam10174 570 YKEESGKAQAEVE-------RLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQ---LLE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1284 DLLTRIEQMTR--AKANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEE-----KEALINQLS 1356
Cdd:pfam10174 640 EARRREDNLADnsQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEilemkQEALLAAIS 719
|
....*
gi 1411134203 1357 REKSN 1361
Cdd:pfam10174 720 EKDAN 724
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1254-1421 |
4.27e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1254 LAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRAKANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQKte 1333
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1334 lwsESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKSQSALAHALQKAQRDCDLLREQYE-EEQEVKAELH 1412
Cdd:COG1579 90 ---EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEaELEELEAERE 166
|
....*....
gi 1411134203 1413 RTLSKVNAE 1421
Cdd:COG1579 167 ELAAKIPPE 175
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1252-1856 |
4.33e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1252 DSLAELEGQVENLQQVKQKLEKDRSDL-----QLEVD-----DLLTRIEQMTRAKANAEKLCTLYEERLNEANAKLDKVT 1321
Cdd:PRK01156 173 DVIDMLRAEISNIDYLEEKLKSSNLELenikkQIADDekshsITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1322 QLANDLAAQKTELWSESGE--FLRRLEEK-EALINQLSREKSNFTRQIEELRGQLE------KETKSQSALAHALQKAQR 1392
Cdd:PRK01156 253 RYESEIKTAESDLSMELEKnnYYKELEERhMKIINDPVYKNRNYINDYFKYKNDIEnkkqilSNIDAEINKYHAIIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1393 DCDLLREQYEEEQEVKAELHRTLSkvnaEMVQWRMKYE---NNVIQKTEDLEDAKKELAIRLQETAEAMGVANARNASLE 1469
Cdd:PRK01156 333 VLQKDYNDYIKKKSRYDDLNNQIL----ELEGYEMDYNsylKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1470 RARHRLQLELGDALSDLG--KVRSAAARLDQKQLQSGKALADWKQKHEESQTLL--DASRKEIQALSTELLKLKHAYKEs 1545
Cdd:PRK01156 409 KELNEINVKLQDISSKVSslNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLgeEKSNHIINHYNEKKSRLEEKIRE- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1546 ivgqetLRRENKNLQEEISNLTNQvregtKNLTEMEKVKKLIEQEKTevqvtLEETEGALERNESKILRFQLELLKAKAE 1625
Cdd:PRK01156 488 ------IEIEVKDIDEKIVDLKKR-----KEYLESEEINKSINEYNK-----IESARADLEDIKIKINELKDKHDKYEEI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1626 LERKLSEKDEELENfRRKQQCTIDSMQSSLDSEAksrieatrLKKKMEEdlnemelqlscANRQVSEATKSLGQLQIQIK 1705
Cdd:PRK01156 552 KNRYKSLKLEDLDS-KRTSWLNALAVISLIDIET--------NRSRSNE-----------IKKQLNDLESRLQEIEIGFP 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1706 DLQMQLDDSTQlnsDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRrlseEELLEATERINLFYTQNTSLLSQKKKLE 1785
Cdd:PRK01156 612 DDKSYIDKSIR---EIENEANNLNNKYNEIQENKILIEKLRGKIDNYK----KQIAEIDSIIPDLKEITSRINDIEDNLK 684
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411134203 1786 ADVAQMQKeaeevvqecqnaeekakkaatEAANLSEelkkKQDTIAHLEKTRENMEQTITDLQKRLAEAEQ 1856
Cdd:PRK01156 685 KSRKALDD---------------------AKANRAR----LESTIEILRTRINELSDRINDINETLESMKK 730
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1045-1283 |
4.83e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1045 KLNRAAkvVQEAHQQtLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHK-LEGDLKLNQESMENL 1123
Cdd:PHA02562 170 KLNKDK--IRELNQQ-IQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKtIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1124 ESSQRHLAEELRKKELENSQMNSKVENekglVAQLQKMVKELQT------QIKDLKEKLEAERTTRAKMEKERADLTQDL 1197
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQ----FQKVIKMYEKGGVcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1198 ADLNERLEEVGGASLAQLEITKKQETKFQKLRRDMEEAtLHFEATSASLKKRHADSLAELEGqvenLQQVKQKLEKDRSD 1277
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKA-KKVKAAIEELQAEFVDNAEELAK----LQDELDKIVKTKSE 397
|
....*.
gi 1411134203 1278 LQLEVD 1283
Cdd:PHA02562 398 LVKEKY 403
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1157-1414 |
5.72e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1157 QLQKMVKELQ----TQIKDLKEKLEAERTTrakmekeraDLTQDLADLNERLEEVGGA-SLAQLEITKKQETKFQKLrrd 1231
Cdd:PRK05771 17 YKDEVLEALHelgvVHIEDLKEELSNERLR---------KLRSLLTKLSEALDKLRSYlPKLNPLREEKKKVSVKSL--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1232 mEEATLHFEATSASLkkrhADSLAELEGQVENLQQVKQKLEKDRSDLQ------LEVDDLLTR-----------IEQMTR 1294
Cdd:PRK05771 85 -EELIKDVEEELEKI----EKEIKELEEEISELENEIKELEQEIERLEpwgnfdLDLSLLLGFkyvsvfvgtvpEDKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1295 AKANAEKLCTLYEERLNE--------ANAKLDKVTQLANDLAAQKTELwSESGEFLRRLEEKEALINQLSREKSNFTRQI 1366
Cdd:PRK05771 160 LKLESDVENVEYISTDKGyvyvvvvvLKELSDEVEEELKKLGFERLEL-EEEGTPSELIREIKEELEEIEKERESLLEEL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1411134203 1367 EELRGQLEKEtksqsalahalqkaQRDCDLLREQYEEEQEVKAELHRT 1414
Cdd:PRK05771 239 KELAKKYLEE--------------LLALYEYLEIELERAEALSKFLKT 272
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1687-1927 |
5.86e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1687 NRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQ---VAVAERRNSLLQsELEDLRSLQEQTERGRRLSEEELLEA 1763
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglVDLSEEAKLLLQ-QLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1764 TERINLFYTQNTSLLS--QKKKLEADVAQMQKEAEEvvqecqnaeekakkaateaanLSEELKKKQDTIAHLEKTRENME 1841
Cdd:COG3206 246 RAQLGSGPDALPELLQspVIQQLRAQLAELEAELAE---------------------LSARYTPNHPDVIALRAQIAALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1842 QTITDLQKRLAEAEQTALMGSRKQIQKLESRVRelegELEGEIRRSAEAQRGARRLERcikeltyQAEEDKKNLSRMQTQ 1921
Cdd:COG3206 305 AQLQQEAQRILASLEAELEALQAREASLQAQLA----QLEARLAELPELEAELRRLER-------EVEVARELYESLLQR 373
|
....*.
gi 1411134203 1922 MDKLQL 1927
Cdd:COG3206 374 LEEARL 379
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1552-1803 |
6.34e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1552 LRRENKNLQEEISNLTNQVREGTKNL-----TEMEKVKKLIEQ---EKTEVQVTLEETEGALE----RNESKI------- 1612
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAEPSRLyslyeKEIEDLRRQLDTltvERARLQLELDNLRLAAEdfrqKYEDELnlrtsae 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1613 -----LRFQL-ELLKAKAELERKLSEKDEELENFRRKQQCTIDSMQSSL-DSEAKSRIEATRlKKKMEEDLNEMELQLSC 1685
Cdd:pfam00038 103 ndlvgLRKDLdEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsDTQVNVEMDAAR-KLDLTSALAEIRAQYEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1686 -ANRQVSEATKslgQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRlseeellEAT 1764
Cdd:pfam00038 182 iAAKNREEAEE---WYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLA-------ETE 251
|
250 260 270
....*....|....*....|....*....|....*....
gi 1411134203 1765 ERINLFYTQNTSLLSQkkkLEADVAQMQKEAEEVVQECQ 1803
Cdd:pfam00038 252 ERYELQLADYQELISE---LEAELQETRQEMARQLREYQ 287
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1439-1856 |
6.84e-04 |
|
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: 44.68 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1439 DLEDAKKELAIRLQETAEAMGVANARNASLERARHRLQ-----LELGDALSDLGKVRSAAARLDQKQLQS---------- 1503
Cdd:pfam05622 4 EAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQerldqLESGDDSGTPGGKKYLLLQKQLEQLQEenfrletard 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1504 ---------GKALADWKQKHEESQTLLDasrkEIQALSTELLKLKHA-------------YKESIVGQETLRRENKNLQE 1561
Cdd:pfam05622 84 dyrikceelEKEVLELQHRNEELTSLAE----EAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1562 EISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQvtleETEGALERNESKILRFQLELLKAKA-------ELERKLSEKD 1634
Cdd:pfam05622 160 RNAEYMQRTLQLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKLEEklealqkEKERLIIERD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1635 ---EELENFRRKQQCTIDSMQSSLDSEAKSRIEATRLKKKMEEDLNEMELQLSCANRQVSEATKslGQLQIQIKDLQMQL 1711
Cdd:pfam05622 236 tlrETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQE--GSYRERLTELQQLL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1712 DDSTQLNSDLKEQVAVAERRNSLLQSELEDL-RSLQEQTERgrrlseeelleaterinlfyTQNTSLLsqKKKLEadvAQ 1790
Cdd:pfam05622 314 EDANRRKNELETQNRLANQRILELQQQVEELqKALQEQGSK--------------------AEDSSLL--KQKLE---EH 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411134203 1791 MQKEAEevvqecqnaeekakkaateaanLSEELKKKQDTIAHLE-KTRENMEQTITDLQKRLAEAEQ 1856
Cdd:pfam05622 369 LEKLHE----------------------AQSELQKKKEQIEELEpKQDSNLAQKIDELQEALRKKDE 413
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
936-1348 |
6.93e-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: 44.50 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 936 QEKNDLilqLQAEQETLANVEEQCEWLIKSKIQLEARVKELSErveeeeeinseltaRGRKLEDECSELKKEIDDLEtml 1015
Cdd:pfam07888 41 QERAEL---LQAQEAANRQREKEKERYKRDREQWERQRRELES--------------RVAELKEELRQSREKHEELE--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1016 vksEKEKrttehkvknlteEVEFLNEDISKLNRAAKVVQEAHQQTLDDLhmeEEKLSSLSkanlkleQQVVGLEGALEQE 1095
Cdd:pfam07888 101 ---EKYK------------ELSASSEELSEEKDALLAQRAAHEARIREL---EEDIKTLT-------QRVLERETELERM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1096 RKARINCERELHKLEGDLKLNQESMENLESSQRHLAEELrkKELENSQmnskvenekglvAQLQKMVKELQTQIKDLKEK 1175
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF--QELRNSL------------AQRDTQVLQLQDTITTLTQK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1176 LEAERTTRAKMEKERADL--TQDLADLNERLEEVGGASLAQLEITKKQ-ETKFQKLRRDMEEATLHFEATSASLKKRHAD 1252
Cdd:pfam07888 222 LTTAHRKEAENEALLEELrsLQERLNASERKVEGLGEELSSMAAQRDRtQAELHQARLQAAQLTLQLADASLALREGRAR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1253 SLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLltRIEQMTRAKANAE-------KLCTLYEER--LNEANAKLDKVTQL 1323
Cdd:pfam07888 302 WAQERETLQQSAEADKDRIEKLSAELQRLEERL--QEERMEREKLEVElgrekdcNRVQLSESRreLQELKASLRVAQKE 379
|
410 420
....*....|....*....|....*
gi 1411134203 1324 ANDLAAQKTELWsesgEFLRRLEEK 1348
Cdd:pfam07888 380 KEQLQAEKQELL----EYIRQLEQR 400
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1511-1675 |
7.21e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1511 KQKHEESQTLLDASRKEIQALSTEllKLKHAYKESIVGQETLRRENKNLQEEISNLTNQVREGTKNLtemEKVKKLIEQE 1590
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKE--ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENL---DRKLELLEKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1591 KTEvqvtleetegaLERNESKILRFQLELLKAKAELERKLSEKDEELENfrrkqqctIDSMQSS------LDS-EAKSRI 1663
Cdd:PRK12704 109 EEE-----------LEKKEKELEQKQQELEKKEEELEELIEEQLQELER--------ISGLTAEeakeilLEKvEEEARH 169
|
170
....*....|..
gi 1411134203 1664 EATRLKKKMEED 1675
Cdd:PRK12704 170 EAAVLIKEIEEE 181
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1672-1976 |
7.38e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1672 MEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDL----QMQLDDSTQLNSDLKEQVAVAERRNSL----------LQS 1737
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLsieyNNAMDDYNNLKSALNELSSLEDMKNRYeseiktaesdLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1738 ELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVAQMQKEAE-----EVVQECQNAEEKAKKA 1812
Cdd:PRK01156 268 ELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAiikklSVLQKDYNDYIKKKSR 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1813 ATEAANLSEELKKKQD-------TIAHLEKTRENMEQTITDLQKRLAEAEQTALMGS----------RKQIQKLESRV-- 1873
Cdd:PRK01156 348 YDDLNNQILELEGYEMdynsylkSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPdaikkelneiNVKLQDISSKVss 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1874 ----RELEGELEGEIRRSAEAQRG--------------------------ARRLERCIKELTYQA---EEDKKNLSRMQT 1920
Cdd:PRK01156 428 lnqrIRALRENLDELSRNMEMLNGqsvcpvcgttlgeeksnhiinhynekKSRLEEKIREIEIEVkdiDEKIVDLKKRKE 507
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1411134203 1921 QMDKLQL-KVHNYKQQVEVAEAQanqyLSKYKKQQHELNEVKERAEVAESQVNKLKI 1976
Cdd:PRK01156 508 YLESEEInKSINEYNKIESARAD----LEDIKIKINELKDKHDKYEEIKNRYKSLKL 560
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1095-1642 |
7.70e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1095 ERKARINCERELHKLEGDLKLNQESMENLE---SSQRHLAEELRKKELENSQMNSKVENEKGLVAQLQKMVKELQTQIKD 1171
Cdd:PRK01156 150 QRKKILDEILEINSLERNYDKLKDVIDMLRaeiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNN 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1172 LKEK----------LEAERTTRAKMEKERADLTQDLADLNERLEEVGGASLAQLEITKKQETK-------FQKLRRDMEE 1234
Cdd:PRK01156 230 AMDDynnlksalneLSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKnrnyindYFKYKNDIEN 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1235 ATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDrsDLQLEVDDLLTRIEQMTRAKANAEKLCTLYEERLNEAN 1314
Cdd:PRK01156 310 KKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYD--DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1315 AKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLE---------------KETKS 1379
Cdd:PRK01156 388 RMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlGEEKS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1380 QSALAHALQKAQR---DCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQKTEDLEDAKKELAiRLQETAE 1456
Cdd:PRK01156 468 NHIINHYNEKKSRleeKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKIN-ELKDKHD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1457 AMGVANARNASLErarhrlqleLGDalsdlgkvrsaaarLDQKQLQSGKALAdwkqkhEESQTLLDASRKEIQALSTELL 1536
Cdd:PRK01156 547 KYEEIKNRYKSLK---------LED--------------LDSKRTSWLNALA------VISLIDIETNRSRSNEIKKQLN 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1537 KLKHAYKESIVGQETLRRENKN----LQEEISNLTNQVREGTKNLTEMEKVKKLIE-------------QEKTEVQVTLE 1599
Cdd:PRK01156 598 DLESRLQEIEIGFPDDKSYIDKsireIENEANNLNNKYNEIQENKILIEKLRGKIDnykkqiaeidsiiPDLKEITSRIN 677
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1411134203 1600 ETEGALERNESKI---------LRFQLELLKAK-AELERKLSEKDEELENFRR 1642
Cdd:PRK01156 678 DIEDNLKKSRKALddakanrarLESTIEILRTRiNELSDRINDINETLESMKK 730
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1717-1951 |
8.88e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1717 LNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRR--LSEEELLEATERINLFYTQNTSLLSQKKKLEADVAQMQKE 1794
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1795 AEEvvqecqnaeekakkaateaanLSEELKKKQDTIAHLEKTRE--NMEQTITDLQKRLAEAEQTALMGSRkQIQKLESR 1872
Cdd:COG3206 242 LAA---------------------LRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAELSARYTPNHP-DVIALRAQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1873 VRELEGELEGEIRRS-AEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQlkvhNYKQQVEVAEAQANQYLSKYK 1951
Cdd:COG3206 300 IAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR----RLEREVEVARELYESLLQRLE 375
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
1597-1766 |
9.16e-04 |
|
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: 43.48 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1597 TLEETEGALE------RNESKILRFQL----ELLKAKA------ELERKLSEKDEELENFRRKQQC-TIDSMQSSL---- 1655
Cdd:pfam04849 98 VLTERNEALEeqlgsaREEILQLRHELskkdDLLQIYSndaeesETESSCSTPLRRNESFSSLHGCvQLDALQEKLrgle 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1656 DSEAKSRIEATRLKKKMEE-DLNEMEL------QLSCANRQVSEATKSLG--------------QLQIQIKDLQMQLDDS 1714
Cdd:pfam04849 178 EENLKLRSEASHLKTETDTyEEKEQQLmsdcveQLSEANQQMAELSEELArkmeenlrqqeeitSLLAQIVDLQHKCKEL 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1411134203 1715 TQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATER 1766
Cdd:pfam04849 258 GIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
960-1993 |
9.37e-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: 44.66 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 960 EWLIKSKI--QLEARVKELSERVEEEEEINSELTARGRKLEDECSELKKEIDDLETMLVKSEKE-------KRTTEHKVK 1030
Cdd:TIGR01612 531 DQNIKAKLykEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEiiyinklKLELKEKIK 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1031 NLTEEVEFLNEDISklnraAKVVQEAHQQTLDDL-----HMEEEKLSSLSKANLKLEQQVVGL-EGALEQ--ERKARINC 1102
Cdd:TIGR01612 611 NISDKNEYIKKAID-----LKKIIENNNAYIDELakispYQVPEHLKNKDKIYSTIKSELSKIyEDDIDAlyNELSSIVK 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1103 ERELHKLEGDLKLnqesmENLESSQRHLAEELRKKELENSQMN-SKVENEKG-LVAQLQKMVKELQTQI-KDLKEKLEAE 1179
Cdd:TIGR01612 686 ENAIDNTEDKAKL-----DDLKSKIDKEYDKIQNMETATVELHlSNIENKKNeLLDIIVEIKKHIHGEInKDLNKILEDF 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1180 RTTrakmEKERADLTQDLADLNERLEeVGGASLAQLEITKKQETKFQKLRRdmEEATLHFEATSASLK--KRHADSLAEL 1257
Cdd:TIGR01612 761 KNK----EKELSNKINDYAKEKDELN-KYKSKISEIKNHYNDQINIDNIKD--EDAKQNYDKSKEYIKtiSIKEDEIFKI 833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1258 EGQVENLQqvkqklekdrsdlqlevDDLLTRIEQMTRAKANaeklctlYEERLNEANAKLdkvTQLANDLAAQKTElwSE 1337
Cdd:TIGR01612 834 INEMKFMK-----------------DDFLNKVDKFINFENN-------CKEKIDSEHEQF---AELTNKIKAEISD--DK 884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1338 SGEFLRRLEEKEALINQLSREKSNFTRQIEELRgQLEKETKSQSALAHALQKAQRDCDLLREQYEeeQEVKaelhrTLSK 1417
Cdd:TIGR01612 885 LNDYEKKFNDSKSLINEINKSIEEEYQNINTLK-KVDEYIKICENTKESIEKFHNKQNILKEILN--KNID-----TIKE 956
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1418 VNAEMVQWRMKYENNVIQKTEDLEDAKKELAIRLQEtaeamgvanARNASLERARHRLQLELGDAlsdlgKVRSAAARLD 1497
Cdd:TIGR01612 957 SNLIEKSYKDKFDNTLIDKINELDKAFKDASLNDYE---------AKNNELIKYFNDLKANLGKN-----KENMLYHQFD 1022
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1498 QKQlqsgKALADWKQKHEE-------------------SQTLLDASRKEIQALSTELL---------------KLKHAYK 1543
Cdd:TIGR01612 1023 EKE----KATNDIEQKIEDanknipnieiaihtsiyniIDEIEKEIGKNIELLNKEILeeaeinitnfneikeKLKHYNF 1098
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1544 ESIVGQETLRRENK--NLQEEISNLTNQVREGTKNLTEME-KVKKLIEQEKTEVQVTLEETEGALERNESKILRFQLELL 1620
Cdd:TIGR01612 1099 DDFGKEENIKYADEinKIKDDIKNLDQKIDHHIKALEEIKkKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENI 1178
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1621 KAKAELERKLSEKDEELENfrrkQQCTIDSMQSSLDseaksriEATRLKKKMEEDLNEMELQLSCANRQVSEATksLGQL 1700
Cdd:TIGR01612 1179 VTKIDKKKNIYDEIKKLLN----EIAEIEKDKTSLE-------EVKGINLSYGKNLGKLFLEKIDEEKKKSEHM--IKAM 1245
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1701 QIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEeelleaterinlfyTQNTSL-LS 1779
Cdd:TIGR01612 1246 EAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISD--------------IREKSLkII 1311
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1780 QKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELK--KKQDTIAHLEKTRENMEQTITDLQKRLAEAEQt 1857
Cdd:TIGR01612 1312 EDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKlnKIKKIIDEVKEYTKEIEENNKNIKDELDKSEK- 1390
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1858 aLMGSRKQIQKLESrvrelegelegeIRRSAEAQRGARRLERCIKELTyqaeEDKKNLSRMQTQMDKLQLKVHNYKQQV- 1936
Cdd:TIGR01612 1391 -LIKKIKDDINLEE------------CKSKIESTLDDKDIDECIKKIK----ELKNHILSEESNIDTYFKNADENNENVl 1453
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411134203 1937 ------EVAEAQAnQYLSKYKKQQ------HELNEVKERAEVA-----ESQVNKLKI-KAREFGKKVRQAQTELL 1993
Cdd:TIGR01612 1454 llfkniEMADNKS-QHILKIKKDNatndhdFNINELKEHIDKSkgckdEADKNAKAIeKNKELFEQYKKDVTELL 1527
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1317-1632 |
1.04e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1317 LDKVTQLANDLAAQKTELwsesgeflRRLEEKEAliNQLSREKSNFTRQIEELRGQLEKETKSQSALAHALQKAQRDCDL 1396
Cdd:pfam00038 17 IDKVRFLEQQNKLLETKI--------SELRQKKG--AEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1397 LREQYEEE----QEVKAELHrTLSKVNAEMVQWRMKYENNVIQKTEDLEDAKKELAIRLQETAEAMGVANaRNASLERAR 1472
Cdd:pfam00038 87 FRQKYEDElnlrTSAENDLV-GLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQ-VNVEMDAAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1473 hrlQLELGDALSDLGKVRSAAARLDQKQLQsgkalADWKQKHEESQTLLDASRKEIQALSTELLKLKHAYkesivgqETL 1552
Cdd:pfam00038 165 ---KLDLTSALAEIRAQYEEIAAKNREEAE-----EWYQSKLEELQQAAARNGDALRSAKEEITELRRTI-------QSL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1553 RRENKNLQEEISNLTNQVREgtknltemekvkklieqektevqvtLEET-EGALERNESKILRFQLELLKAKAELERKLS 1631
Cdd:pfam00038 230 EIELQSLKKQKASLERQLAE-------------------------TEERyELQLADYQELISELEAELQETRQEMARQLR 284
|
.
gi 1411134203 1632 E 1632
Cdd:pfam00038 285 E 285
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1252-1424 |
1.05e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1252 DSLAELEGQVENLQQvKQKLEKDRS-DLQLEVDDLLTRIEQmtrAKANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQ 1330
Cdd:PRK09039 53 SALDRLNSQIAELAD-LLSLERQGNqDLQDSVANLRASLSA---AEAERSRLQALLAELAGAGAAAEGRAGELAQELDSE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1331 KTElwseSGEFLRRLEekeaLINQlsreksnftrQIEELRGQLeketksqSALAHALQKAqrdcdllrEQYEEEQEVK-A 1409
Cdd:PRK09039 129 KQV----SARALAQVE----LLNQ----------QIAALRRQL-------AALEAALDAS--------EKRDRESQAKiA 175
|
170
....*....|....*
gi 1411134203 1410 ELHRTLSKVNAEMVQ 1424
Cdd:PRK09039 176 DLGRRLNVALAQRVQ 190
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1623-1858 |
1.21e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1623 KAELERKLSEKDEELENFRRKqqctIDSMQSSLDsEAKSRIEATRLK-KKMEEDLNEMELQLSCANRQVSEATKSLGQlq 1701
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAE----LDALQAELE-ELNEEYNELQAElEALQAEIDKLQAEIAEAEAEIEERREELGE-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1702 iQIKDLQMQLDDSTQLN--------SDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATErinlfytQ 1773
Cdd:COG3883 91 -RARALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA-------L 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1774 NTSLLSQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAE 1853
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
....*
gi 1411134203 1854 AEQTA 1858
Cdd:COG3883 243 AASAA 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1472-1904 |
1.21e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1472 RHRLQLELGDALSDLGKVRSAAARLDQKQLQSG-KALADWKQKHEESQTL---LDASRKEIQALSTELLKLKH--AYKES 1545
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELeEELKEAEEKEEEYAELqeeLEELEEELEELEAELEELREelEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1546 IVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKILRFQLELLKAKAE 1625
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1626 LERKLSEKDEELENFRRKqqctIDSMQSSLDseaksRIEATRLKKKMEEDLNEMELQL--------------SCANRQVS 1691
Cdd:COG4717 204 LQQRLAELEEELEEAQEE----LEELEEELE-----QLENELEAAALEERLKEARLLLliaaallallglggSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1692 EATKSLGQLQIQIKDLQMQLDDSTQLNSDLkEQVAVAERRNSLLQSELEDLRS----------------LQEQTERGRRL 1755
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEA-EELQALPALEELEEEELEELLAalglppdlspeellelLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1756 SEEELLEATERINLFYTQNTSLLSQKK-KLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKKK-----QDT 1829
Cdd:COG4717 354 REAEELEEELQLEELEQEIAALLAEAGvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeeelEEE 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411134203 1830 IAHLEKTRENMEQTITDLQKRLAEAE-QTALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKEL 1904
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEaELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
998-1326 |
1.24e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 998 EDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAkvvqeahQQTLDDLHME-EEKLSSLSK 1076
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLA-------DETLADRVEEiREQLDEAEE 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1077 ANLKLEQQVVGLEgALEQERKARINCERELHKLEGDLKLNQESMENLESSQRHLAEEL-RKKELENSQMNSKVENEKGLV 1155
Cdd:PRK04863 909 AKRFVQQHGNALA-QLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVqRRAHFSYEDAAEMLAKNSDLN 987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1156 AQLQKMVKELQTQIKDLKEKLeaeRTTRAKMekerADLTQDLADLnerleevggaslaQLEITKKQETkFQKLRRDMEEA 1235
Cdd:PRK04863 988 EKLRQRLEQAEQERTRAREQL---RQAQAQL----AQYNQVLASL-------------KSSYDAKRQM-LQELKQELQDL 1046
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1236 TLHFEATSASLKKRHADslaELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRakanaeKLCTLYEERLNeANA 1315
Cdd:PRK04863 1047 GVPADSGAEERARARRD---ELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLER------DYHEMREQVVN-AKA 1116
|
330
....*....|.
gi 1411134203 1316 KLDKVTQLAND 1326
Cdd:PRK04863 1117 GWCAVLRLVKD 1127
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1250-1467 |
1.31e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1250 HADS-LAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRI----EQMTRAKANAEKLctlyEERLNEANAKLDK-VTQL 1323
Cdd:COG3883 13 FADPqIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelqAELEALQAEIDKL----QAEIAEAEAEIEErREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1324 ANDLAAQKTE----------LWSES-GEFLRRL-------EEKEALINQLSREK---SNFTRQIEELRGQLEKETKSQSA 1382
Cdd:COG3883 89 GERARALYRSggsvsyldvlLGSESfSDFLDRLsalskiaDADADLLEELKADKaelEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1383 LAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQKTEDLEDAKKELAIRLQETAEAMGVAN 1462
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
....*
gi 1411134203 1463 ARNAS 1467
Cdd:COG3883 249 AGAAG 253
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1577-1673 |
1.65e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1577 LTEMEKVKKLIEQEKTEVQVTLEETEGALERNESKILRFQLELLKA-KAELERKLSEKDEELENFRRKqqctIDSMQSSL 1655
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAeVEELEAELEEKDERIERLERE----LSEARSEE 457
|
90
....*....|....*...
gi 1411134203 1656 DSEAKSRIEATRLKKKME 1673
Cdd:COG2433 458 RREIRKDREISRLDREIE 475
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
908-1140 |
1.73e-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: 42.83 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 908 EECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQcewlIKskiQLEARVKelserveeeeEIN 987
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR----IR---ALEQELA----------ALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 988 SELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKV----KNLTEEVEFLnEDISKLNRAAKVVQEAHQQTLDD 1063
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRL-QYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411134203 1064 LHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARincERELHKLEGDLKLNQESMENLESSQRHLAEELRKKELE 1140
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1700-2004 |
1.89e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1700 LQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLS 1779
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1780 QKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQTAL 1859
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1860 MGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVHNYKQQVEVA 1939
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1411134203 1940 EAQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVRQAQTELLVTLQGSKRIVS 2004
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1152-1302 |
1.93e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.74 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1152 KGLVAQLQKMVKELQTQIKDLKEKLeaeRTTRAKMEKERADLTQDLADLNERLEEVGGAsLAQLEItkkqetkfQKLRRD 1231
Cdd:cd22656 120 KALLDDLLKEAKKYQDKAAKVVDKL---TDFENQTEKDQTALETLEKALKDLLTDEGGA-IARKEI--------KDLQKE 187
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411134203 1232 MEEATlhfEATSASLKKRhadsLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRAKANAEKL 1302
Cdd:cd22656 188 LEKLN---EEYAAKLKAK----IDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEKL 251
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1763-1991 |
2.06e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1763 ATERINLFYTQNTSLLSQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKKKQdtiAHLEKTRENMEQ 1842
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1843 TITDLQKRLAEAEQ-TALMGSrKQIQKLESRVrelegeleGEIRRSAEAQRgaRRLERcIKELTYQAEEDKKNLSRMQTQ 1921
Cdd:COG3883 91 RARALYRSGGSVSYlDVLLGS-ESFSDFLDRL--------SALSKIADADA--DLLEE-LKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1922 MDKLQLKVHNYKQQVEVAEAQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVRQAQTE 1991
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
1888-1996 |
2.22e-03 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 40.55 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1888 AEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVHNYKQQVEVA-------EAQANQYLSKYKK-QQHELN- 1958
Cdd:pfam06009 6 REANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAgrsvkklEELAPDLLDKLKPlKQLEVNs 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1411134203 1959 --------EVKERAEVAESQVNKLKIKAREFGKKVRQAQTELLVTL 1996
Cdd:pfam06009 86 sslsdnisRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTD 131
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1128-1411 |
2.42e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.71 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1128 RHLAEELRKKELENSQmnskveNEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEV 1207
Cdd:pfam05667 211 RNAAELAAAQEWEEEW------NSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSF 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1208 GGASLAQLEITKK-QETKFQKLRRDMEEATLHFEATSAS-----LKKRHADSLAELEGQVENLQQVKQKLEKDRSDLQLE 1281
Cdd:pfam05667 285 SGSSTTDTGLTKGsRFTHTEKLQFTNEAPAATSSPPTKVeteeeLQQQREEELEELQEQLEDLESSIQELEKEIKKLESS 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1282 vddlltrIEQMTRAKANaeklctlyEERLNEANAKLDKVTQLANDLAAQKTElwsesgeflrRLEEKEALINQLSREKSN 1361
Cdd:pfam05667 365 -------IKQVEEELEE--------LKEQNEELEKQYKVKKKTLDLLPDAEE----------NIAKLQALVDASAQRLVE 419
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1411134203 1362 FTRQIEELRGQLEKETKS-QSALAHALQKAQRDCDLLREQYEEEQEVKAEL 1411
Cdd:pfam05667 420 LAGQWEKHRVPLIEEYRAlKEAKSNKEDESQRKLEEIKELREKIKEVAEEA 470
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1625-1993 |
2.52e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1625 ELERKLSEKDEELENFRRKQQCTIDSMQSSLDSEAKSRIEATRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQI 1704
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1705 KDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKL 1784
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1785 EADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKKKQdtIAHLEKTRENMEQTITDLQKRLAEAEQTALMGSRK 1864
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEA--EKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1865 QIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKE-LTYQAEEDKKNLSRMQTQMDKLQLKVHNYKQQVEVAEAQA 1943
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEiAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1944 NQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVRQAQTELL 1993
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1089-1801 |
2.78e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1089 EGALEQERKARINCERElhklegDLKLNQESMENLESSQRHLAEELRKKELENSQMNSKV------------------EN 1150
Cdd:pfam10174 44 ERALRKEEAARISVLKE------QYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFttspvdgedkfstpelteEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1151 EKGLVAQLQKMVKELQTQIKDLKEkleaertTRAKMEKERADLTQDLADLNERLEEVGGASLaqleiTKKQETKFQKLRR 1230
Cdd:pfam10174 118 FRRLQSEHERQAKELFLLRKTLEE-------MELRIETQKQTLGARDESIKKLLEMLQSKGL-----PKKSGEEDWERTR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1231 DMEEATLHFEATSASLKKRHADSLAELEGQ------------VENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMtraKAN 1298
Cdd:pfam10174 186 RIAEAEMQLGHLEVLLDQKEKENIHLREELhrrnqlqpdpakTKALQTVIEMKDTKISSLERNIRDLEDEVQML---KTN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1299 AEKLCTLYEERL-------NEANAKLDKVTQLANDLAAQKTELWSesgeflrrLEEK-EALINQLSREKsnftRQIEELR 1370
Cdd:pfam10174 263 GLLHTEDREEEIkqmevykSHSKFMKNKIDQLKQELSKKESELLA--------LQTKlETLTNQNSDCK----QHIEVLK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1371 GQLEKETKSQSALahalqkaQRDCDLLREQYEEEQEVKAELHRTLSKVNAE-------------MVQWRMKYENNVIQKT 1437
Cdd:pfam10174 331 ESLTAKEQRAAIL-------QTEVDALRLRLEEKESFLNKKTKQLQDLTEEkstlageirdlkdMLDVKERKINVLQKKI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1438 EDLEDAKKELAIRLQETAEAMGVANARNASLERARHRLQLELGDALSDLGKVRSAAARLDQKQLQSgkaLADWKQKHEES 1517
Cdd:pfam10174 404 ENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEE---LESLKKENKDL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1518 QTLLDASRKEIQALSTELLKLKHayKESIVGQETLRRENKNLQEEIsNLTNQVREGTKNLTEMEKVkklieQEKTEVQVT 1597
Cdd:pfam10174 481 KEKVSALQPELTEKESSLIDLKE--HASSLASSGLKKDSKLKSLEI-AVEQKKEECSKLENQLKKA-----HNAEEAVRT 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1598 LEETEGALERNESKILRFQLELLKAKAELERkLSEKDEELENFRRKQQCTIDSMQSSLDSEAKSR-IEATRLKKKMEEDL 1676
Cdd:pfam10174 553 NPEINDRIRLLEQEVARYKEESGKAQAEVER-LLGILREVENEKNDKDKKIAELESLTLRQMKEQnKKVANIKHGQQEMK 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1677 NEMELQLSCANRQVSEATKSlgQLQIQIKDLQMQLDDSTQLNSDLKE-----QVAVAERRNSLLQSELEDLRSLQEQTEr 1751
Cdd:pfam10174 632 KKGAQLLEEARRREDNLADN--SQQLQLEELMGALEKTRQELDATKArlsstQQSLAEKDGHLTNLRAERRKQLEEILE- 708
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1411134203 1752 grrLSEEELLEATERINlfytQNTSLL----SQKKKLEADVAQMQKEAEEVVQE 1801
Cdd:pfam10174 709 ---MKQEALLAAISEKD----ANIALLelssSKKKKTQEEVMALKREKDRLVHQ 755
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1124-1294 |
3.14e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1124 ESSQRHLAEELRKKELENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEaerttrakmEKERAdltqdladlNER 1203
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELE---------EKDER---------IER 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1204 LEEvggaslaqlEITKKQETKFQKLRRDMEEATLhfEATSASLKKRhadsLAELEGQVENLqqvKQKLEKDRSDLQLEVD 1283
Cdd:COG2433 446 LER---------ELSEARSEERREIRKDREISRL--DREIERLERE----LEEERERIEEL---KRKLERLKELWKLEHS 507
|
170
....*....|....
gi 1411134203 1284 DLLT---RIEQMTR 1294
Cdd:COG2433 508 GELVpvkVVEKFTK 521
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
997-1510 |
3.23e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 997 LEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSK 1076
Cdd:COG5185 84 KARKFLKEKKLDTKILQEYVNSLIKLPNYEWSADILISLLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVETGIIKD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1077 ANLKLEQQVVglEGALEQERKARINCER----ELHKLEGD-----LKLNQESMENLESSQRHLAEELrKKELENSQMNSK 1147
Cdd:COG5185 164 IFGKLTQELN--QNLKKLEIFGLTLGLLkgisELKKAEPSgtvnsIKESETGNLGSESTLLEKAKEI-INIEEALKGFQD 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1148 VENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAK-MEKERADLTQDLADLNERLEEvggaSLAQLEITKKQETKFQ 1226
Cdd:COG5185 241 PESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKrLNENANNLIKQFENTKEKIAE----YTKSIDIKKATESLEE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1227 KLRRdmeeatlhfeatsASLKKRHADSLAELEgqvENLQQVKQKLEKDRSDLQlevddlltriEQMTRAKANAEKLCTLY 1306
Cdd:COG5185 317 QLAA-------------AEAEQELEESKRETE---TGIQNLTAEIEQGQESLT----------ENLEAIKEEIENIVGEV 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1307 EERLNEANAKLDKVTqlandLAAQKTELwsesGEFLRRLEEKEALINQ-LSREKSNFTRQIEELRGQLEKETKSQSALAH 1385
Cdd:COG5185 371 ELSKSSEELDSFKDT-----IESTKESL----DEIPQNQRGYAQEILAtLEDTLKAADRQIEELQRQIEQATSSNEEVSK 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1386 ALQKAQRDCDLLReqyeeeqevkaelHRTLSKVNAEMVQWRMKYENNVIQKTEDLEDAKKELAIRLQETAEAMGVANAR- 1464
Cdd:COG5185 442 LLNELISELNKVM-------------READEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKl 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1411134203 1465 NASLERAR---HRLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADW 1510
Cdd:COG5185 509 ERQLEGVRsklDQVAESLKDFMRARGYAHILALENLIPASELIQASNAK 557
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1216-1389 |
3.88e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1216 EITKKQETKFQKLRRDMEeatlhfeatsaslkKRHADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRA 1295
Cdd:PRK12704 57 EALLEAKEEIHKLRNEFE--------------KELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1296 KANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQktelwsesgEFLRRLEEKealinqLSREKSNFTRQIEElRGQLEK 1375
Cdd:PRK12704 123 QQELEKKEEELEELIEEQLQELERISGLTAEEAKE---------ILLEKVEEE------ARHEAAVLIKEIEE-EAKEEA 186
|
170
....*....|....
gi 1411134203 1376 ETKSQSALAHALQK 1389
Cdd:PRK12704 187 DKKAKEILAQAIQR 200
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
989-1137 |
3.88e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 989 ELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQqtLDDLHMEE 1068
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE--YEALQKEI 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1411134203 1069 EklsSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMENLESSQRHLAEELRKK 1137
Cdd:COG1579 99 E---SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1664-1844 |
3.99e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1664 EATRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVA--ERRNSLLQSELED 1741
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1742 LRSLQEQTergrrlsEEELLEATERINlfytqntSLLSQKKKLEADVAQMQKEAEEVVQEcqnaeekakkaateaanLSE 1821
Cdd:COG1579 101 LKRRISDL-------EDEILELMERIE-------ELEEELAELEAELAELEAELEEKKAE-----------------LDE 149
|
170 180
....*....|....*....|...
gi 1411134203 1822 ELKKKQDTIAHLEKTRENMEQTI 1844
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKI 172
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1254-1522 |
4.07e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1254 LAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRAKANAeklctlyEERLNEANAKLDKVTQLANDLAAQKTE 1333
Cdd:pfam00038 56 IEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSA-------ENDLVGLRKDLDEATLARVDLEAKIES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1334 LwSESGEFLRRLEEKEalINQLsreksnfTRQIEELRGQLEKETKSQSALAHALQKaqrdcdlLREQYEEEQEvkaelhr 1413
Cdd:pfam00038 129 L-KEELAFLKKNHEEE--VREL-------QAQVSDTQVNVEMDAARKLDLTSALAE-------IRAQYEEIAA------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1414 tLSKVNAEMvQWRMKYEN---NVIQKTEDLEDAKKELA---IRLQE-TAEAMGVANArNASLERARHRLQLELGDALSDL 1486
Cdd:pfam00038 185 -KNREEAEE-WYQSKLEElqqAAARNGDALRSAKEEITelrRTIQSlEIELQSLKKQ-KASLERQLAETEERYELQLADY 261
|
250 260 270
....*....|....*....|....*....|....*.
gi 1411134203 1487 gkvRSAAARLDQkQLQSGKalADWKQKHEESQTLLD 1522
Cdd:pfam00038 262 ---QELISELEA-ELQETR--QEMARQLREYQELLN 291
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1662-2020 |
4.14e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1662 RIEATRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKdlqmQLDDSTQLNSDLKEQVAVAERRNSLLQSELED 1741
Cdd:pfam02463 194 ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEE----RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1742 LRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEadvaqmqKEAEEVVQECQNAEEKAKKAATEAANLSE 1821
Cdd:pfam02463 270 VLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE-------EKLKESEKEKKKAEKELKKEKEEIEELEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1822 ELKKKQDTIAHLEKTRENMEQtitdLQKRLAEAEQTALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCI 1901
Cdd:pfam02463 343 ELKELEIKREAEEEEEEELEK----LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLE 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1902 KELTYQAEEDKKNLSRMQTQMDKLQLKVHNYKQQVEVAEAQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREF 1981
Cdd:pfam02463 419 DLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
330 340 350
....*....|....*....|....*....|....*....
gi 1411134203 1982 GKKVRQAQTELLVTLQGSKRIVSPALKGQQLEKYKEGAV 2020
Cdd:pfam02463 499 SQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVA 537
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1735-1972 |
4.21e-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: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1735 LQSELEDLRSLQEQTERGRRlsEEELLEATERINLFYTQNTSLLSQKKKLEA--DVAQMQKEAEEVVQECQNaeekakka 1812
Cdd:COG4913 230 LVEHFDDLERAHEALEDARE--QIELLEPIRELAERYAAARERLAELEYLRAalRLWFAQRRLELLEAELEE-------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1813 ateaanLSEELKKKQDTIAHLEKTRENMEQTITDLQKRLAEAEQtalmgsrKQIQKLEsrvreleGELEGEIRRSAEAQR 1892
Cdd:COG4913 300 ------LRAELARLEAELERLEARLDALREELDELEAQIRGNGG-------DRLEQLE-------REIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1893 GARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVHNYKQQVEVAEAQANQYLSKYKKQQHELNEvkERAEVAESQVN 1972
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA--EIASLERRKSN 437
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
996-1189 |
4.52e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 996 KLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTlddlhmeEEKLSSLS 1075
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY-------EEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1076 KAnlkleqqvvglegaleqerkarinceRELHKLEGDLKLNQESMENLESSQRHLAEELRKKELENSQMNSKVENEKGLV 1155
Cdd:COG1579 87 NN--------------------------KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190
....*....|....*....|....*....|....
gi 1411134203 1156 AQLQkmvKELQTQIKDLKEKLEAERTTRAKMEKE 1189
Cdd:COG1579 141 EEKK---AELDEELAELEAELEELEAEREELAAK 171
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
996-1152 |
4.93e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 996 KLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAK----------VVQEAhqQTLDDLH 1065
Cdd:COG3883 41 ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsggsvsyldVLLGS--ESFSDFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1066 MEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMENLESSQRHLAEELRKKELENSQMN 1145
Cdd:COG3883 119 DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
....*..
gi 1411134203 1146 SKVENEK 1152
Cdd:COG3883 199 AELEAEL 205
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1229-1646 |
4.98e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1229 RRDMEEATLHFEATSASLKK-------RHADSLAELEGQVENLQQVKQKLEKDRSDLQL----------------EVDDL 1285
Cdd:PRK04863 281 RRVHLEEALELRRELYTSRRqlaaeqyRLVEMARELAELNEAESDLEQDYQAASDHLNLvqtalrqqekieryqaDLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1286 LTRIEQMTRAKANAEKLCTLYEERLNEANAKLDKV-TQLAN---DLAAQKTElwseSGEF---LRRLEEKEALINQLSRE 1358
Cdd:PRK04863 361 EERLEEQNEVVEEADEQQEENEARAEAAEEEVDELkSQLADyqqALDVQQTR----AIQYqqaVQALERAKQLCGLPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1359 KSNFTRQIEELRGQLEKETKSQSALAHALqkaqRDCDLLREQYEEEQEVkaelhrtLSKVNAEMVqwRMKYENNVIQKTE 1438
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKL----SVAQAAHSQFEQAYQL-------VRKIAGEVS--RSEAWDVARELLR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1439 DLEDAKkELAIRLQEtaeamgvanarnaslerarhrLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADwkqkHEESQ 1518
Cdd:PRK04863 504 RLREQR-HLAEQLQQ---------------------LRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD----EDELE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1519 TLLDASRKEIQALSTELlklkhayKESIVGQETLRRENKNLQEEISNLTNQvreGTKNLTEMEKVKKLIEQekteVQVTL 1598
Cdd:PRK04863 558 QLQEELEARLESLSESV-------SEARERRMALRQQLEQLQARIQRLAAR---APAWLAAQDALARLREQ----SGEEF 623
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1411134203 1599 EETEGAlerneskilrfqLELLKAKAELERKLSEKDEELEnfRRKQQC 1646
Cdd:PRK04863 624 EDSQDV------------TEYMQQLLERERELTVERDELA--ARKQAL 657
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
822-1322 |
5.02e-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: 42.05 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 822 GFLGQLEAMRDERLSKVFTLFQARAQGKLMRIKFQKILEERDALILIQWNIRAFMAVKnwawmrlffkIKPLVKSSERGE 901
Cdd:pfam07111 173 GLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQ----------VPPEVHSQTWEL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 902 EIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQ----EKNDLILQLQAEQETLANVEEQCEWLIKSkiqlearvkels 977
Cdd:pfam07111 243 ERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHmlalQEEELTRKIQPSDSLEPEFPKKCRSLLNR------------ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 978 eRVEEEEEINSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAH 1057
Cdd:pfam07111 311 -WREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEAR 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1058 QQTLDDLHMEEEKL----SSLSKANLKLEQQVVGLEGALEQ--ERKARIN-CERELHKLEGdLKLNQESMENLESSQRHL 1130
Cdd:pfam07111 390 RRQQQQTASAEEQLkfvvNAMSSTQIWLETTMTRVEQAVARipSLSNRLSyAVRKVHTIKG-LMARKVALAQLRQESCPP 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1131 AEELRKKELENS-QMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAK----MEKERADLTQDLADLNERLE 1205
Cdd:pfam07111 469 PPPAPPVDADLSlELEQLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEvaqqLEQELQRAQESLASVGQQLE 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1206 EV---------GGASLAQlEITKKQETKFQKLRRDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRs 1276
Cdd:pfam07111 549 VArqgqqesteEAASLRQ-ELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEK- 626
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1411134203 1277 dlqlEVDDLLTRIEQMTRaKANAEKLCTLYEERLNEANAKLDKVTQ 1322
Cdd:pfam07111 627 ----ERNQELRRLQDEAR-KEEGQRLARRVQELERDKNLMLATLQQ 667
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
986-1285 |
5.12e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 986 INSELTARGRKLEDECSELKKEIDDLETMLVKSEKekrttehkvknlteEVEFLNE-DISKLNRAAKVV--QEAHQQTLD 1062
Cdd:PLN02939 108 IAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEK--------------NILLLNQaRLQALEDLEKILteKEALQGKIN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1063 DLHM------EEEKLSSLSKANLK-LEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMEN----LESSQRHLA 1131
Cdd:PLN02939 174 ILEMrlsetdARIKLAAQEKIHVEiLEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDdiqfLKAELIEVA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1132 ---EELRKKELENSQMNSKV-ENEKGLVAQLQKMVKELQTQIKDLKEKLE--AERTTRAKMEKERADLT----QDLADLN 1201
Cdd:PLN02939 254 eteERVFKLEKERSLLDASLrELESKFIVAQEDVSKLSPLQYDCWWEKVEnlQDLLDRATNQVEKAALVldqnQDLRDKV 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1202 ERLEEvggaSLAQLEITKKQETKFQKLRRDMEEATLHFEATSA---SLKKRHADSLAELEGQVENLQQvkqklEKDRSDL 1278
Cdd:PLN02939 334 DKLEA----SLKEANVSKFSSYKVELLQQKLKLLEERLQASDHeihSYIQLYQESIKEFQDTLSKLKE-----ESKKRSL 404
|
....*..
gi 1411134203 1279 QLEVDDL 1285
Cdd:PLN02939 405 EHPADDM 411
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1021-1232 |
5.21e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1021 EKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEE----KLSSLSKANLKLEQQVVGLEGALEQER 1096
Cdd:PHA02562 182 QIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKtikaEIEELTDELLNLVMDIEDPSAALNKLN 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1097 KARINCERELHKLEGDLKLNQES------MENLESSQRHLAE-ELRKKELENS--QMNSKVENEKGLV---AQLQKMVKE 1164
Cdd:PHA02562 262 TAAAKIKSKIEQFQKVIKMYEKGgvcptcTQQISEGPDRITKiKDKLKELQHSleKLDTAIDELEEIMdefNEQSKKLLE 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1165 LQTQIKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVGgaslAQLE--ITKKQETKFQKLRRDM 1232
Cdd:PHA02562 342 LKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQ----DELDkiVKTKSELVKEKYHRGI 407
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1054-1418 |
5.87e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 41.20 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1054 QEAHQQTLDDLH--------------MEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQES 1119
Cdd:pfam15742 12 QEEVQQLRQNLQrlqilctsaekelrYERGKNLDLKQHNSLLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1120 MENLESSQRHLAEELRkkelENSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKE--KLEAERTTRAKMEKERADLTQDL 1197
Cdd:pfam15742 92 IRELELEVLKQAQSIK----SQNSLQEKLAQEKSRVADAEEKILELQQKLEHAHKvcLTDTCILEKKQLEERIKEASENE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1198 ADLNERLEEvggaSLAQLEITKKQETKFQKLRRDMEEATLHFEATSASLKKRhadsLAELEGQVENLQQvkqklEKDRSD 1277
Cdd:pfam15742 168 AKLKQQYQE----EQQKRKLLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLR----IQQQEAQLKQLEN-----EKRKSD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1278 LQLEVDDLLTriEQMTRAKANAEKLCTLYEERLNEANAKLDKVTQLANDlaaQKTELWSESGEFLRRLEEKEALINQLSR 1357
Cdd:pfam15742 235 EHLKSNQELS--EKLSSLQQEKEALQEELQQVLKQLDVHVRKYNEKHHH---HKAKLRRAKDRLVHEVEQRDERIKQLEN 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411134203 1358 EksnftrqIEELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKV 1418
Cdd:pfam15742 310 E-------IGILQQQSEKEKAFQKQVTAQNEILLLEKRKLLEQLTEQEELIKNNKRTISSV 363
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1343-1643 |
5.90e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.54 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1343 RRLEEKEALINQLSREKSNFTRQIEELRGQLEKE--TKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRtlsKVNA 1420
Cdd:NF033838 81 RKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAEltSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEK---KAKD 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1421 EMVQWRMKYENNVIqKTEDLEDAKKELAIRlqetaeamgvanarNASLERARHRLQLElgdalSDLGKVRSAAARLDQKQ 1500
Cdd:NF033838 158 QKEEDRRNYPTNTY-KTLELEIAESDVEVK--------------KAELELVKEEAKEP-----RDEEKIKQAKAKVESKK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1501 LQSG---KALADWKQKHEESQTLLDASRKEI---QALSTELLKLKHAYK--------------------ESIVGQETLRR 1554
Cdd:NF033838 218 AEATrleKIKTDREKAEEEAKRRADAKLKEAvekNVATSEQDKPKRRAKrgvlgepatpdkkendakssDSSVGEETLPS 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1555 ENKNLQEEISNLTNQVREGTKNLTEMEK---------VKKLIEQEKTEVQVTLEETEGAL-------ERNESKILRFQLE 1618
Cdd:NF033838 298 PSLKPEKKVAEAEKKVEEAKKKAKDQKEedrrnyptnTYKTLELEIAESDVKVKEAELELvkeeakePRNEEKIKQAKAK 377
|
330 340
....*....|....*....|....*...
gi 1411134203 1619 LLKAKAE---LERKLSEKDEELENFRRK 1643
Cdd:NF033838 378 VESKKAEatrLEKIKTDRKKAEEEAKRK 405
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
963-1294 |
6.04e-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: 41.65 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 963 IKSKIQLEARVKELSERVEEEEEINSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEflNED 1042
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEER--KRE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1043 ISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANL---------------KLEQQVVGLEGALEQERKARincERELH 1107
Cdd:pfam17380 362 LERIRQEEIAMEISRMRELERLQMERQQKNERVRQELeaarkvkileeerqrKIQQQKVEMEQIRAEQEEAR---QREVR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1108 KLEGDLKLNQESMENLESSQRHLAEELRKKELENSQMNSKVENE---KGLVAQLQKMVkeLQTQIKDLKEKLEAERTTRA 1184
Cdd:pfam17380 439 RLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEkrdRKRAEEQRRKI--LEKELEERKQAMIEEERKRK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1185 KMEKERADLTQDLADLNERLEEvggaslaqlEITKKQETKFQKLRRDMEEATLHFEATSaslkkrhadSLAELEGQVENL 1264
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREA---------EEERRKQQEMEERRRIQEQMRKATEERS---------RLEAMEREREMM 578
|
330 340 350
....*....|....*....|....*....|
gi 1411134203 1265 QQVKqklEKDRSDLQLEVDDLLTRIEQMTR 1294
Cdd:pfam17380 579 RQIV---ESEKARAEYEATTPITTIKPIYR 605
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1483-1984 |
6.65e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1483 LSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQTLLDASRKEIQALSTELLKLKHAYKESIVGQETLRRENKNLQEE 1562
Cdd:PRK01156 182 ISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1563 ISNLTNQVREGTKNLTEMEKVKKLI-----------------EQEKTEVQVTLEETEGALERNESKILRFQlELLKAKAE 1625
Cdd:PRK01156 262 ESDLSMELEKNNYYKELEERHMKIIndpvyknrnyindyfkyKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDYND 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1626 LERKLSEKDE------ELENFRRKQQCTIDSMQSSLDSEAKSRIEATRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQ 1699
Cdd:PRK01156 341 YIKKKSRYDDlnnqilELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1700 LQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRN--SLLQSELEDlrslqEQTERGRRLSEEELLEATERINLFYTQNTSL 1777
Cdd:PRK01156 421 ISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcPVCGTTLGE-----EKSNHIINHYNEKKSRLEEKIREIEIEVKDI 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1778 LSQKKKLEADVAQMQKEAEEVVQECQNAEEKAKKAATEAANLSEELKKKQDTIAHLEKTRENMEqtITDLQKRLAEAEQT 1857
Cdd:PRK01156 496 DEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLK--LEDLDSKRTSWLNA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1858 ALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRG----ARRLERCIKELTYQA---EEDKKNLSRMQTQMDKLQLKVH 1930
Cdd:PRK01156 574 LAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGfpddKSYIDKSIREIENEAnnlNNKYNEIQENKILIEKLRGKID 653
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1411134203 1931 NYKQQVevaeaqanqylSKYKKQQHELNEVKERAEVAESQVNKL-----KIKAREFGKK 1984
Cdd:PRK01156 654 NYKKQI-----------AEIDSIIPDLKEITSRINDIEDNLKKSrkaldDAKANRARLE 701
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1431-1679 |
7.00e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1431 NNVIQKTEDLEDAKKELAIRLQETAEAMGVANARN-------ASLERARHRLQLElgdALSDLGKVRSAAARLD------ 1497
Cdd:PLN02939 159 EKILTEKEALQGKINILEMRLSETDARIKLAAQEKihveileEQLEKLRNELLIR---GATEGLCVHSLSKELDvlkeen 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1498 ---QKQLQSGKALADWKQKHEES-------QTLLDASRKEIQalSTELLKLKHAYKESIVGQETLRRENKNLQEEISNLT 1567
Cdd:PLN02939 236 mllKDDIQFLKAELIEVAETEERvfklekeRSLLDASLRELE--SKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRAT 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1568 NQVREGTKNLTEMEKVKKLIEqektEVQVTLEETegalerNESKILRFQLELLKAKAE-LERKLSEKDEELENFRRKQQC 1646
Cdd:PLN02939 314 NQVEKAALVLDQNQDLRDKVD----KLEASLKEA------NVSKFSSYKVELLQQKLKlLEERLQASDHEIHSYIQLYQE 383
|
250 260 270
....*....|....*....|....*....|...
gi 1411134203 1647 TIDSMQSSLdseaKSRIEATRlKKKMEEDLNEM 1679
Cdd:PLN02939 384 SIKEFQDTL----SKLKEESK-KRSLEHPADDM 411
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1169-1355 |
7.11e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.89 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1169 IKDLKEKLEAERTTRAKMEKERADLTQDLADLNERLEEVggasLAQLEITKKQETKFQKLRRDMEEATLHFeatsaslkK 1248
Cdd:pfam13851 28 IKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKA----QEEVEELRKQLENYEKDKQSLKNLKARL--------K 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1249 RHADSLAELEGQVENLQQVKQKLEKDRSDLQLEVDDLLTRIEQMTRAKANA-EKLCTLYEERLNEANAKLDKVTQLANdL 1327
Cdd:pfam13851 96 VLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLlEKKLQALGETLEKKEAQLNEVLAAAN-L 174
|
170 180
....*....|....*....|....*...
gi 1411134203 1328 AAQKTELWSESGEFLrrLEEKEALINQL 1355
Cdd:pfam13851 175 DPDALQAVTEKLEDV--LESKNQLIKDL 200
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1102-1214 |
7.34e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1102 CERELHKLEgdLKLNQESMENLESSQRHLAE---ELRKKELENSQMNSKVENEKGLVAQLQKmvkelqtqikdLKEKLEA 1178
Cdd:COG0542 416 LERRLEQLE--IEKEALKKEQDEASFERLAElrdELAELEEELEALKARWEAEKELIEEIQE-----------LKEELEQ 482
|
90 100 110
....*....|....*....|....*....|....*..
gi 1411134203 1179 ERTTRAKMEKERADLTQDLADLNERL-EEVGGASLAQ 1214
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLrEEVTEEDIAE 519
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1105-1465 |
7.86e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.21 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1105 ELHKLEG---DLKLNQESMENLESSQRHLAEELRKKELENSQMnskvENEKGLVAQLQKMVKELQTQIKDLKEKLEAERT 1181
Cdd:pfam05622 74 ENFRLETardDYRIKCEELEKEVLELQHRNEELTSLAEEAQAL----KDEMDILRESSDKVKKLEATVETYKKKLEDLGD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1182 TRAKM---EKERADLTQDLADLNERLEEVGGASlAQLEITKKQetkFQKLRRDMEEATLHFEATSASLKKrhadslaeLE 1258
Cdd:pfam05622 150 LRRQVkllEERNAEYMQRTLQLEEELKKANALR-GQLETYKRQ---VQELHGKLSEESKKADKLEFEYKK--------LE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1259 GQVENLQQVKQKLEKDRSDLQLEVDDLltRIEQMTRAKAN-AEKLCTLYEERLNEANAKL------DKVTQLAND----L 1327
Cdd:pfam05622 218 EKLEALQKEKERLIIERDTLRETNEEL--RCAQLQQAELSqADALLSPSSDPGDNLAAEImpaeirEKLIRLQHEnkmlR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1328 AAQKTELWSESGEFLRRLEEKEALINQLSREKSNFTRQIEELRGQLEKETKS-QSALAHAlqkaqRDCDLLREQYEEEQE 1406
Cdd:pfam05622 296 LGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKAlQEQGSKA-----EDSSLLKQKLEEHLE 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411134203 1407 VKAELHRTLSKVNAEMVQWRMKYENNVIQKTEDLEDA--KKELAIRLQETAEAMGVANARN 1465
Cdd:pfam05622 371 KLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEAlrKKDEDMKAMEERYKKYVEKAKS 431
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
907-1026 |
7.98e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.20 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 907 KEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKelserveEEEEI 986
Cdd:pfam05911 680 TEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLK-------CMAES 752
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1411134203 987 NSELTARGRKLEDECSELKKEIDDLEtmlVKSEKEKRTTE 1026
Cdd:pfam05911 753 YEDLETRLTELEAELNELRQKFEALE---VELEEEKNCHE 789
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
901-1266 |
7.99e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 901 EEIAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANV------EEQCEWLIKSKIQLEARVK 974
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVqtalrqQEKIERYQADLEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 975 ELSERVEEEEEINSELTARGRKLEDECSELKKEIDDLETMLvkSEKEKRTTE-HKVKNLTEEVEFLNEDISKLNRAAKVV 1053
Cdd:PRK04863 366 EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAL--DVQQTRAIQyQQAVQALERAKQLCGLPDLTADNAEDW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1054 QE---AHQQTLDD-LHMEEEKLSSLSKAN------LKLEQQVVGlegalEQERKARINCERELhklEGDLKLNQESMENL 1123
Cdd:PRK04863 444 LEefqAKEQEATEeLLSLEQKLSVAQAAHsqfeqaYQLVRKIAG-----EVSRSEAWDVAREL---LRRLREQRHLAEQL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1124 ESSQRHLAEELRKKELENS----------QMNSKVENEkglvAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADL 1193
Cdd:PRK04863 516 QQLRMRLSELEQRLRQQQRaerllaefckRLGKNLDDE----DELEQLQEELEARLESLSESVSEARERRMALRQQLEQL 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1194 TQDLADL----------NERLEEVGGASLAQLEITKKQETKFQKLRRDMEEATLHfeatsaslKKRHADSLAELEGQVEN 1263
Cdd:PRK04863 592 QARIQRLaarapawlaaQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVE--------RDELAARKQALDEEIER 663
|
...
gi 1411134203 1264 LQQ 1266
Cdd:PRK04863 664 LSQ 666
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
964-1298 |
8.16e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 964 KSKIQLEARVKELSERVEEEEEINSELTARGRKLEDECSELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDI 1043
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1044 SKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVVGLEGALEQERKARINCERELHKLEGDLKLNQESMENL 1123
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1124 ESSQRHLAEELRKKELE------NSQMNSKVENEKGLVAQLQKMVKELQTQIKDLKEKLEAERTTRAKMEKERADLTQDL 1197
Cdd:COG4372 170 EQELQALSEAEAEQALDellkeaNRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1198 ADLNERLEEVGGASLAQLEITKKQETKFQKLRRDMEEATLHFEATSASLKKRHADSLAELEGQVENLQQVKQKLEKDRSD 1277
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
330 340
....*....|....*....|.
gi 1411134203 1278 LQLEVDDLLTRIEQMTRAKAN 1298
Cdd:COG4372 330 LALAILLAELADLLQLLLVGL 350
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1118-1417 |
8.24e-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: 40.83 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1118 ESMENLESSQRHLAEELRKKELENSQMNSKVENekgLVAQLQKMVKELQTQIKDLKEKLEaerttraKMEKERADLTQDL 1197
Cdd:pfam04108 3 SSAQDLCRWANELLTDARSLLEELVVLLAKIAF---LRRGLSVQLANLEKVREGLEKVLN-------ELKKDFKQLLKDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1198 ADLNERLEEVggaslaqLEITKKQETKFQKLRRDMEEATLH-F--EATSASLKKRHADSLAELEGQVENLQQVKQKLEKD 1274
Cdd:pfam04108 73 DAALERLEET-------LDKLRNTPVEPALPPGEEKQKTLLdFidEDSVEILRDALKELIDELQAAQESLDSDLKRFDDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1275 RSDLQLEVDDLLTRieqmTRAKANAEKLCTLYEERLNEANAKLDKVTQLANDLAAQKTELWSESGEFLRRLEEKEALINQ 1354
Cdd:pfam04108 146 LRDLQKELESLSSP----SESISLIPTLLKELESLEEEMASLLESLTNHYDQCVTAVKLTEGGRAEMLEVLENDARELDD 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411134203 1355 LSREKSNFTRQIEELRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSK 1417
Cdd:pfam04108 222 VVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQLIAEIQSRLPEYLAALKEFEERWEE 284
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1099-1199 |
8.84e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.61 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411134203 1099 RINC-ERELHKLEGDLKLNQESMENLESSQRHLAEELRKKE---------LENSQMNSKVEN-----EKGLVAQlqkmVK 1163
Cdd:pfam03148 252 RIEEtEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEaplklaqtrLENRTYRPNVELcrdeaQYGLVDE----VK 327
|
90 100 110
....*....|....*....|....*....|....*.
gi 1411134203 1164 ELQTQIKDLKEKLEAERTTRAKMEKERADLTQDLAD 1199
Cdd:pfam03148 328 ELEETIEALKQKLAEAEASLQALERTRLRLEEDIAV 363
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