|
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 ... |
96-757 |
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: 1432.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAAISEPKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADI 255
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 256 QIYFLEKSRVVYQQPGERNYHIFYQILSGNQELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAIDVLGFLPD 335
Cdd:cd14929 161 DIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDILGFLPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 336 EKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQVTYAV 415
Cdd:cd14929 241 EKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTYAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 416 GALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEEYRKE 495
Cdd:cd14929 321 GALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 496 GLDWLSIDYGLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPEKNFEVHFELAHYAG 575
Cdd:cd14929 401 GIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHFELVHYAG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 576 VVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSASQFGEKTHKKGTSFHLITSLHKENINKLMTDLKS 655
Cdd:cd14929 481 VVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQFGEKKRKKGASFQTVASLHKENLNKLMTNLKS 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 656 TAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFSKSKFVSSRKATEE 735
Cdd:cd14929 561 TAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSSRKAAEE 640
|
650 660
....*....|....*....|..
gi 261245016 736 VLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14929 641 LLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
96-757 |
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: 1069.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAAISEPK----KKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLS 251
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKkesgKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 252 FADIQIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAIDVL 330
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGaDPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 331 GFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQ 410
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 411 VTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQE 490
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 491 EYRKEGLDWLSIDYGLDVQACIDFIEKP-MGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPtsPEKNFEVHFE 569
Cdd:cd01377 401 EYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKP--KPKKSEAHFI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 570 LAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSAsqfGEKTHKKGTSFHLITSLHKENINKL 649
Cdd:cd01377 479 LKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGG---GGKKKKKGGSFRTVSQLHKEQLNKL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 650 MTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFSKSkFVSS 729
Cdd:cd01377 556 MTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKG-FDDG 634
|
650 660
....*....|....*....|....*...
gi 261245016 730 RKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd01377 635 KAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
96-757 |
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: 1031.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAAISE-PKKKL--------GNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGA 246
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDgPGKKAqflatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 247 RGTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQ-ELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEK 325
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKpELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 326 AIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRS 405
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 406 QNLQQVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLF 485
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 486 ILEQEEYRKEGLDWLSIDYGLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPEK-NF 564
Cdd:cd14927 401 ILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKrKY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 565 EVHFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLF----TKDIIAGSASQFGEKtHKKGTSFHLITS 640
Cdd:cd14927 481 EAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYenyvGSDSTEDPKSGVKEK-RKKAASFQTVSQ 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 641 LHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRI 720
Cdd:cd14927 560 LHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSA 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 261245016 721 FSKSKFVSSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14927 640 IPDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
97-757 |
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: 938.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTGE 176
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 177 SGSGKTVNTKLIIQYFATMAAISEPKKK-----LGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLS 251
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKkdskmKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 252 FADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQ-ELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAIDVL 330
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKpELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 331 GFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQ 410
Cdd:cd14913 242 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 411 VTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQE 490
Cdd:cd14913 322 VHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 491 EYRKEGLDWLSIDYGLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPEKNFEVHFEL 570
Cdd:cd14913 402 EYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFSL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 571 AHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSASQFGEKTHKKGTSFHLITSLHKENINKLM 650
Cdd:cd14913 482 IHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKLM 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 651 TDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFSKSKFVSSR 730
Cdd:cd14913 562 SNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSK 641
|
650 660
....*....|....*....|....*..
gi 261245016 731 KATEEVLDFLEIDHPHYQCGVTKVFFK 757
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 ... |
97-757 |
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: 871.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTGE 176
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 177 SGSGKTVNTKLIIQYFATMAAISEPKKK-----LGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLS 251
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKdqtpgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 252 FADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQ-ELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAIDVL 330
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKpELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 331 GFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQ 410
Cdd:cd14917 242 GFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 411 VTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQE 490
Cdd:cd14917 322 VIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 491 EYRKEGLDWLSIDYGLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPEKNFEVHFEL 570
Cdd:cd14917 402 EYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHFSL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 571 AHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSASQFGEKTHKKGTSFHLITSLHKENINKLM 650
Cdd:cd14917 482 IHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLM 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 651 TDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFSKSKFVSSR 730
Cdd:cd14917 562 TNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSR 641
|
650 660
....*....|....*....|....*..
gi 261245016 731 KATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14917 642 KGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
84-757 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 869.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 84 IEDLSMLLYLNEASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDML 163
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 164 RNGENQSIVFTGESGSGKTVNTKLIIQYFATMAAISEPKKKlGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIH 243
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV-GRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 244 FGARGTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVsTNPSDFHICS-CGVVAVESLDDAKEFL 321
Cdd:pfam00063 160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGaSAQLKKELRL-TNPKDYHYLSqSGCYTIDGIDDSEEFK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 322 ATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEY 401
Cdd:pfam00063 239 ITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRET 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 402 VTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVLDAK-LTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFF 480
Cdd:pfam00063 319 VSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKtIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 481 NQQLFILEQEEYRKEGLDWLSIDYGlDVQACIDFIE-KPMGIFSILEEECMLPKATDQMFKTKLFDHHfGKSAYFQTPTS 559
Cdd:pfam00063 399 NHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 560 PEKNfevHFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLF----TKDIIAGSASQFGEKTHKKGTSF 635
Cdd:pfam00063 477 QGET---HFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFpdyeTAESAAANESGKSTPKRTKKKRF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 636 HLITSLHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWI 715
Cdd:pfam00063 554 ITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRI 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 261245016 716 LNPRIfSKSKFVSSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:pfam00063 634 LAPKT-WPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
77-769 |
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: 854.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 77 NPEELEMIEDLSMLLYLNEASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVAN 156
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 157 RAFQDMLRNGENQSIVFTGESGSGKTVNTKLIIQYFatmAAISEPKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRF 236
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYL---ASVSGSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 237 GKLIRIHFGARGTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVSTnPSDFHICS-CGVVAVESL 314
Cdd:smart00242 158 GKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGaSEELKKELGLKS-PEDYRYLNqGGCLTVDGI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 315 DDAKEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEA-DGTENADKAAFLMGIHASELLKGLIYP 393
Cdd:smart00242 237 DDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTvKDKEELSNAAELLGVDPEELEKALTKR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 394 RIKVGNEYVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTN 473
Cdd:smart00242 317 KIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 474 EKLQQFFNQQLFILEQEEYRKEGLDWLSIDYGlDVQACIDFIE-KPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSA 552
Cdd:smart00242 397 EKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 553 YfqtpTSPEKNFEVHFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFtkdiiagsaSQFGEKTHKKG 632
Cdd:smart00242 476 F----SKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLF---------PSGVSNAGSKK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 633 tSFHLITSLHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQR 712
Cdd:smart00242 543 -RFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQR 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 261245016 713 YWILNPRiFSKSKFVSSRKATEEVLDFLEIDHPHYQCGVTKVFFKAFILDQLEERRD 769
Cdd:smart00242 622 YRVLLPD-TWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
97-757 |
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: 850.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTGE 176
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 177 SGSGKTVNTKLIIQYFATMAAISEPKKK------LGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTL 250
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKenpnanKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 251 SFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQ-ELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAIDV 329
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKpELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 330 LGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQ 409
Cdd:cd14916 242 LGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 410 QVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQ 489
Cdd:cd14916 322 QVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 490 EEYRKEGLDWLSIDYGLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPEKNFEVHFE 569
Cdd:cd14916 402 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHFS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 570 LAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSA-SQFGEKTHKKGTSFHLITSLHKENINK 648
Cdd:cd14916 482 LVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGdSGKGKGGKKKGSSFQTVSALHRENLNK 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 649 LMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFSKSKFVS 728
Cdd:cd14916 562 LMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFID 641
|
650 660
....*....|....*....|....*....
gi 261245016 729 SRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14916 642 SRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
97-757 |
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: 847.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTGE 176
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 177 SGSGKTVNTKLIIQYFATMAAISE------PKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTL 250
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDkkkeqqPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 251 SFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQ-ELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAIDV 329
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKpELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAIDI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 330 LGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQ 409
Cdd:cd14923 242 LGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 410 QVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQ 489
Cdd:cd14923 322 QVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 490 EEYRKEGLDWLSIDYGLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPEKNFEVHFE 569
Cdd:cd14923 402 EEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHFS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 570 LAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSASQFGEKT--HKKGTSFHLITSLHKENIN 647
Cdd:cd14923 482 LVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSGGSKKggKKKGSSFQTVSAVFRENLN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 648 KLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFSKSKFV 727
Cdd:cd14923 562 KLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQFI 641
|
650 660 670
....*....|....*....|....*....|
gi 261245016 728 SSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14923 642 DSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
98-757 |
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: 840.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 98 VLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTGES 177
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 178 GSGKTVNTKLIIQYFATMAAISEPKKK-----LGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSF 252
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 253 ADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQ-ELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAIDVLG 331
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 332 FLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQV 411
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 412 TYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEE 491
Cdd:cd14918 323 YNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 492 YRKEGLDWLSIDYGLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPEKNFEVHFELA 571
Cdd:cd14918 403 YKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFSLI 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 572 HYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSASQFGEKTHKKGTSFHLITSLHKENINKLMT 651
Cdd:cd14918 483 HYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAKKKGSSFQTVSALFRENLNKLMT 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 652 DLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFSKSKFVSSRK 731
Cdd:cd14918 563 NLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDSKK 642
|
650 660
....*....|....*....|....*.
gi 261245016 732 ATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14918 643 ASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
97-757 |
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: 835.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTGE 176
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 177 SGSGKTVNTKLIIQYFATMAAISEPKKK-------LGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGT 249
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 250 LSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQ-ELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAID 328
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 329 VLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNL 408
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 409 QQVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILE 488
Cdd:cd14912 322 EQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 489 QEEYRKEGLDWLSIDYGLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPEKNFEVHF 568
Cdd:cd14912 402 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAHF 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 569 ELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIA-GSASQFGEKT--HKKGTSFHLITSLHKEN 645
Cdd:cd14912 482 SLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAeGASAGGGAKKggKKKGSSFQTVSALFREN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 646 INKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFSKSK 725
Cdd:cd14912 562 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 641
|
650 660 670
....*....|....*....|....*....|..
gi 261245016 726 FVSSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14912 642 FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
97-757 |
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: 835.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTGE 176
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 177 SGSGKTVNTKLIIQYFATMAAISEPKKK-------LGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGT 249
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 250 LSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQ-ELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAID 328
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 329 VLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNL 408
Cdd:cd14915 242 ILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 409 QQVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILE 488
Cdd:cd14915 322 QQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 489 QEEYRKEGLDWLSIDYGLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPEKNFEVHF 568
Cdd:cd14915 402 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAHF 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 569 ELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSASQFGEK-THKKGTSFHLITSLHKENIN 647
Cdd:cd14915 482 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKgGKKKGSSFQTVSALFRENLN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 648 KLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFSKSKFV 727
Cdd:cd14915 562 KLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI 641
|
650 660 670
....*....|....*....|....*....|
gi 261245016 728 SSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
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 ... |
97-757 |
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: 833.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTGE 176
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 177 SGSGKTVNTKLIIQYFATMAAISEPKKK-------LGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGT 249
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 250 LSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQ-ELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAID 328
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 329 VLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNL 408
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 409 QQVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILE 488
Cdd:cd14910 322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 489 QEEYRKEGLDWLSIDYGLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPEKNFEVHF 568
Cdd:cd14910 402 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAHF 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 569 ELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSASQFGEK-THKKGTSFHLITSLHKENIN 647
Cdd:cd14910 482 SLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKgGKKKGSSFQTVSALFRENLN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 648 KLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFSKSKFV 727
Cdd:cd14910 562 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI 641
|
650 660 670
....*....|....*....|....*....|
gi 261245016 728 SSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14910 642 DSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
96-757 |
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: 823.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAAIS---EPKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSF 252
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKktdEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 253 ADIQIYFLEKSRVVYQQPGERNYHIFYQILSGN-QELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAIDVLG 331
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSvPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 332 FLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQV 411
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 412 TYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEE 491
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 492 YRKEGLDWLSIDYGLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPEKNFEV-HFEL 570
Cdd:cd14909 401 YKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAaHFAI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 571 AHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTkDIIAGSASQFGEK--THKKGTSFHLITSLHKENINK 648
Cdd:cd14909 481 AHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFA-DHAGQSGGGEQAKggRGKKGGGFATVSSAYKEQLNS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 649 LMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFSKSKfvS 728
Cdd:cd14909 560 LMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE--D 637
|
650 660
....*....|....*....|....*....
gi 261245016 729 SRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14909 638 PKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
96-757 |
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: 813.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAAISEPKKK-LGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFAD 254
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDgKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 255 IQIYFLEKSRVVYQQPGERNYHIFYQILSGNQ-ELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAIDVLGFL 333
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKpELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 334 PDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQVTY 413
Cdd:cd14934 241 AEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 414 AVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEEYR 493
Cdd:cd14934 321 SIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 494 KEGLDWLSIDYGLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPE-KNFEVHFELAH 572
Cdd:cd14934 401 REGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKgKGPEAHFELVH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 573 YAGVVPYNISGWIGKNKGLLNETVVALLQKSSnKVLANLFTKDIIAGSasqfGEKTHKKGTSFHLITSLHKENINKLMTD 652
Cdd:cd14934 481 YAGTVGYNITGWLEKNKDPLNETVVGLFQKSS-LGLLALLFKEEEAPA----GSKKQKRGSSFMTVSNFYREQLNKLMTT 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 653 LKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFSKSkFVSSRKA 732
Cdd:cd14934 556 LHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVDNKKA 634
|
650 660
....*....|....*....|....*
gi 261245016 733 TEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14934 635 SELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
32-1312 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 757.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 32 KCWVPDGKNAYIEAEVKESGDDGQVIVET---RDGEIMRIKEDKLQQ--MNPEELEMIEDLSMLLYLNEASVLHTLRRRY 106
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPAVLHNLEKRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 107 DHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTGESGSGKTVNTK 186
Cdd:COG5022 91 NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 187 LIIQYFATMAAISEPKKklGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADIQIYFLEKSRVV 266
Cdd:COG5022 171 RIMQYLASVTSSSTVEI--SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 267 YQQPGERNYHIFYQILSGNQELRNMLLVSTNPSDFHICS-CGVVAVESLDDAKEFLATEKAIDVLGFLPDEKFGCYKLVG 345
Cdd:COG5022 249 HQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSqGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 346 AIMHFGNLKFKRNlREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQVTYAVGALSQSIYER 425
Cdd:COG5022 329 AILHIGNIEFKED-RNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 426 MFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEEYRKEGLDWLSIDYg 505
Cdd:COG5022 408 LFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY- 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 506 LDVQACIDFIEK--PMGIFSILEEECMLPKATDQMFKTKLFDH-HFGKSAYFQTPTSPEKNFEVhfelAHYAGVVPYNIS 582
Cdd:COG5022 487 FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNKFVV----KHYAGDVEYDVE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 583 GWIGKNKGLLNETVVALLQKSSNKVLANLFTKDiiagsasqfgEKTHKKGTsFHLITSLHKENINKLMTDLKSTAPHFVR 662
Cdd:COG5022 563 GFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE----------ENIESKGR-FPTLGSRFKESLNSLMSTLNSTQPHYIR 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 663 CINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNP---RIFSKSKFVSSRKATEEVLDF 739
Cdd:COG5022 632 CIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPsksWTGEYTWKEDTKNAVKSILEE 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 740 LEIDHPHYQCGVTKVFFKAFILDQLEERRDEKISKVFTLFQARARGKLMRITFQKILEERDALALIQENIRAFIAVKNCP 819
Cdd:COG5022 712 LVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYEL 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 820 WMGLFFKIKPLAKSVGAGEEIAGLKEECAQLQKALESSESQREELKTKQvSLVQEKNDLRLQLQAEQETLANSEEQCESL 899
Cdd:COG5022 792 KWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEF-SLKAEVLIQKFGRSLKAKKRFSLLKKETIY 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 900 IKSKVELEVKIKELSRQVEEEEEINSeLTARGRKLEDECSELKKEIYDleailaksekgkcaaehkvrNLTEEVHSLNEE 979
Cdd:COG5022 871 LQSAQRVELAERQLQELKIDVKSISS-LKLVNLELESEIIELKKSLSS--------------------DLIENLEFKTEL 929
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 980 VSKLSRvvkdaqetqqqtqeqlHIEEEKLSNMSkanLKLAQQIDVLEGDLERERKARMKCErekrKLQDELKMNQEGAEN 1059
Cdd:COG5022 930 IARLKK----------------LLNNIDLEEGP---SIEYVKLPELNKLHEVESKLKETSE----EYEDLLKKSTILVRE 986
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1060 LESSRQKLaEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESERtIRAKVEREKGDLVQDLEDLNE 1139
Cdd:COG5022 987 GNKANSEL-KNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELS-ILKPLQKLKGLLLLENNQLQA 1064
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1140 RLEeaggtslaQMEITKQQEARFQKLHHDMEET---TRHFEATSASLKKRHAENLAELEgQVEHLQQVRLVLEQDKSDLQ 1216
Cdd:COG5022 1065 RYK--------ALKLRRENSLLDDKQLYQLESTenlLKTINVKDLEVTNRNLVKPANVL-QFIVAQMIKLNLLQEISKFL 1135
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1217 LQVDDLLNRVDQmaRAKANAEKLCGLYERRLNEANTKLDevtqlAHDLTTQKTKLQSESGEFFKRL------EEKEALIS 1290
Cdd:COG5022 1136 SQLVNTLEPVFQ--KLSVLQLELDGLFWEANLEALPSPP-----PFAALSEKRLYQSALYDEKSKLsssevnDLKNELIA 1208
|
1290 1300
....*....|....*....|..
gi 261245016 1291 QLSREKSNFTRQVEELRAQLEE 1312
Cdd:COG5022 1209 LFSKIFSGWPRGDKLKKLISEG 1230
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
96-757 |
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: 752.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRR-SEVPPHIFAVANRAFQDMLRNGENQSIVFT 174
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 175 GESGSGKTVNTKLIIQYFATMAA--ISEPKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSF 252
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGsgSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 253 ADIQIYFLEKSRVVYQQPGERNYHIFYQILSGN-----QELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAI 327
Cdd:cd00124 161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLsdgarEELKLELLLSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 328 DVLGFLPDEKFGCYKLVGAIMHFGNLKF--KRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRS 405
Cdd:cd00124 241 DVLGFSDEEQDSIFRILAAILHLGNIEFeeDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 406 QNLQQVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHF--FVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQ 483
Cdd:cd00124 321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEStsFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 484 LFILEQEEYRKEGLDWLSIDYgLDVQACIDFIE-KPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPEK 562
Cdd:cd00124 401 VFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 563 NFEVHfelaHYAGVVPYNISGWIGKNKGLLNETVVALLQkssnkvlanlftkdiiagSASQFgekthkkgtsfhlitslh 642
Cdd:cd00124 480 EFGIK----HYAGDVTYDADGFLEKNKDTLPPDLVDLLR------------------SGSQF------------------ 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 643 KENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRiFS 722
Cdd:cd00124 520 RSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPG-AT 598
|
650 660 670
....*....|....*....|....*....|....*
gi 261245016 723 KSKFVSSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
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 ... |
96-757 |
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: 670.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAAiSEPKKK-------------LGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRI 242
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAA-SKPKGSgavphpavnpavlIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 243 HFGARGTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLA 322
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 323 TEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYV 402
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 403 TRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVLD-AKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFN 481
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 482 QQLFILEQEEYRKEGLDWLSIDYGLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFdhhfgkSAYFQTPTSPE 561
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLV------SAHSMHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 562 KNFE--VHFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSA------SQFGEKThKKGT 633
Cdd:cd14911 474 TDFRgvADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAqqaltdTQFGART-RKGM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 634 sFHLITSLHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRY 713
Cdd:cd14911 553 -FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 261245016 714 WILNPRIFSKSkFVSSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14911 632 ELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
96-757 |
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: 646.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAAiSEPKKKLGN----LEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLS 251
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVAS-SHKGRKDHNipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 252 FADIQIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVSTnPSDFHICSCGVVAVESLDDAKEFLATEKAIDVL 330
Cdd:cd14920 160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGaGEHLKSDLLLEG-FNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 331 GFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQ 410
Cdd:cd14920 239 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 411 VTYAVGALSQSIYERMFQWLVARMNQVLD-AKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQ 489
Cdd:cd14920 319 ADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 490 EEYRKEGLDWLSIDYGLDVQACIDFIEKPM---GIFSILEEECMLPKATDQMFKTKLFDHHfGKSAYFQTPTSPEKnfEV 566
Cdd:cd14920 399 EEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKD--KA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 567 HFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDI-------IAGSASQFGEKTHK-KGTSFHLI 638
Cdd:cd14920 476 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqVTGMTETAFGSAYKtKKGMFRTV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 639 TSLHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNP 718
Cdd:cd14920 556 GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 635
|
650 660 670
....*....|....*....|....*....|....*....
gi 261245016 719 RIFSKSkFVSSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14920 636 NAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
97-757 |
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: 632.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRY-DHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd01380 2 AVLHNLKVRFcQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAAISEPKKklgNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADI 255
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET---QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 256 QIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAIDVLGFLP 334
Cdd:cd01380 159 RTYLLEKSRVVFQAEEERNYHIFYQLCAAaSLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 335 DEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQVTYA 414
Cdd:cd01380 239 EEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 415 VGALSQSIYERMFQWLVARMNQVLDA--KLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEEY 492
Cdd:cd01380 319 RDALAKHIYAQLFDWIVDRINKALASpvKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 493 RKEGLDWLSIDYgLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGK-SAYFQTPTSPEKNFEVHfela 571
Cdd:cd01380 399 VKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVK---- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 572 HYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNkvlanlftkdiiagsasqfgektHKK--GTSFhlitslhKENINKL 649
Cdd:cd01380 474 HFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN-----------------------RKKtvGSQF-------RDSLILL 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 650 MTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRifSKSKFVSS 729
Cdd:cd01380 524 METLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPS--KEWLRDDK 601
|
650 660
....*....|....*....|....*...
gi 261245016 730 RKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd01380 602 KKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
96-757 |
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: 598.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAAISEPKKKL-------GNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARG 248
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQssialshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 249 TLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAID 328
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 329 VLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNL 408
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 409 QQVTYAVGALSQSIYERMFQWLVARMNQVLD-AKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFIL 487
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 488 EQEEYRKEGLDWLSIDYGLDVQACIDFIEKPM---GIFSILEEECMLPKATDQMFKTKLFDHHfGKSAYFQTPTSPEKnf 564
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQ-GNNPKFQKPKKLKD-- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 565 EVHFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTK-------DIIAG-SASQFGEKTHKKGTsFH 636
Cdd:cd14932 478 DADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDvdrivglDKVAGmGESLHGAFKTRKGM-FR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 637 LITSLHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWIL 716
Cdd:cd14932 557 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 636
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 261245016 717 NPRIFSKSkFVSSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14932 637 TPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
96-757 |
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: 580.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAAISEPKKK---LGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSF 252
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 253 ADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQE-LRNMLLVSTNpSDFHICSCGVVAVESLDDAKEFLATEKAIDVLG 331
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEkMRSDLLLEGF-NNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 332 FLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQV 411
Cdd:cd14921 240 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 412 TYAVGALSQSIYERMFQWLVARMNQVLD-AKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQE 490
Cdd:cd14921 320 DFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 491 EYRKEGLDWLSIDYGLDVQACIDFIEKPM---GIFSILEEECMLPKATDQMFKTKLFDHHfGKSAYFQTPTSPEKNFEvh 567
Cdd:cd14921 400 EYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKDKTE-- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 568 FELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTK-DIIAG-------SASQFGEKTHKKGTSFHLIT 639
Cdd:cd14921 477 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvDRIVGldqmakmTESSLPSASKTKKGMFRTVG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 640 SLHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPR 719
Cdd:cd14921 557 QLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 636
|
650 660 670
....*....|....*....|....*....|....*...
gi 261245016 720 IFSKSkFVSSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14921 637 AIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
96-757 |
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: 576.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAAISEPKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADI 255
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 256 QIYFLEKSRVVYQQPGERNYHIFYQILSGNQELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAIDVLGFLPD 335
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 336 EKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQVTYAV 415
Cdd:cd14919 241 EQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 416 GALSQSIYERMFQWLVARMNQVLD-AKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEEYRK 494
Cdd:cd14919 321 EALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 495 EGLDWLSIDYGLDVQACIDFIEKPM---GIFSILEEECMLPKATDQMFKTKLFDHHfGKSAYFQTPTSPEKnfEVHFELA 571
Cdd:cd14919 401 EGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKD--KADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 572 HYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTK-------DIIAGSASQF--GEKTHKKGTsFHLITSLH 642
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGMSETAlpGAFKTRKGM-FRTVGQLY 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 643 KENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFS 722
Cdd:cd14919 557 KEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIP 636
|
650 660 670
....*....|....*....|....*....|....*
gi 261245016 723 KSkFVSSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14919 637 KG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
97-757 |
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: 570.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYkRKRRSEvPPHIFAVANRAFQDMLRNGENQSIVFTGE 176
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY-RQKLLD-SPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 177 SGSGKTVNTKLIIQYFATMAAISepkkklGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADIQ 256
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGS------SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 257 IYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVSTnPSDFH-ICSCGVVAVESLDDAKEFLATEKAIDVLGFLP 334
Cdd:cd01383 154 TYLLEKSRVVQLANGERSYHIFYQLCAGaSPALREKLNLKS-ASEYKyLNQSNCLTIDGVDDAKKFHELKEALDTVGISK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 335 DEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQVTYA 414
Cdd:cd01383 233 EDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 415 VGALSQSIYERMFQWLVARMNQVLDA-KLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEEYR 493
Cdd:cd01383 313 RDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 494 KEGLDWLSIDYgLDVQACIDFIE-KPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFqtptspeKNFEVHFELAH 572
Cdd:cd01383 393 LDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFK-------GERGGAFTIRH 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 573 YAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKvLANLF--------TKDIIAGSASQFGEKTHKKGTSFhlitslhKE 644
Cdd:cd01383 465 YAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQ-LPQLFaskmldasRKALPLTKASGSDSQKQSVATKF-------KG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 645 NINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFSKS 724
Cdd:cd01383 537 QLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSAS 616
|
650 660 670
....*....|....*....|....*....|...
gi 261245016 725 KfvSSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd01383 617 Q--DPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
96-757 |
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: 567.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAAISEPKK-------KLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARG 248
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKdqnslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 249 TLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVStNPSDFHICSCGVVAVESLDDAKEFLATEKAI 327
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGaGDKLRSELLLE-NYNNYRFLSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 328 DVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQN 407
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 408 LQQVTYAVGALSQSIYERMFQWLVARMNQVLD-AKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFI 486
Cdd:cd15896 320 QEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 487 LEQEEYRKEGLDWLSIDYGLDVQACIDFIEKPM---GIFSILEEECMLPKATDQMFKTKLFDHHfGKSAYFQTPTSPEKn 563
Cdd:cd15896 400 LEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPKKLKD- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 564 fEVHFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTK-------DIIAGSASQFGEKTHKKGTsFH 636
Cdd:cd15896 478 -EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDvdrivglDKVSGMSEMPGAFKTRKGM-FR 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 637 LITSLHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWIL 716
Cdd:cd15896 556 TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 635
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 261245016 717 NPRIFSKSkFVSSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd15896 636 TPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
96-757 |
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: 566.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYfatMAAISEPKKKlgnLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADI 255
Cdd:cd01381 81 ESGAGKTESTKLILQY---LAAISGQHSW---IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 256 QIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVsTNPSDFHICSCG-VVAVESLDDAKEFLATEKAIDVLGFL 333
Cdd:cd01381 155 EQYLLEKSRIVSQAPDERNYHIFYCMLAGlSAEEKKKLEL-GDASDYYYLTQGnCLTCEGRDDAAEFADIRSAMKVLMFT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 334 PDEKFGCYKLVGAIMHFGNLKFKRNLRE--EQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQV 411
Cdd:cd01381 234 DEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 412 TYAVGALSQSIYERMFQWLVARMNQVL------DAKLTShffVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLF 485
Cdd:cd01381 314 LDVRDAFVKGIYGRLFIWIVNKINSAIykprgtDSSRTS---IGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 486 ILEQEEYRKEGLDWLSIDYgLDVQACIDFI-EKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQtptsPEKNF 564
Cdd:cd01381 391 KLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLK----PKSDL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 565 EVHFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSasqfgEKTHKKGTsfhlITSLHKE 644
Cdd:cd01381 466 NTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGS-----ETRKKSPT----LSSQFRK 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 645 NINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIfSKS 724
Cdd:cd01381 537 SLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGI-PPA 615
|
650 660 670
....*....|....*....|....*....|...
gi 261245016 725 KFVSSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd01381 616 HKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
96-757 |
4.14e-179 |
|
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: 558.56 E-value: 4.14e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAAISEPKKK---LGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSF 252
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEpgvPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 253 ADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQELRNMLLVSTNPSDFHICSCGVVAVESlDDAKEFLATEKAIDVLGF 332
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 333 LPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQVT 412
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 413 YAVGALSQSIYERMFQWLVARMNQVLD-AKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEE 491
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 492 YRKEGLDWLSIDYGLDVQACIDFIEKPM---GIFSILEEECMLPKATDQMFKTKLFDHHfGKSAYFQTPTSPEKnfEVHF 568
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHLRD--QADF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 569 ELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFtKDI--IAG--SASQFGEKT---HKKGTSFHLITSL 641
Cdd:cd14930 477 SVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIW-KDVegIVGleQVSSLGDGPpggRPRRGMFRTVGQL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 642 HKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIF 721
Cdd:cd14930 556 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 635
|
650 660 670
....*....|....*....|....*....|....*.
gi 261245016 722 SKSkFVSSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14930 636 PKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
97-757 |
6.91e-179 |
|
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: 557.16 E-value: 6.91e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTGE 176
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 177 SGSGKTVNTKLIIQYFAtmAAISEPKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADIQ 256
Cdd:cd01378 82 SGAGKTEASKRIMQYIA--AVSGGSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 257 IYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAIDVLGFLPD 335
Cdd:cd01378 160 NYLLEKSRVVGQIKGERNFHIFYQLLKGaSQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 336 EKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTEnADKAAFLMGIHASELLKGLIYPRIKVGNEY---VTRSQNLQQVT 412
Cdd:cd01378 240 EQDSIFRILAAILHLGNIQFAEDEEGNAAISDTSV-LDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 413 YAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFV-GILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEE 491
Cdd:cd01378 319 YARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKViGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 492 YRKEGLDWLSIDYgLDVQACIDFIE-KPMGIFSILEEECMLP-KATDQMFKTKLfDHHFGKSAYFQTPTSPEKNFEVHFE 569
Cdd:cd01378 399 YVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHFELRRGEFR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 570 LAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSasqfgekthKK-----GTSFhlitslhKE 644
Cdd:cd01378 477 IKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDS---------KKrpptaGTKF-------KN 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 645 NINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFSKS 724
Cdd:cd01378 541 SANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAW 620
|
650 660 670
....*....|....*....|....*....|...
gi 261245016 725 KFvSSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd01378 621 DG-TWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
97-757 |
4.69e-177 |
|
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: 552.70 E-value: 4.69e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTGE 176
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 177 SGSGKTVNTKLIIQYFAtmAAISEPKKklgnLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADIQ 256
Cdd:cd14883 82 SGAGKTETTKLILQYLC--AVTNNHSW----VEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 257 IYFLEKSRVVYQQPGERNYHIFYQILSG---NQELRNMLLVStNPSDFHICS-CGVVAVESLDDAKEFLATEKAIDVLGF 332
Cdd:cd14883 156 DYLLEQSRITFQAPGERNYHVFYQLLAGakhSKELKEKLKLG-EPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVLGI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 333 LPDEKFGCYKLVGAIMHFGNLKFKRNLREE-QLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQV 411
Cdd:cd14883 235 PEEMQEGIFSVLSAILHLGNLTFEDIDGETgALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 412 TYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEE 491
Cdd:cd14883 315 RDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 492 YRKEGLDWLSIDYGlDVQACIDFIEK-PMGIFSILEEECMLPKATDQMFKTKLFDHHfGKSAYFQTPTspEKNFEVHFEL 570
Cdd:cd14883 395 YEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPD--RRRWKTEFGV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 571 AHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFT---KDIIAGSASQFGEKTHKKGTSFHLIT--SLHKEN 645
Cdd:cd14883 471 KHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTypdLLALTGLSISLGGDTTSRGTSKGKPTvgDTFKHQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 646 INKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFSKSK 725
Cdd:cd14883 551 LQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADH 630
|
650 660 670
....*....|....*....|....*....|..
gi 261245016 726 fVSSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14883 631 -KETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
96-757 |
5.99e-176 |
|
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: 549.20 E-value: 5.99e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFT 174
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 175 GESGSGKTVNTKLIIQYFATMAAISEPKKKlgNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFAD 254
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGR--SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 255 IQIYFLEKSRVVYQQPGERNYHIFYQILSGNQELRNMLLVSTNPSDFHI---CSCgvVAVESLDDAKEFLATEKAIDVLG 331
Cdd:cd01384 159 IRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYlnqSKC--FELDGVDDAEEYRATRRAMDVVG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 332 FLPDEKFGCYKLVGAIMHFGNLKFKRNLreeqlEADGTENADK--------AAFLMGIHASELLKGLIYPRIKVGNEYVT 403
Cdd:cd01384 237 ISEEEQDAIFRVVAAILHLGNIEFSKGE-----EDDSSVPKDEksefhlkaAAELLMCDEKALEDALCKRVIVTPDGIIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 404 RSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQ 483
Cdd:cd01384 312 KPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 484 LFILEQEEYRKEGLDWLSIDYgLDVQACIDFIE-KPMGIFSILEEECMLPKATDQMFKTKLFdHHFGKSAYFQTPtspeK 562
Cdd:cd01384 392 VFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLY-QTLKDHKRFSKP----K 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 563 NFEVHFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSasqfgekthKKGTSFHLITSLH 642
Cdd:cd01384 466 LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGT---------SSSSKFSSIGSRF 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 643 KENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFS 722
Cdd:cd01384 537 KQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLK 616
|
650 660 670
....*....|....*....|....*....|....*
gi 261245016 723 KSKfvSSRKATEEVLDFLEIDhpHYQCGVTKVFFK 757
Cdd:cd01384 617 GSD--DEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
96-757 |
1.94e-157 |
|
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: 498.70 E-value: 1.94e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFT 174
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 175 GESGSGKTVNTKLIIQYFATMAAisepkKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFAD 254
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWG-----SGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 255 IQIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVSTNpsdfhicscgvvavesLDDAKEFLATEKAIDVLGFL 333
Cdd:cd01382 156 VSHYLLEKSRICVQSKEERNYHIFYRLCAGaPEDLREKLLKDPL----------------LDDVGDFIRMDKAMKKIGLS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 334 PDEKFGCYKLVGAIMHFGNLKFKRNLREE----QLEADGTENADKAAFLMGIHASELLKGLIYpRI-------KVGNEYv 402
Cdd:cd01382 220 DEEKLDIFRVVAAVLHLGNIEFEENGSDSgggcNVKPKSEQSLEYAAELLGLDQDELRVSLTT-RVmqttrggAKGTVI- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 403 TRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVLDAKlTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQ 482
Cdd:cd01382 298 KVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFE-TSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 483 QLFILEQEEYRKEGLDWLSIDYgLDVQACIDFIE-KPMGIFSILEEECMLPKATDQMFKTKLFDHHfGKSAYFQTP-TSP 560
Cdd:cd01382 377 RILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKH-KNHFRLSIPrKSK 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 561 EKnfeVHFELA--------HYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSasqfGEKTHKKG 632
Cdd:cd01382 455 LK---IHRNLRddegflirHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK----DSKQKAGK 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 633 TSFHLITSLHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQR 712
Cdd:cd01382 528 LSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNM 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 261245016 713 Y--------WILNPRIFSKSKFvssrKAteevLDFLEIDhphYQCGVTKVFFK 757
Cdd:cd01382 608 YkkylppklARLDPRLFCKALF----KA----LGLNEND---FKFGLTKVFFR 649
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
96-757 |
2.31e-157 |
|
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: 498.92 E-value: 2.31e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFT 174
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 175 GESGSGKTVNTKLIIQYFATMAaisepkkklGNLED----QIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTL 250
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA---------GGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 251 SFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQELRNMLLVSTNPSDFhICSCGVVAVESLDDAKEFLATEKAIDVL 330
Cdd:cd14903 152 VGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAY-TGANKTIKIEGMSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 331 GFLPDEKFGCYKLVGAIMHFGNLKF--KRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNL 408
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIqsKPNDDEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 409 QQVTYAVGALSQSIYERMFQWLVARMNQVL--DAKLTSHffVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFI 486
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASLgnDAKMANH--IGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 487 LEQEEYRKEGLDWLSIDYgLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPEKNFEV 566
Cdd:cd14903 389 TVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 567 HfelaHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDII---AGSASQFGEKTHKKGTSFHLIT--SL 641
Cdd:cd14903 468 K----HYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVEspaAASTSLARGARRRRGGALTTTTvgTQ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 642 HKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIF 721
Cdd:cd14903 544 FKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGR 623
|
650 660 670
....*....|....*....|....*....|....*..
gi 261245016 722 SKSKFVssRKATEEVLDFLEIDHP-HYQCGVTKVFFK 757
Cdd:cd14903 624 NTDVPV--AERCEALMKKLKLESPeQYQMGLTRIYFQ 658
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
96-757 |
5.83e-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: 490.06 E-value: 5.83e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNG----ENQS 170
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSGvldpSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 171 IVFTGESGSGKTVNTKLIIQYFA-------------TMAAISEPKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFG 237
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLAritsgfaqgasgeGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 238 KLIRIHFGARGTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQE-LRNMLLVsTNPSDFHICSCGVVAVESLDD 316
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEaLRERLKL-QTPVEYFYLRGECSSIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 317 AKEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGT-ENADKAAFLMGIHASELLKGLIYPRI 395
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 396 KVGNEYVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEK 475
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 476 LQQFFNQQLFILEQEEYRKEGLDWLSIDYGlDVQACIDFIE-----KPmGIFSILeEEC--MLPKATDQMFKTKLFDHHF 548
Cdd:cd14890 400 LQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgkvngKP-GIFITL-DDCwrFKGEEANKKFVSQLHASFG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 549 GKSAYFQTPTSPEKN-FEVH--------FELAHYAGVVPYNISGWIGKNkgllNETVVALLqkssnkvlanlftKDIIAG 619
Cdd:cd14890 477 RKSGSGGTRRGSSQHpHFVHpkfdadkqFGIKHYAGDVIYDASGFNEKN----NETLNAEM-------------KELIKQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 620 SASQFGEKThkKGTSFHliTSLHkeninKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEA 699
Cdd:cd14890 540 SRRSIREVS--VGAQFR--TQLQ-----ELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQG 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 261245016 700 FPSWMLYDDFKQRYWILNPRIFSKSKFVssrkatEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14890 611 FALREEHDSFFYDFQVLLPTAENIEQLV------AVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
96-755 |
7.24e-153 |
|
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: 486.60 E-value: 7.24e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAY------KRKRRSEVPPHIFAVANRAFQDMLR----N 165
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFasrgQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 166 GENQSIVFTGESGSGKTVNTKLIIQYfatMAAISEPKKKLG------NLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKL 239
Cdd:cd14901 81 KCDQSILVSGESGAGKTETTKIIMNY---LASVSSATTHGQnatereNVRDRVLESNPILEAFGNARTNRNNNSSRFGKF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 240 IRIHFGARGTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSG--NQELRNMLLVSTNPSDFHICSCGVVAVESLDDA 317
Cdd:cd14901 158 IRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGasSDELHALGLTHVEEYKYLNSSQCYDRRDGVDDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 318 KEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKF-KRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIK 396
Cdd:cd14901 238 VQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 397 VGNEYVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVL--DAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNE 474
Cdd:cd14901 318 AGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaySESTGASRFIGIVDIFGFEIFATNSLEQLCINFANE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 475 KLQQFFNQQLFILEQEEYRKEGLDWLSIDYGlDVQACIDFIE-KPMGIFSILEEECMLPKATDQMFKTKLFDhHFGKSAY 553
Cdd:cd14901 398 KLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYD-LLAKHAS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 554 FQtpTSPEKNFEVHFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLAnlftkdiiAGSASQFgekthkkgt 633
Cdd:cd14901 476 FS--VSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS--------STVVAKF--------- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 634 sfhlitslhKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRY 713
Cdd:cd14901 537 ---------KVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTY 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 261245016 714 WILNPRIFSKS----KFVSSRKATEEVLDFLEIDHPHYQCGVTKVF 755
Cdd:cd14901 608 SCLAPDGASDTwkvnELAERLMSQLQHSELNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
96-718 |
4.06e-152 |
|
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: 484.97 E-value: 4.06e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQKEVMAAYKRKRRSEvPPHIFAVANRAFQDMLRNGENQSIVFT 174
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSISK-SPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 175 GESGSGKTVNTKLIIQYFATMAaiSEPKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHF---------G 245
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAG--SEDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklkskrmsG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 246 ARGTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQELRN-----------------MLLVSTNPSDF--HI--- 303
Cdd:cd14888 158 DRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNtglsyeendeklakgadAKPISIDMSSFepHLkfr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 304 ---CScGVVAVESLDDAKEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREE---QLEADGTENADKAAF 377
Cdd:cd14888 238 yltKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSegaVVSASCTDDLEKVAS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 378 LMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVLD-AKLTSHFFVGILDTTGF 456
Cdd:cd14888 317 LLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGVLDIFGF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 457 EILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEEYRKEGLDWLSIDYGlDVQACID-FIEKPMGIFSILEEECMLPKAT 535
Cdd:cd14888 397 ECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDlLQEKPLGIFCMLDEECFVPGGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 536 DQMFKTKLFDHHFGKSAYFQTPTSPEkNFEVHfelaHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKD 615
Cdd:cd14888 476 DQGLCNKLCQKHKGHKRFDVVKTDPN-SFVIV----HFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSAY 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 616 IiagsASQFGEKTHKKGtsFHLITSLHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRV 695
Cdd:cd14888 551 L----RRGTDGNTKKKK--FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQV 624
|
650 660
....*....|....*....|...
gi 261245016 696 CCEAFPSWMLYDDFKQRYWILNP 718
Cdd:cd14888 625 SRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
96-757 |
2.38e-151 |
|
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: 483.80 E-value: 2.38e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYfatMAAISEpKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADI 255
Cdd:cd01385 81 ESGSGKTESTNFLLHH---LTALSQ-KGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 256 QIYFLEKSRVVYQQPGERNYHIFYQILSGNQELRNMLLVSTNPSDFH-ICSCGVVAVESLDDAKEFLATEKAIDVLGFLP 334
Cdd:cd01385 157 EKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHyLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 335 DEKFGCYKLVGAIMHFGNLKFKRNL--REEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQVT 412
Cdd:cd01385 237 ETQRQIFSVLSAVLHLGNIEYKKKAyhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 413 YAVGALSQSIYERMFQWLVARMNQ-VLDAKLTSH---FFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILE 488
Cdd:cd01385 317 ATRDAMAKCLYSALFDWIVLRINHaLLNKKDLEEakgLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 489 QEEYRKEGLDWLSIDYgLDVQACIDFIE-KPMGIFSILEEECMLPKATDQMFKTKlFDHHFGKSAYFQTPTSPEKNFEVH 567
Cdd:cd01385 397 QEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQVMEPAFIIA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 568 felaHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKD--------------------IIAGSASQ---- 623
Cdd:cd01385 475 ----HYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDpvavfrwavlrafframaafREAGRRRAqrta 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 624 -FGEKTHKKGTSFHLITSLHKE----------NINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEG 692
Cdd:cd01385 551 gHSLTLHDRTTKSLLHLHKKKKppsvsaqfqtSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLET 630
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261245016 693 IRVCCEAFPSWMLYDDFKQRYWILNPRIFSKSKfvssrkatEEVLDFLE---IDHPHYQCGVTKVFFK 757
Cdd:cd01385 631 VRIRRSGYSVRYTFQEFITQFQVLLPKGLISSK--------EDIKDFLEklnLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
96-757 |
2.89e-150 |
|
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: 478.89 E-value: 2.89e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAAISepkkklGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADI 255
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGST------NGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 256 QIYFLEKSRVVYQQPGERNYHIFYQIL-SGNQELRNMLLVSTNPSDFHICSCgvVAVESLDDAKEFLATEKAIDVLGFLP 334
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLaSPDPASRGGWGSSAAYGYLSLSGC--IEVEGVDDVADFEEVVLAMEQLGFDD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 335 DEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENAD---KAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQ-NLQQ 410
Cdd:cd14872 233 ADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDvlkEVATLLGVDAATLEEALTSRLMEIKGCDPTRIPlTPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 411 VTYAVGALSQSIYERMFQWLVARMNQVLD-AKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQ 489
Cdd:cd14872 313 ATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 490 EEYRKEGLDWLSIDYgLDVQACIDFIEK-PMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSayFQTPTSPEKNfEVHF 568
Cdd:cd14872 393 ALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS--TFVYAEVRTS-RTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 569 ELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFtkdiiagSASQFGEKThKKGTsfhlITSLHKENINK 648
Cdd:cd14872 469 IVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF-------PPSEGDQKT-SKVT----LGGQFRKQLSA 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 649 LMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIfSKSKFVS 728
Cdd:cd14872 537 LMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTI-AKRVGPD 615
|
650 660
....*....|....*....|....*....
gi 261245016 729 SRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14872 616 DRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
96-757 |
1.70e-145 |
|
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: 466.54 E-value: 1.70e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQ-KEVMAAYK-RKRRSEVPPHIFAVANRAFQDMLR----NGEN 168
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPlLYDvPGFDSQRKeEATASSPPPHVFSIAERAYRAMKGvgkgQGTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 169 QSIVFTGESGSGKTVNTKLIIQYFATMAAISEPKKKLGN-------LEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIR 241
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGaanahesIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 242 IHFGARGTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQELRNMLLVSTNPSDFHICSCG-VVAVESLDDAKEF 320
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 321 LATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQL--EADGTENADKAAFLMGIHASELLKGLIYpRIKVG 398
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVfaQSADGVNVAKAAGLLGVDAAELMFKLVT-QTTST 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 399 neyvTRSQNLQ------QVTYAVGALSQSIYERMFQWLVARMN----------QVLDAKLTSHFFVGILDTTGFEILDYN 462
Cdd:cd14892 320 ----ARGSVLEikltarEAKNALDALCKYLYGELFDWLISRINachkqqtsgvTGGAASPTFSPFIGILDIFGFEIMPTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 463 SLEQLCINFTNEKLQQFFNQQLFILEQEEYRKEGLDWLSIDYGlDVQACIDFIEK-PMGIFSILEEECMLP-KATDQMFK 540
Cdd:cd14892 396 SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 541 TKLFDHHFGKSAYFQTPtspekNFEV-HFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQkssnkvlanlftkdiiag 619
Cdd:cd14892 475 TIYHQTHLDKHPHYAKP-----RFECdEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLR------------------ 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 620 SASQFgekthkkgtsfhlitslhKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEA 699
Cdd:cd14892 532 SSSKF------------------RTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREG 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261245016 700 FPSWMLYDDFKQRYWIL-------NPRIFSKSKFVSSRKATEEVLDFLEIDhpHYQCGVTKVFFK 757
Cdd:cd14892 594 FPIRRQFEEFYEKFWPLarnkagvAASPDACDATTARKKCEEIVARALERE--NFQLGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
96-757 |
3.19e-143 |
|
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: 460.03 E-value: 3.19e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFT 174
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 175 GESGSGKTVNTKLIIQYFATMAAIS---EPKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLS 251
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSlelSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 252 FADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQELRNMLLVSTNPSDFHICS-CGVVAVESLDDAKEFLATEKAIDVL 330
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 331 GFLPDEKFGCYKLVGAIMHFGNLKFkrnlreeqLEADGTENADKAAF-----LMGIHASELLKGLIYPRIKVGNEYVTRS 405
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKTALgrsaeLLGLDPTQLTDALTQRSMFLRGEEILTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 406 QNLQQVTYAVGALSQSIYERMFQWLVARMNQVLDAKltSHF-FVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQL 484
Cdd:cd14873 313 LNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGK--EDFkSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 485 FILEQEEYRKEGLDWLSIDYgLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHfGKSAYFQTPTSPEKNF 564
Cdd:cd14873 391 FSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPRVAVNNF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 565 EVHfelaHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSASQFGEKT-HKKGTsfhlITSLHK 643
Cdd:cd14873 469 GVK----HYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSkHRRPT----VSSQFK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 644 ENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFSK 723
Cdd:cd14873 541 DSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALP 620
|
650 660 670
....*....|....*....|....*....|....
gi 261245016 724 SKFvssRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14873 621 EDV---RGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
97-757 |
3.24e-142 |
|
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: 456.35 E-value: 3.24e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTGE 176
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 177 SGSGKTVNTKLIIQYFATMAaisepKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADIQ 256
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG-----KANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 257 IYFLEKSRVVYQQPGERNYHIFYQILSGNQE---LRNMLLVSTNPSD-FHICSCGVVAVESLDDAKE-FLATEKAIDVLG 331
Cdd:cd01379 157 EYLLEKSRVVHQAIGERNFHIFYYIYAGLAEdkkLAKYKLPENKPPRyLQNDGLTVQDIVNNSGNREkFEEIEQCFKVIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 332 FLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEAD----GTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQN 407
Cdd:cd01379 237 FTKEEVDSVYSILAAILHIGDIEFTEVESNHQTDKSsrisNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 408 LQQVTYAVGALSQSIYERMFQWLVARMNQVL-------DAKLTshffVGILDTTGFEILDYNSLEQLCINFTNEKLQQFF 480
Cdd:cd01379 317 VEEATDARDAMAKALYGRLFSWIVNRINSLLkpdrsasDEPLS----IGILDIFGFENFQKNSFEQLCINIANEQIQYYF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 481 NQQLFILEQEEYRKEGLDWLSIDYGlDVQACID-FIEKPMGIFSILEEECMLPKATDQMFKTKLfdHHFGKSAYFQTPTS 559
Cdd:cd01379 393 NQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKF--HNNIKSKYYWRPKS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 560 PEKNFEVHfelaHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLanlftkdiiagsasqfgekthKKGTSFHLIT 639
Cdd:cd01379 470 NALSFGIH----HYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV---------------------RQTVATYFRY 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 640 SLHkeninKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNpr 719
Cdd:cd01379 525 SLM-----DLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLA-- 597
|
650 660 670
....*....|....*....|....*....|....*....
gi 261245016 720 iFSKSKFV-SSRKATEEVLDFLEIDhpHYQCGVTKVFFK 757
Cdd:cd01379 598 -FKWNEEVvANRENCRLILERLKLD--NWALGKTKVFLK 633
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
96-757 |
3.51e-141 |
|
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: 454.60 E-value: 3.51e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAaisepkKKLGNL-EDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFgARGTLSFAD 254
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN------QRRNNLvTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 255 IQIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAIDVLGFL 333
Cdd:cd01387 154 TSQYLLEKSRIVTQAKNERNYHVFYELLAGlPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 334 PDEKFGCYKLVGAIMHFGNLKF-KRNLR--EEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQ 410
Cdd:cd01387 234 SEEQDSIFRILASVLHLGNVYFhKRQLRhgQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 411 VTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQE 490
Cdd:cd01387 314 ALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 491 EYRKEGLDWLSIDYgLDVQACIDFI-EKPMGIFSILEEECMLPKATDQMFKTKLFDHHfGKSAYFQTPTSPEKNFEVHfe 569
Cdd:cd01387 394 EYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPRMPLPEFTIK-- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 570 laHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKdiiagSASQFGEKTHKKGTS--------FHLITSL 641
Cdd:cd01387 470 --HYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSS-----HRAQTDKAPPRLGKGrfvtmkprTPTVAAR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 642 HKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYwilnpRIF 721
Cdd:cd01387 543 FQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRY-----RCL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 261245016 722 SKSKFVSSRKATEEVLDFLEID----HPHYQCGVTKVFFK 757
Cdd:cd01387 618 VALKLPRPAPGDMCVSLLSRLCtvtpKDMYRLGATKVFLR 657
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
96-757 |
3.77e-135 |
|
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: 436.81 E-value: 3.77e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKR-RSEVPPHIFAVANRAFQDMLRNGENQSIVFT 174
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 175 GESGSGKTVNTKLIIQYFATMAAISEPkkklgNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFAD 254
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDS-----DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 255 IQIYFLEKSRVVYQQPGERNYHIFYQILSG--NQELRNMLLvsTNPSDFHICSCGVVAVESLDDAKEF----LATEKAID 328
Cdd:cd14897 156 IDDYLLEKSRVVHRGNGEKNFHIFYALFAGmsRDRLLYYFL--EDPDCHRILRDDNRNRPVFNDSEELeyyrQMFHDLTN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 329 VL---GFLPDEKFGCYKLVGAIMHFGNLKFkrnlrEEQLEADGTENADK-----AAFLMGIHASELLKGLIYPRIKVGNE 400
Cdd:cd14897 234 IMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTIRGE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 401 YVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMN-----QVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEK 475
Cdd:cd14897 309 RIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINrnlwpDKDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNER 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 476 LQQFFNQQLFILEQEEYRKEGLDWLSIDYGlDVQACID-FIEKPMGIFSILEEECMLPKATDQMFKTKLFDhHFGKSAYF 554
Cdd:cd14897 389 LQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLElFFKKPLGILPLLDEESTFPQSTDSSLVQKLNK-YCGESPRY 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 555 QTPTSPEKNFEVHfelaHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTkdiiagsaSQFgekthkkgts 634
Cdd:cd14897 467 VASPGNRVAFGIR----HYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT--------SYF---------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 635 fhlitslhKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYW 714
Cdd:cd14897 525 --------KRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYK 596
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 261245016 715 ILNPriFSKSKFVSSRKATEEVLDFLEIDhpHYQCGVTKVFFK 757
Cdd:cd14897 597 EICD--FSNKVRSDDLGKCQKILKTAGIK--GYQFGKTKVFLK 635
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
98-757 |
9.66e-134 |
|
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: 433.95 E-value: 9.66e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 98 VLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDML----RNGENQSIVF 173
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 174 TGESGSGKTVNTKLIIQYfatmaaISEPKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFgARGTLSFA 253
Cdd:cd14889 83 SGESGAGKTESTKLLLRQ------IMELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 254 DIQIYFLEKSRVVYQQPGERNYHIFYQILSG----NQELRNMLlvstNPSDFHICSCGVVAVESLDD-AKEFLATEKAID 328
Cdd:cd14889 156 KINEYLLEKSRVVHQDGGEENFHIFYYMFAGisaeDRENYGLL----DPGKYRYLNNGAGCKREVQYwKKKYDEVCNAMD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 329 VLGFLPDEKFGCYKLVGAIMHFGNLKFKrnlrEEQLEADGTENADK-----AAFLMGIHASELLKGLIYPRIKVGNEYVT 403
Cdd:cd14889 232 MVGFTEQEEVDMFTILAGILSLGNITFE----MDDDEALKVENDSNgwlkaAAGQFGVSEEDLLKTLTCTVTFTRGEQIQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 404 RSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHF---FVGILDTTGFEILDYNSLEQLCINFTNEKLQQFF 480
Cdd:cd14889 308 RHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVelrEIGILDIFGFENFAVNRFEQACINLANEQLQYFF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 481 NQQLFILEQEEYRKEGLDWLSIDYgLDVQACID-FIEKPMGIFSILEEECMLPKATDQMFKTKLfDHHFGKSAYFQTPTS 559
Cdd:cd14889 388 NHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDlFLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGKSRS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 560 PEKNFEVHfelaHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSASQFGEKTHKKG------T 633
Cdd:cd14889 466 KSPKFTVN----HYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGsdnfnsT 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 634 SFHLITSLHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRY 713
Cdd:cd14889 542 RKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERY 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 261245016 714 WIL--NPRI-FSKSKFVSSRKATEEVldfleidhpHYQCGVTKVFFK 757
Cdd:cd14889 622 KILlcEPALpGTKQSCLRILKATKLV---------GWKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
96-725 |
3.88e-133 |
|
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: 432.53 E-value: 3.88e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQKEVMAAYKRK--------RRSEVPPHIFAVANRAFQDMLRNG 166
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 167 ENQSIVFTGESGSGKTVNTKLIIQYFATMAA--------------ISEPKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDN 232
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 233 SSRFGKLIRIHFGAR-GTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGN--QELRNMLLVSTNPSDF--HICSCG 307
Cdd:cd14907 161 SSRFGKYVSILVDKKkRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGAdqQLLQQLGLKNQLSGDRydYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 308 VVAVESLDDAKEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNL--REEQLEADGTENADKAAFLMGIHASE 385
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 386 LLKGLIYPRIKVGNEYVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQ------VLDAKLTSHFF--VGILDTTGFE 457
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDtimpkdEKDQQLFQNKYlsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 458 ILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEEYRKEGL-DWLS-IDYgLDVQACIDFIEK-PMGIFSILEEECMLPKA 534
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLeDYLNqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 535 TDQMFKTKLFDHHFGKSAYFQTPTSPEKNFEVHfelaHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTK 614
Cdd:cd14907 480 TDEKLLNKIKKQHKNNSKLIFPNKINKDTFTIR----HTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSG 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 615 DIiaGSASQFGEKTHKKGTSFHLITSLHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIR 694
Cdd:cd14907 556 ED--GSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIR 633
|
650 660 670
....*....|....*....|....*....|..
gi 261245016 695 VCCEAFPSWMLYDDFKQRYWILNPRI-FSKSK 725
Cdd:cd14907 634 VRKQGYPYRKSYEDFYKQYSLLKKNVlFGKTK 665
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
97-716 |
1.63e-129 |
|
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: 420.87 E-value: 1.63e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQKEVMAAY-----------KRKRRSEVPPHIFAVANRAFQDMLR 164
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 165 --NGE--NQSIVFTGESGSGKTVNTKLIIQYFATM------AAISEPKKKLGnLEDQIVKMNPLLEAFGNAKTQKNDNSS 234
Cdd:cd14900 82 glNGVmsDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlaASVSMGKSTSG-IAAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 235 RFGKLIRIHFGARGTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGnqelrnmllvstnpsdfhicscgvvAVESL 314
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIG-------------------------ASEAA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 315 DDAKEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENA-------DKAAFLMGIHASELL 387
Cdd:cd14900 216 RKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 388 KGLIYPRIKVGNEYVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVL--DAKLTSH---FFVGILDTTGFEILDYN 462
Cdd:cd14900 296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmDDSSKSHgglHFIGILDIFGFEVFPKN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 463 SLEQLCINFTNEKLQQFFNQQLFILEQEEYRKEGLDWLSIDYGlDVQACIDFI-EKPMGIFSILEEECMLPKATDQMFKT 541
Cdd:cd14900 376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLAS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 542 KLFdHHFGKSAYFQtpTSPEKNFEVHFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQkssnkvlanlftkdiiagSA 621
Cdd:cd14900 455 KLY-RACGSHPRFS--ASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV------------------YG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 622 SQFgekthkkgtsfhlitslhKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFP 701
Cdd:cd14900 514 LQF------------------KEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFP 575
|
650
....*....|....*
gi 261245016 702 SWMLYDDFKQRYWIL 716
Cdd:cd14900 576 IRLLHDEFVARYFSL 590
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
96-713 |
5.16e-127 |
|
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: 416.99 E-value: 5.16e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQKEVMAAYKR--------KRRSEVPPHIFAVANRAFQDMLRNG 166
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKAsmtstspvSQLSELPPHVFAIGGKAFGGLLKPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 167 E-NQSIVFTGESGSGKTVNTKLIIQYFATM----AAISEPKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIR 241
Cdd:cd14902 81 RrNQSILVSGESGSGKTESTKFLMQFLTSVgrdqSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 242 IHFGARGTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQELRNMLLVSTNPSDFHI-----CSCGVVAVESLDD 316
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELlnsygPSFARKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 317 AKEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFK---RNLREEQLEADGTENADKAAFLMGIHASELLKGLIYP 393
Cdd:cd14902 241 AQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTaenGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 394 RIKVGNEYVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFF---------VGILDTTGFEILDYNSL 464
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 465 EQLCINFTNEKLQQFFNQQLFILEQEEYRKEGLDWLSIDYGlDVQACIDFIE-KPMGIFSILEEECMLPKATDQMFKTKL 543
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSNQALSTKF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 544 FDHHfgksayfqtptSPEKNFEVHfelaHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSASQ 623
Cdd:cd14902 480 YRYH-----------GGLGQFVVH----HFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSPGAD 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 624 FGEKTHKKGTSFHL--ITSLHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFP 701
Cdd:cd14902 545 NGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYS 624
|
650
....*....|..
gi 261245016 702 SWMLYDDFKQRY 713
Cdd:cd14902 625 VRLAHASFIELF 636
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
96-757 |
1.58e-124 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 407.24 E-value: 1.58e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAaisepKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFgARGTLSFADI 255
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLY-----QDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 256 QIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAIDVLGFLP 334
Cdd:cd14896 155 SHYLLETSRVVFQAQAERSFHVFYELLAGlDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 335 DEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENAD--KAAFLMGIHAsELLKGLIYPRIKVGN-EYVTRSQNLQQV 411
Cdd:cd14896 235 EELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQVPP-ERLEGAVTHRVTETPyGRVSRPLPVEGA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 412 TYAVGALSQSIYERMFQWLVARMNQVLDAKLT--SHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQ 489
Cdd:cd14896 314 IDARDALAKTLYSRLFTWLLKRINAWLAPPGEaeSDATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 490 EEYRKEGLDWLSIdYGLDVQACIDFI-EKPMGIFSILEEECMLPKATDQMFKTKLFDHHfGKSAYFQTPTSPEKNFEVHf 568
Cdd:cd14896 394 EECQRELLPWVPI-PQPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQLPLPVFTVR- 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 569 elaHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKdiiagSASQFGEKTHKKGTSFHLITSLhkeniNK 648
Cdd:cd14896 471 ---HYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE-----AEPQYGLGQGKPTLASRFQQSL-----GD 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 649 LMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRifsKSKFVS 728
Cdd:cd14896 538 LTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSE---RQEALS 614
|
650 660 670
....*....|....*....|....*....|
gi 261245016 729 SRKATEEVL-DFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14896 615 DRERCGAILsQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
96-757 |
3.16e-124 |
|
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: 406.64 E-value: 3.16e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFT 174
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 175 GESGSGKTVNTKLIIQYFATMAAISEPKKKlgnleDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFAD 254
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTI-----AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 255 IQIYFLEKSRVVYQQPGERNYHIFYQILSG--NQELRNMLLVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAIDVLGF 332
Cdd:cd14904 156 CETYLLEKSRVVSIAEGERNYHIFYQLLAGlsSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 333 LPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGtENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQVT 412
Cdd:cd14904 236 DNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNG-SQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 413 YAVGALSQSIYERMFQWLVARMNQVL---DAKLTSHffVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQ 489
Cdd:cd14904 315 ENRDALAKAIYSKLFDWMVVKINAAIstdDDRIKGQ--IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 490 EEYRKEGLDWLSIDYGlDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHH--FGKSAYFQTPtspeKNFEVH 567
Cdd:cd14904 393 EEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFP----KVKRTQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 568 FELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFtkDIIAGSASQFGEKTHKKGTSFHLITSLHKENIN 647
Cdd:cd14904 468 FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF--GSSEAPSETKEGKSGKGTKAPKSLGSQFKTSLS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 648 KLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWIL-NPRIFSKskf 726
Cdd:cd14904 546 QLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMfPPSMHSK--- 622
|
650 660 670
....*....|....*....|....*....|..
gi 261245016 727 vSSRKATEEVLDFLEIDHP-HYQCGVTKVFFK 757
Cdd:cd14904 623 -DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
838-1914 |
1.69e-123 |
|
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: 418.04 E-value: 1.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 838 EEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKSKVELEVKIKELSRQV 917
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 918 EEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQQT 997
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 998 QEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLRKKEFE 1077
Cdd:pfam01576 165 TSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1078 MGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNERLEEAGGTSLAQMEITKQ 1157
Cdd:pfam01576 245 LQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1158 QEARFQKLHHDMEETTRHFEATSASLKKRHAENLAELEGQVEHLQQVRLVLEQDKSDLQLQVDDLLNRVDQMARAKANAE 1237
Cdd:pfam01576 325 REQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1238 KLCGLYERRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQ 1317
Cdd:pfam01576 405 HKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQK 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1318 SALSHALQSAKHDYDLLREQYEEEQEVKAELHRALSKGNKETVQWRAKYEHDAMQrTEDLEEAKKKLAIRLQEAAEAMEV 1397
Cdd:pfam01576 485 LNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT-LEALEEGKKRLQRELEALTQQLEE 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1398 SNAKNASLERARHRLQLELGDALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEVLTFRQ 1477
Cdd:pfam01576 564 KAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLAR 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1478 ACEESTEAQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALERNESKILRFQLELS 1557
Cdd:pfam01576 644 ALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQ 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1558 EAKAELERKLSEKEEEAERLREKHQQAMGSLQSNLDLEASSRIEATRLRKKMEGDLKEMEIQLCAANRQVSQMTRALGQL 1637
Cdd:pfam01576 724 ALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKL 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1638 QGQMKDLHQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATERINLFHTQNTSLLSQ 1717
Cdd:pfam01576 804 QAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDE 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1718 KKKLEADVAQVQKEAGEMLQACQKAEEKAKKTAAEAANMSEELKKEQDTNAHLERMRKNMEQTIKDLQKRLDEAEQTAVL 1797
Cdd:pfam01576 884 KRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKS 963
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1798 GSKKQIQKLESRVRDLEGELESEVRRSAEAQREARRLERGIKELTYQAEEDKKNLSRMQALSDKLQLKVQSYKQQVEAAE 1877
Cdd:pfam01576 964 KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAE 1043
|
1050 1060 1070
....*....|....*....|....*....|....*..
gi 261245016 1878 AQANQYLSKYKKQQHELNEAKERAEAAESQVNKLRAK 1914
Cdd:pfam01576 1044 EEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
96-757 |
1.69e-120 |
|
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: 395.95 E-value: 1.69e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTL--RRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEvmaAYKRKRRSEVPPHIFAVANRAFQDMLRNGE---NQS 170
Cdd:cd14891 1 AGILHNLeeRSKLDNQRPYTFMANVLIAVNPLRRLPEPDKS---DYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 171 IVFTGESGSGKTVNTKlIIQYFATMAAISEPKKKLGN--------------LEDQIVKMNPLLEAFGNAKTQKNDNSSRF 236
Cdd:cd14891 78 IVISGESGAGKTETSK-IILRFLTTRAVGGKKASGQDieqsskkrklsvtsLDERLMDTNPILESFGNAKTLRNHNSSRF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 237 GKLIRIHFGARG-TLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQELRNMLLVSTNPSDFH-ICSCGVVAVESL 314
Cdd:cd14891 157 GKFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIyLNQSGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 315 DDAKEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKA----AFLMGIHASELLKGL 390
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEAlataAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 391 IYPRIKVGNEYVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILD-YNSLEQLCI 469
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 470 NFTNEKLQQFFNQQLFILEQEEYRKEGLDWLSIDYGlDVQACIDFI-EKPMGIFSILEEECMLPKATDQMFKTKLFDHHf 548
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 549 GKSAYFqtPTSPEKNFEVHFELAHYAGVVPYNISGWIGKNkgllNETVvallqkssNKVLANLFTkdiiagSASQFGEKT 628
Cdd:cd14891 475 KRHPCF--PRPHPKDMREMFIVKHYAGTVSYTIGSFIDKN----NDII--------PEDFEDLLA------SSAKFSDQM 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 629 HkkgtsfhlitslhkeninKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDD 708
Cdd:cd14891 535 Q------------------ELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAE 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 261245016 709 FKQRYWILNPRIfSKSKFVSSRKA-TEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14891 597 LVDVYKPVLPPS-VTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
58-810 |
6.52e-114 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 382.84 E-value: 6.52e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 58 VETRDGEIMRIKEDKLQQMNpeelEMIE-----DLSMLLYLNEASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQ 132
Cdd:PTZ00014 71 IDPPTNSTFEVKPEHAFNAN----SQIDpmtygDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 133 KEVMAAYKRKRRSE-VPPHIFAVANRAFQDMLRNGENQSIVFTGESGSGKTVNTKLIIQYFATmaaisePKKKLGNLEDQ 211
Cdd:PTZ00014 147 NDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS------SKSGNMDLKIQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 212 IVKM--NPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSG-NQEL 288
Cdd:PTZ00014 221 NAIMaaNPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGaNDEM 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 289 RNMLLVStNPSDFHICSCGVVAVESLDDAKEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFkrnlreEQLEADG 368
Cdd:PTZ00014 301 KEKYKLK-SLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEI------EGKEEGG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 369 TENA-----------DKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQV 437
Cdd:PTZ00014 374 LTDAaaisdeslevfNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNAT 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 438 LDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEEYRKEGLDWLSIDYgLDVQACIDFI-E 516
Cdd:PTZ00014 454 IEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLcG 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 517 KPMGIFSILEEECMLPKATDQMF----KTKLFDHHFgksaYFQTPTSPEKNFEVhfelAHYAGVVPYNISGWIGKNKGLL 592
Cdd:PTZ00014 533 KGKSVLSILEDQCLAPGGTDEKFvsscNTNLKNNPK----YKPAKVDSNKNFVI----KHTIGDIQYCASGFLFKNKDVL 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 593 NETVVALLQKSSNKVLANLFTKDIIagSASQFGEKThkkgtsfhLITSLHKENINKLMTDLKSTAPHFVRCINPNKNKIP 672
Cdd:PTZ00014 605 RPELVEVVKASPNPLVRDLFEGVEV--EKGKLAKGQ--------LIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKP 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 673 GVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIfSKSKFVSSRKATEEVLDFLEIDHPHYQCGVT 752
Cdd:PTZ00014 675 LDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAV-SNDSSLDPKEKAEKLLERSGLPKDSYAIGKT 753
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 261245016 753 KVFFKAFILDQLEERRDEKISKVFTLFQArARGKLMRITFQKILEER-DALALIQENIR 810
Cdd:PTZ00014 754 MVFLKKDAAKELTQIQREKLAAWEPLVSV-LEALILKIKKKRKVRKNiKSLVRIQAHLR 811
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
96-757 |
1.35e-110 |
|
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: 368.85 E-value: 1.35e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYK-----RKRRSEVP----PHIFAVANRAFQDMLRNG 166
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqegllRSQGIESPqalgPHVFAIADRSYRQMMSEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 167 E-NQSIVFTGESGSGKTVNTKLIIQYFATMAA----ISEPKKKLGNLE--DQIVKMNPLLEAFGNAKTQKNDNSSRFGKL 239
Cdd:cd14908 81 RaSQSILISGESGAGKTESTKIVMLYLTTLGNgeegAPNEGEELGKLSimDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 240 IRIHFGARGTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQ-------ELRNMLLVSTN-PSDFHICSCG-VVA 310
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDeeehekyEFHDGITGGLQlPNEFHYTGQGgAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 311 VESLDDAKEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENAD---KAAFLMGIHASELL 387
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKclaRVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 388 KGLIYPRIKVGNEYVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVL--DAKLTSHFFVGILDTTGFEILDYNSLE 465
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 466 QLCINFTNEKLQQFFNQQLFILEQEEYRKEGLDWLSIDYGlDVQACIDFIE-KPMGIFSILEEECMLP-KATDQMFKTKL 543
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 544 FDHHFgksayfqtptsPEKNFEVH----------------FELAHYAGVVPYNI-SGWIGKNKGLLNetvvallqkssnk 606
Cdd:cd14908 480 YETYL-----------PEKNQTHSentrfeatsiqktkliFAVRHFAGQVQYTVeTTFCEKNKDEIP------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 607 vlanlFTKDIIAGSASQFgekthkkgtsfhlitslhKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRC 686
Cdd:cd14908 536 -----LTADSLFESGQQF------------------KAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRY 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 687 NGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRI--FSKSKFVSSRKATEEVLDFLEIDHPHY----------------- 747
Cdd:cd14908 593 GGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPLIpeVVLSWSMERLDPQKLCVKKMCKDLVKGvlspamvsmknipedtm 672
|
730
....*....|
gi 261245016 748 QCGVTKVFFK 757
Cdd:cd14908 673 QLGKSKVFMR 682
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
97-757 |
8.63e-108 |
|
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: 361.58 E-value: 8.63e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQ----KEVMAAYkrkrrSEVPPHIFAVANRAFQDMLR------- 164
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYDlhkyREEMPGW-----TALPPHVFSIAEGAYRSLRRrlhepga 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 165 NGENQSIVFTGESGSGKTVNTKLIIQYFA----TMAAISEPKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLI 240
Cdd:cd14895 77 SKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 241 RIHFGAR---GTLSFA--DIQIYFLEKSRVVYQQPGERNYHIFYQILSG--NQELRNMLLVSTNPSDFHICSCG--VVAV 311
Cdd:cd14895 157 RMFFEGHeldTSLRMIgtSVETYLLEKVRVVHQNDGERNFHVFYELLAGaaDDMKLELQLELLSAQEFQYISGGqcYQRN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 312 ESLDDAKEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENA------------------D 373
Cdd:cd14895 237 DGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqhlD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 374 KAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVL-----------DAKL 442
Cdd:cd14895 317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASpqrqfalnpnkAANK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 443 TSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEEYRKEGLDWLSIDYGLDvQACIDFIE-KPMGI 521
Cdd:cd14895 397 DTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEqRPSGI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 522 FSILEEECMLPKATDQMFKTKLF----DH-HFGKSAYFQTptspeknfEVHFELAHYAGVVPYNISGWIGKNKGLLNETV 596
Cdd:cd14895 476 FSLLDEECVVPKGSDAGFARKLYqrlqEHsNFSASRTDQA--------DVAFQIHHYAGAVRYQAEGFCEKNKDQPNAEL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 597 VALLQKSSNKVLANLFTK-DIIAGSASQFGE-KTHKKGTSFHL--ITSLHKENINKLMTDLKSTAPHFVRCINPNKNKIP 672
Cdd:cd14895 548 FSVLGKTSDAHLRELFEFfKASESAELSLGQpKLRRRSSVLSSvgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESAS 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 673 GVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYwilnpRIFSKSKFVSSRKATeEVLDFLEIDhpHYQCGVT 752
Cdd:cd14895 628 DQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQY-----RLLVAAKNASDATAS-ALIETLKVD--HAELGKT 699
|
....*
gi 261245016 753 KVFFK 757
Cdd:cd14895 700 RVFLR 704
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
96-713 |
6.25e-104 |
|
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: 350.93 E-value: 6.25e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQKEVMAAYKRKRRSEV----------PPHIFAVANRAFQDMLR 164
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAYDHNSQFgdrvtstdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 165 NGENQSIVFTGESGSGKTVNTKLIIQYFA------------TMAAISEPKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDN 232
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnnnltnSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 233 SSRFGKLIRIHF-GARGTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGN-----QELRNMLLVSTNPSDFHICSC 306
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvsKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 307 GVVAV--ESLDDAKEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKR--NLREEQLEADGTENA---------- 372
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 373 DKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVL-------------- 438
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 439 -DAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEEYRKEGLDWLSIDYGlDVQACIDFIE- 516
Cdd:cd14899 401 vDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEh 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 517 KPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPEKNFEVHFELAHYAGVVPYNISGWIGKNKGLLNETV 596
Cdd:cd14899 480 RPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 597 VALLQKSSNKVLANLFT--------KDIIAGSASQFGEKTHKKGTSFHLITSLHKENINKLMTDLKSTAPHFVRCINPNK 668
Cdd:cd14899 560 AQLLAGSSNPLIQALAAgsndedanGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKPND 639
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 261245016 669 NKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRY 713
Cdd:cd14899 640 SHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
96-755 |
9.61e-104 |
|
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: 348.38 E-value: 9.61e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQKEVMAAYKRKRRSE-VPPHIFAVANRAFQDM--LRNGENQSI 171
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQkLKPHIFTVGEQTYRNVksLIEPVNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 172 VFTGESGSGKTVNTKLIIQYFATMAAIS---EPKKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARG 248
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPtswESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 249 TLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQELRNMLLVSTNPSDFHicscGVVAVESLDDAKEFLATEKAID 328
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFS----WLPNPERNLEEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 329 VLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQ---LEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRS 405
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQpcqPMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQVFK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 406 QNLQQVTYAV--GALSQSIYERMFQWLVARMNQVLDAKLTS-HFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQ 482
Cdd:cd14880 317 KPCSRAECDTrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 483 QLFILEQEEYRKEGLDWLSIDYGlDVQACIDFIE-KPMGIFSILEEECMLPKATD-QMFKTKLFDHHFGKSAYFQTPTSP 560
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSaAQLQTRIESALAGNPCLGHNKLSR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 561 EKNFEVhfelAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDiiAGSASQFGEKTHKKGTSFHLItS 640
Cdd:cd14880 476 EPSFIV----VHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPAN--PEEKTQEEPSGQSRAPVLTVV-S 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 641 LHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRi 720
Cdd:cd14880 549 KFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRRL- 627
|
650 660 670
....*....|....*....|....*....|....*...
gi 261245016 721 fskskfvssRKATEEVLDFLEIDHPHYQ---CGVTKVF 755
Cdd:cd14880 628 ---------RPHTSSGPHSPYPAKGLSEpvhCGRTKVF 656
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
96-757 |
1.81e-102 |
|
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: 344.18 E-value: 1.81e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQKEVMAAY-----KRKRRSEVPPHIFAVANRAFQDMLRNGENQ 169
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYrqadtSRGFPSDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 170 SIVFTGESGSGKTVNTKLIIQYFATMAAISEPKkklgnLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGT 249
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSSTD-----VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 250 LSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSG--NQELRNMLLVSTNPSDFhICSCGVVAVESLDDAKEFLATEKAI 327
Cdd:cd14886 156 LKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGlsPEEKKSLGFKSLESYNF-LNASKCYDAPGIDDQKEFAPVRSQL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 328 DVLgfLPDEKF-GCYKLVGAIMHFGNLKFKR---NLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVT 403
Cdd:cd14886 235 EKL--FSKNEIdSFYKCISGILLAGNIEFSEegdMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETII 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 404 RSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQ 483
Cdd:cd14886 313 SPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 484 LFILEQEEYRKEGLDWLSIDYGlDVQACIDFIEKP-MGIFSILEEECMLPKATDQMFkTKLFDHHFGKSAYFqtptsPEK 562
Cdd:cd14886 393 VFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKF-TSSCKSKIKNNSFI-----PGK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 563 NFEVHFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLaNLFTKDIIAGSASQFGEkthkkgtsfhLITSLH 642
Cdd:cd14886 466 GSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIV-NKAFSDIPNEDGNMKGK----------FLGSTF 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 643 KENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIFS 722
Cdd:cd14886 535 QLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSS 614
|
650 660 670
....*....|....*....|....*....|....*.
gi 261245016 723 KSKFVSSRKAT-EEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14886 615 SQNAGEDLVEAvKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
96-757 |
6.64e-102 |
|
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: 342.74 E-value: 6.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKR-KRRSEVPPHIFAVANRAFQDMLRNGENQSIVFT 174
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 175 GESGSGKTVNTKLIIQYFATmaaisepkKKLGNL----EDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTL 250
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS--------AKSGNMdlriQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 251 SFADIQIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNML-LVSTNPSDFHICSCgvVAVESLDDAKEFLATEKAID 328
Cdd:cd14876 153 RYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGaDSEMKSKYhLLGLKEYKFLNPKC--LDVPGIDDVADFEEVLESLK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 329 VLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAF-----LMGIHASELLKGLIYPRIKVGNEYVT 403
Cdd:cd14876 231 SMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISNESLEVFkeacsLLFLDPEALKRELTVKVTKAGGQEIE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 404 RSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQ 483
Cdd:cd14876 311 GRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 484 LFILEQEEYRKEGLDWLSIDYGLDVQACIDFIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPEKN 563
Cdd:cd14876 391 VFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDSNIN 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 564 FEVhfelAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTkdiiagsasqfGEKTHK----KGTsfhLIT 639
Cdd:cd14876 471 FIV----VHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFE-----------GVVVEKgkiaKGS---LIG 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 640 SLHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPR 719
Cdd:cd14876 533 SQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLG 612
|
650 660 670
....*....|....*....|....*....|....*...
gi 261245016 720 IfSKSKFVSSRKATEEVLDFLEIDHPHYQCGVTKVFFK 757
Cdd:cd14876 613 I-ANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
96-757 |
2.28e-99 |
|
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: 335.63 E-value: 2.28e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMI-YTYSGIFCVAINPYKWLPVYQKEVMAAY-KRKRRSEVPPHIFAVANRAF-QDMLRNGENQSIV 172
Cdd:cd14875 1 ATLLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFnAIFVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 173 FTGESGSGKTVNTKLIIQYFATMAAISEPKKKLGNLEDQIVK----MNPLLEAFGNAKTQKNDNSSRFGKLIRIHF-GAR 247
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFdPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 248 GTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSG-----NQELRNMllvsTNPSDFHICSCGVVAV------ESLDD 316
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGlspeeKKELGGL----KTAQDYKCLNGGNTFVrrgvdgKTLDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 317 AKEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENAdKAAFLMGIHASELLKGLIyprIK 396
Cdd:cd14875 237 AHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL---VK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 397 VGNEYVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVLDAKL--TSHFFVGILDTTGFEILDYNSLEQLCINFTNE 474
Cdd:cd14875 313 SKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQLCINYANE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 475 KLQQFFNQQLFILEQEEYRKEGLDWLSIDYGlDVQACID-FIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAY 553
Cdd:cd14875 393 SLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNmFDQKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 554 FQTPTSPEKNfevHFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAgsasqfGEKTHKKGT 633
Cdd:cd14875 472 FVLPKSTIPN---QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGL------ARRKQTVAI 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 634 SFhlitslhKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRY 713
Cdd:cd14875 543 RF-------QRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYF 615
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 261245016 714 WILNPRifSKSKFVSSRKATEEVLDFLEI-------DHPHYQCGVTKVFFK 757
Cdd:cd14875 616 YLIMPR--STASLFKQEKYSEAAKDFLAYyqrlygwAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
96-717 |
2.94e-99 |
|
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: 337.34 E-value: 2.94e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQKEVMAAYKRKRR-SEVPPHIFAVANRAFQDMLRNGENQSIVF 173
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 174 TGESGSGKTVNTKLIIQYF-ATMAAISEPKKKLGN----LEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHF-GAR 247
Cdd:cd14906 81 SGESGSGKTEASKTILQYLiNTSSSNQQQNNNNNNnnnsIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 248 GTLSFADIQIYFLEKSRVVYQqPGERN--YHIFYQILSG-NQELRNMLLVSTNPSDFHICSCGVVAVESL---------- 314
Cdd:cd14906 161 GKIDGASIETYLLEKSRISHR-PDNINlsYHIFYYLVYGaSKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsn 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 315 -----DDAKEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRN---LREEQLEADGTENADKAAFLMGIHASEL 386
Cdd:cd14906 240 hnnktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDsdfSKYAYQKDKVTASLESVSKLLGYIESVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 387 LKGLIYPRIKVGNE--YVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSH-----------FFVGILDT 453
Cdd:cd14906 320 KQALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNdlaggsnkknnLFIGVLDI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 454 TGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEEYRKEGLDWLSIDYgLDVQACIDFIE-KPMGIFSILEEECMLP 532
Cdd:cd14906 400 FGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMP 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 533 KATDQMFKTKLFDHHFGKSAYFQTPTSpeknfEVHFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLF 612
Cdd:cd14906 479 KGSEQSLLEKYNKQYHNTNQYYQRTLA-----KGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 613 TKDIIAGSasqfgeKTHKKGTSFHLITSLHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEG 692
Cdd:cd14906 554 QQQITSTT------NTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNT 627
|
650 660
....*....|....*....|....*
gi 261245016 693 IRVCCEAFPSWMLYDDFKQRYWILN 717
Cdd:cd14906 628 IKVRKMGYSYRRDFNQFFSRYKCIV 652
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
96-757 |
1.58e-95 |
|
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: 325.42 E-value: 1.58e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATMAAISEPKKKLgnleDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADI 255
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSV----EKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 256 QIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVSTNPSDFhicSCGVVAVESLDD----AKEFLATEKAIDVL 330
Cdd:cd01386 157 QTLLLERSRVARRPEGESNFNVFYYLLAGaDAALRTELHLNQLAESN---SFGIVPLQKPEDkqkaAAAFSKLQAAMKTL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 331 GFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQ 410
Cdd:cd01386 234 GISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 411 VTY------------AVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEildyN----------SLEQLC 468
Cdd:cd01386 314 PARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQ----NpahsgsqrgaTFEDLC 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 469 INFTNEKLQQFFNQQLFILEQEEYRKEGLDwlsIDYGLDV---QACIDFIEK---------------PMGIFSILEEECM 530
Cdd:cd01386 390 HNYAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPElspGALVALIDQapqqalvrsdlrdedRRGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 531 LPKATDQMFKTKLFDhHFGKSAyFQTPTSPEKNFE--VHFELAHYAGV--VPYNISGWIGKNK-GLLNETVVALLQKSSN 605
Cdd:cd01386 467 YPGSSDDTFLERLFS-HYGDKE-GGKGHSLLRRSEgpLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQESQK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 606 KVLAnlftkdiiagsasqfgekTHKKGTSFHLITSLhkeniNKLMTDLKSTAPHFVRCINPNKNKIPGVMDPF------- 678
Cdd:cd01386 545 ETAA------------------VKRKSPCLQIKFQV-----DALIDTLRRTGLHFVHCLLPQHNAGKDERSTSspaagde 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 679 -----LVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNP----RIFSKSKFVSSRKATEEVLDFLEIDHPHYQC 749
Cdd:cd01386 602 lldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkKLGLNSEVADERKAVEELLEELDLEKSSYRI 681
|
....*...
gi 261245016 750 GVTKVFFK 757
Cdd:cd01386 682 GLSQVFFR 689
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
96-757 |
2.75e-94 |
|
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: 320.04 E-value: 2.75e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEvmaaYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFatMAAISEPKKKLGNLEDQivkmNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADI 255
Cdd:cd14937 77 ESGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDS----NFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 256 QIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVSTNpSDFHICSCGVVAVESLDDAKEFLATEKAIDVLGfLP 334
Cdd:cd14937 151 EIFLLENIRVVSQEEEERGYHIFYQIFNGmSQELKNKYKIRSE-NEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMN-MH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 335 DEKFGCYKLVGAIMHFGNLKF-------KRNLREeqLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQN 407
Cdd:cd14937 229 DMKDDLFLTLSGLLLLGNVEYqeiekggKTNCSE--LDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 408 LQQVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFIL 487
Cdd:cd14937 307 VEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 488 EQEEYRKEGLDWLSIDYGLDvQACIDFIEKPMGIFSILEEECMLPKATDQMFkTKLFDHHFGKSAYFqtpTSPEKNFEVH 567
Cdd:cd14937 387 ETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKY---ASTKKDINKN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 568 FELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAGSasqFGEKthkkgtsfHLITSLHKENIN 647
Cdd:cd14937 462 FVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSES---LGRK--------NLITFKYLKNLN 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 648 KLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCeAFPSWMLYDDFKQRYWILNpriFSKSKfV 727
Cdd:cd14937 531 NIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISF-FFQYKYTFDVFLSYFEYLD---YSTSK-D 605
|
650 660 670
....*....|....*....|....*....|..
gi 261245016 728 SSRKATEEVLDFLE--IDHPHYQCGVTKVFFK 757
Cdd:cd14937 606 SSLTDKEKVSMILQntVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
96-757 |
4.39e-88 |
|
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: 302.50 E-value: 4.39e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKR---KRRSEVPPHIFAVANRAFQDMLRNGENQSIV 172
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSssgQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 173 FTGESGSGKTVNTKLIIQYFATMAAISEPkkklgNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGAR-GTLS 251
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT-----TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERkKHLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 252 FADIQIYFLEKSRVVYQQPGERNYHIFYQILSG-----------NQELRNMLLVSTNPSDfhicscgVVAVESLDDAKEF 320
Cdd:cd14878 156 GARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGlsaeekyglhlNNLCAHRYLNQTMRED-------VSTAERSLNREKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 321 LATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNE 400
Cdd:cd14878 229 AVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 401 YVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVL----DAKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKL 476
Cdd:cd14878 309 MIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 477 QQFFNQQLFILEQEEYRKEGLDWLSIdYGLDVQ-ACID-FIEKPMGIFSILEEECMLPKATDQMFKTKL---FDHHFGKS 551
Cdd:cd14878 389 HHYINEVLFLQEQTECVQEGVTMETA-YSPGNQtGVLDfFFQKPSGFLSLLDEESQMIWSVEPNLPKKLqslLESSNTNA 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 552 AYFQTPTS----PEKNFEVHFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKDIIAgSASQFgek 627
Cdd:cd14878 468 VYSPMKDGngnvALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLVT-IASQL--- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 628 thkkgtsfhlitslhKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYD 707
Cdd:cd14878 544 ---------------RKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFS 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 261245016 708 DFKQRYWILNPRIFSKSKFVSSRKATEEVLdfLEIDHPHYQCGVTKVFFK 757
Cdd:cd14878 609 DFLSRYKPLADTLLGEKKKQSAEERCRLVL--QQCKLQGWQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
97-721 |
1.68e-85 |
|
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: 292.57 E-value: 1.68e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKwlPVYQKEVMAAYKrKRRSEVPPHIFAVANRAFQDMLRNGeNQSIVFTGE 176
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVHG-NQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 177 SGSGKTVNTKLIIQYFATMAAISEpkkklgNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFgaRGTLSFADIQ 256
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKITGAKFE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 257 IYFLEKSRVVYQQPGERNYHIFYQILSGNQelrnmlLVSTNpsDFHICSCGVVAVESLDDAKE-FLATEKAIDVLGFLPD 335
Cdd:cd14898 150 TYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKN--DFIDTSSTAGNKESIVQLSEkYKMTCSAMKSLGIANF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 336 EKFGcyKLVGAIMHFGNLKFkrnLREEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQVTYAV 415
Cdd:cd14898 222 KSIE--DCLLGILYLGSIQF---VNDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 416 GALSQSIYERMFQWLVARMNQVLDAklTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEEYRKE 495
Cdd:cd14898 297 NSMARLLYSNVFNYITASINNCLEG--SGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 496 GLDWLSIDYgLDVQACIDFIEKPMGIFSILEEECMLPKATDQ--MFKTKLFDHHFGKSayfqtptspekNFEVHFELAHY 573
Cdd:cd14898 375 GIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKnlLVKIKKYLNGFINT-----------KARDKIKVSHY 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 574 AGVVPYNISGWIGKNKgllnetvvallQKSSNKVLANLFTKDiiAGSASQFgekthkkgtsfhliTSLHKENINKLMTDL 653
Cdd:cd14898 443 AGDVEYDLRDFLDKNR-----------EKGQLLIFKNLLIND--EGSKEDL--------------VKYFKDSMNKLLNSI 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261245016 654 KSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRIF 721
Cdd:cd14898 496 NETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLF 563
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
93-756 |
1.62e-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: 283.29 E-value: 1.62e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 93 LNEASVLHTLRRRYDHWMIYTY---SGIfcVAINPYKWLPVYQKEVMAAYKRK-------RRSEVPPHIFAVANRAFQDM 162
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGSEyydttsgSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 163 LRNGENQSIVFTGESGSGKTVNTKLIIQYFATMAAISEPKKKLGNledQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRI 242
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGTKLSS---QISAAEFVLDSFGNAKTLTNPNASRFGRYTEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 243 HFGARGTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVStNPSDF-----HICSCGVVAVESlDD 316
Cdd:cd14879 156 QFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGaSPEERQHLGLD-DPSDYallasYGCHPLPLGPGS-DD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 317 AKEF--LATekAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFkrnlreeQLEADGTENA---------DKAAFLMGIHASE 385
Cdd:cd14879 234 AEGFqeLKT--ALKTLGFKRKHVAQICQLLAAILHLGNLEF-------TYDHEGGEESavvkntdvlDIVAAFLGVSPED 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 386 LLKGLIYpRIK-VGNEYVTRSQNlqqvtyAVGALSQ------SIYERMFQWLVARMNQVL-DAKLTSHFFVGILDTTGFE 457
Cdd:cd14879 305 LETSLTY-KTKlVRKELCTVFLD------PEGAAAQrdelarTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 458 ILD---YNSLEQLCINFTNEKLQQFFNQQLFILEQEEYRKEGLDWLSIDYgLDVQACIDFI-EKPMGIFSILEEEC-MLP 532
Cdd:cd14879 378 NRSstgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 533 KATDQMFKTKLFDHHFGKSAYFQTPTSPEKNFEVHFELAHYAGVVPYNISGWIGKNKGLLNETVVALLqkssnkvlanlf 612
Cdd:cd14879 457 KKTDEQMLEALRKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLL------------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 613 tkdiiaGSASQFgekthkkgtsfhlitslhKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEg 692
Cdd:cd14879 525 ------RGATQL------------------NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPE- 579
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261245016 693 irVCCEAFPSWML---YDDFKQRYWILNPRIFSkskfVSSRKATEEVLDFLEIDhphYQCGVTKVFF 756
Cdd:cd14879 580 --LAARLRVEYVVsleHAEFCERYKSTLRGSAA----ERIRQCARANGWWEGRD---YVLGNTKVFL 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
111-757 |
7.81e-81 |
|
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: 283.46 E-value: 7.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 111 IYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTGESGSGKTVNTKLIIQ 190
Cdd:cd14887 24 IYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQSILISGESGAGKTETSKHVLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 191 YfatMAAISEPKKKLGN--LEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADIQIYFLEKSRVVYQ 268
Cdd:cd14887 104 Y---LAAVSDRRHGADSqgLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 269 QPGERNYHIFYQILSgnqelrNMLLVSTNPSdfhicscgvVAVESLDDAKEFLATEKAIDVLGFLPDEKFGCYKLVGAIM 348
Cdd:cd14887 181 PSDEFSFHIFYALCN------AAVAAATQKS---------SAGEGDPESTDLRRITAAMKTVGIGGGEQADIFKLLAAIL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 349 HFGNLKF----------KRNL-------------REEQLEADGTENADKAAFLMGIHASELLKGLIYPRIKVGNEYV--- 402
Cdd:cd14887 246 HLGNVEFttdqepetskKRKLtsvsvgceetaadRSHSSEVKCLSSGLKVTEASRKHLKTVARLLGLPPGVEGEEMLrla 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 403 --------TRSQ-NLQQVTYAVGALSQSIYERMFQWLVARMNQVL-------------DAKLTSHF-FVGILDTTGFEIL 459
Cdd:cd14887 326 lvsrsvreTRSFfDLDGAAAARDAACKNLYSRAFDAVVARINAGLqrsakpsesdsdeDTPSTTGTqTIGILDLFGFEDL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 460 ---DYNSLEQLCINFTNEKLQQFFNQQLFILEQEEYRKEGLDWLSIDYGLDVQ------------ACIDFIEKP------ 518
Cdd:cd14887 406 rnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPFSfplastltsspsSTSPFSPTPsfrsss 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 519 --------MGIFSILEEECML-PKATDQMFKTKLFDHHFGKSAY------FQTPTSPEKNFEvhFELAHYAGVVPYNISG 583
Cdd:cd14887 486 afatspslPSSLSSLSSSLSSsPPVWEGRDNSDLFYEKLNKNIInsakykNITPALSRENLE--FTVSHFACDVTYDARD 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 584 WIGKNKGLLNETVVALLQKssnkvlANLFTKDIIAGSASQFGEKTHKKGTsfhlITSLHKENINKLMTDLKSTAPHFVRC 663
Cdd:cd14887 564 FCRANREATSDELERLFLA------CSTYTRLVGSKKNSGVRAISSRRST----LSAQFASQLQQVLKALQETSCHFIRC 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 664 INPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPRifSKSKFVSSRKATEEVLDFLEID 743
Cdd:cd14887 634 VKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPM--ALREALTPKMFCKIVLMFLEIN 711
|
730
....*....|....
gi 261245016 744 HPHYQCGVTKVFFK 757
Cdd:cd14887 712 SNSYTFGKTKIFFR 725
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
96-701 |
9.06e-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: 258.68 E-value: 9.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQKEVMAAYKRKRRSE-------VPPHIFAVANRAFQDMLRNGE 167
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 168 NQSIVFTGESGSGKTVNTKLIIQYFATMAAISEpkkkLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGAR 247
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQ----MTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 248 ---------GTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVSTNPSDFHICSCGV--------- 308
Cdd:cd14884 157 entqknmfnGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLNPDEshqkrsvkg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 309 ---VAVESLD--------DAKEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKrnlreeqleadgtenadKAAF 377
Cdd:cd14884 237 tlrLGSDSLDpseeekakDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-----------------AAAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 378 LMGIHASELLKGLIYPRIKVGNEYVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVL------------DAKLTSH 445
Cdd:cd14884 300 CLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdneDIYSINE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 446 FFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEEYRKEGLDWLSIdyglDVQACIDFIEKPMGIFSIL 525
Cdd:cd14884 380 AIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSD----VAPSYSDTLIFIAKIFRRL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 526 EEECMLP----KATDQMFKTKLFD----------HHFGK-SAYFQTPTSPEKNFEVH-FELAHYAGVVPYNISGWIGKNk 589
Cdd:cd14884 456 DDITKLKnqgqKKTDDHFFRYLLNnerqqqlegkVSYGFvLNHDADGTAKKQNIKKNiFFIRHYAGLVTYRINNWIDKN- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 590 gllnetvvallqksSNKVLANLftKDIIAGSASQFGEKTHKKGTSFHlITSLHKENIN---KLMTDLKSTAPHFVRCINP 666
Cdd:cd14884 535 --------------SDKIETSI--ETLISCSSNRFLREANNGGNKGN-FLSVSKKYIKeldNLFTQLQSTDMYYIRCFLP 597
|
650 660 670
....*....|....*....|....*....|....*
gi 261245016 667 NKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFP 701
Cdd:cd14884 598 NAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLS 632
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
99-713 |
2.63e-72 |
|
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: 258.75 E-value: 2.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 99 LHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRR----------SEVPPHIFAVANRAFQDMLRNGEN 168
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 169 QSIVFTGESGSGKTVNTKLIIQYFATMAAISEPKKK-------LGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIR 241
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDsegasgvLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 242 IHFGARGTLSFADIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQE---LRNMLLVSTNPSDFHICSCGVVAVESLD-DA 317
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdptLRDSLEMNKCVNEFVMLKQADPLATNFAlDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 318 KEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEADGTENA----------DKAAFLMGIHASELL 387
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTvsdaqscalkDPAQILLAAKLLEVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 388 KGLI--YPRI-----KVGNEYVT--RSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVL----DAKLTSHFF-----VG 449
Cdd:cd14893 324 PVVLdnYFRTrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVinsqgVH 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 450 ILDTTGFEILD--YNSLEQLCINFTNEKLQQFFNQQLF-----ILEQEEYRKEG--LDWLSIDYGLDVQACIDFIE-KPM 519
Cdd:cd14893 404 VLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLainfsFLEDESQQVENrlTVNSNVDITSEQEKCLQLFEdKPF 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 520 GIFSILEEECMLPKATDQMFKTKLFDHH---------FGKSAYFQTPTSPEKNFEVHFELAHYAGVVPYNISGWIGKNKG 590
Cdd:cd14893 484 GIFDLLTENCKVRLPNDEDFVNKLFSGNeavgglsrpNMGADTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLSSKNML 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 591 LLNETVVALLQKSSNKVLANLFTKDIIAGSASQFGEKTHKKGTS---FHLITSLHKENIN--------------KLMTDL 653
Cdd:cd14893 564 SISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQTEERGSTsskFRKSASSARESKNitdsaatdvynqadALLHAL 643
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 654 KSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRY 713
Cdd:cd14893 644 NHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
97-719 |
9.60e-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: 248.10 E-value: 9.60e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPvyqkevMAAYKRKRRSEVP-PHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG------NPLTLTSTRSSPLaPQLLKVVQEAVRQQSETGYPQAIILSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLII-QYFATMAAISEpKKKLGNLEDQIVKMNPLleafGNAKTQKNDNSSRFGKLIRIHFgARGTLSFAD 254
Cdd:cd14881 76 TSGSGKTYASMLLLrQLFDVAGGGPE-TDAFKHLAAAFTVLRSL----GSAKTATNSESSRIGHFIEVQV-TDGALYRTK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 255 IQIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNML-LVSTNPSDFHICSCGVVAVESLDDAKEFLATEKAIDVLG- 331
Cdd:cd14881 150 IHCYFLDQTRVIRPLPGEKNYHIFYQMLAGlSQEERVKLhLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKACLGILGi 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 332 -FLpdekfGCYKLVGAIMHFGNLKFKRNLREEQLEADGTEnADKAAFLMGIHASELLKGLiYPRIKVGNEYVTRSQNLQQ 410
Cdd:cd14881 230 pFL-----DVVRVLAAVLLLGNVQFIDGGGLEVDVKGETE-LKSVAALLGVSGAALFRGL-TTRTHNARGQLVKSVCDAN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 411 VTYAV-GALSQSIYERMFQWLVARMNQV--LDAKLTSHF---FVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQL 484
Cdd:cd14881 303 MSNMTrDALAKALYCRTVATIVRRANSLkrLGSTLGTHAtdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 485 FILEQEEYRKEGLDW-LSIDYgLDVQACIDFIEK-PMGIFSILEEECMlPKATDQMFKTKLFDHHFGKSAYFQTPTSPEK 562
Cdd:cd14881 383 FKSSIESCRDEGIQCeVEVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAKPQDDR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 563 NFEVHfelaHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSnkvlanlftkdiiagsaSQFGEKTHKKgtSFHLitslh 642
Cdd:cd14881 461 MFGIR----HFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN-----------------CNFGFATHTQ--DFHT----- 512
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261245016 643 keNINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILNPR 719
Cdd:cd14881 513 --RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPF 587
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
97-757 |
1.26e-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: 245.77 E-value: 1.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLP-VYQKEVMAAYKRKRrsEVPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFATmAAISEPKKklgnLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADI 255
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLT-TDLSRSKY----LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 256 QIYFLEKSRVVYQQPGERNYHIFYQILSG--NQELRNMLLVSTNpSDFHICSCGVVAVESLDDAKEFLATEKAIDVLGFl 333
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQFLKGitDEEKAAYQLGDIN-SYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDF- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 334 PDEKFG-CYKLVGAIMHFGNLKFkrnlreeqLEADG-TENADKAAFlmgihaSELLKGLIYPRIKVGNEYVT-RSQNLQQ 410
Cdd:cd14905 233 PSEKIDlIFKTLSFIIILGNVTF--------FQKNGkTEVKDRTLI------ESLSHNITFDSTKLENILISdRSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 411 VTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHfFVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQE 490
Cdd:cd14905 299 AVENRDSLARSLYSALFHWIIDFLNSKLKPTQYSH-TLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 491 EYRKEGLDWLSIDYGLDVQACIDFIEKpmgIFSILEEECMLPKATDQMFKTKLFD----HH-FGKsayfqtptSPEKnfe 565
Cdd:cd14905 378 EYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQNflsrHHlFGK--------KPNK--- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 566 vhFELAHYAGVVPYNISGWIGKNKG-LLNETVValLQKssNKVLANLFTKD-------IIAGSASQFGEKTHKKGTSFHL 637
Cdd:cd14905 444 --FGIEHYFGQFYYDVRGFIIKNRDeILQRTNV--LHK--NSITKYLFSRDgvfninaTVAELNQMFDAKNTAKKSPLSI 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 638 ITSL------HKENINK-----------------------LMTDLKSTAP---------HFVRCINPNKNKIPGVMDPFL 679
Cdd:cd14905 518 VKVLlscgsnNPNNVNNpnnnsgggggggnsgggsgsggsTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKS 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 680 VLQQLRCNGVLEGIRVccEAFPSWMLYDD--FKQR--YWILNPRIFsKSKFvssRKATEEVLDFLEIDHPHYQCGVTKVF 755
Cdd:cd14905 598 VNEQIKSLCLLETTRI--QRFGYTIHYNNkiFFDRfsFFFQNQRNF-QNLF---EKLKENDINIDSILPPPIQVGNTKIF 671
|
..
gi 261245016 756 FK 757
Cdd:cd14905 672 LR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
96-718 |
3.36e-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: 3.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 96 ASVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYkrkrrsevppHIFAVANRAFQDMLRNGEN-QSIVFT 174
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 175 GESGSGKTVNTKLIIQYFatmaaISEPKKKLGNLedQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFAD 254
Cdd:cd14874 71 GESGSGKSYNAFQVFKYL-----TSQPKSKVTTK--HSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 255 IQIYFLEKSRVVYQQPGERNYHIFYQILSG-NQELRNMLLVSTNPSDFHICSCGVVAVESlDDAKEFLATEKAIDVLGFL 333
Cdd:cd14874 144 KYTVPLEVPRVISQKPGERNFNVFYEVYHGlNDEMKAKFGIKGLQKFFYINQGNSTENIQ-SDVNHFKHLEDALHVLGFS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 334 PDEKFGCYKLVGAIMHFGNLKFKR----NLREEQLEADGTENADKAAFLMGIHASELLKGLIyPRIKVGNeyvtrSQNLQ 409
Cdd:cd14874 223 DDHCISIYKIISTILHIGNIYFRTkrnpNVEQDVVEIGNMSEVKWVAFLLEVDFDQLVNFLL-PKSEDGT-----TIDLN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 410 QVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFfVGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQ 489
Cdd:cd14874 297 AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV-ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 490 EEYRKEGldwLSIDYglDVQACID-------FIEKPMGIFSILEEECMLPKATDQMFKTKLFDHHFGKSAYFQTPTSPEK 562
Cdd:cd14874 376 VDYAKDG---ISVDY--KVPNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKERL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 563 NFEVHfelaHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLF------TKDIIAGSASQFGEKTHKKGtsfh 636
Cdd:cd14874 451 EFGVR----HCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFesyssnTSDMIVSQAQFILRGAQEIA---- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 637 litslhkENINKLMTdlkstapHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWIL 716
Cdd:cd14874 523 -------DKINGSHA-------HFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
..
gi 261245016 717 NP 718
Cdd:cd14874 589 LP 590
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
97-716 |
5.17e-59 |
|
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: 216.53 E-value: 5.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTGE 176
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 177 SGSGKTVNTKLIIQYFATMAaisepkKKLGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRIHFGARGTLSFADIQ 256
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG------DGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 257 IYFLEKSRVVYQQPGERNYHIFYQI---LSGNQELRNMLL------------VSTNPSDFHICSCGVVavESLDDAKEFl 321
Cdd:cd14882 156 MYQLEKLRVSTTDGNQSNFHIFYYFydfIEAQNRLKEYNLkagrnyrylripPEVPPSKLKYRRDDPE--GNVERYKEF- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 322 atEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQLEadGTENADKAAFLMGIHASELLKGLIYPRIKVGNEY 401
Cdd:cd14882 233 --EEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGYAELE--NTEIASRVAELLRLDEKKFMWALTNYCLIKGGSA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 402 VTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVLD---AKLTSHFFVGILDTTGFEILDYNSLEQLCINFTNEKLQQ 478
Cdd:cd14882 309 ERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfprAVFGDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 479 FFNQQLFILEQEEYRKEGLDWLSIDYGLDVQACIDFIEKPMGIFSILEEecmlpkATDQMFKTKL-FDH-HFGKSAYFQT 556
Cdd:cd14882 389 HYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD------ASRSCQDQNYiMDRiKEKHSQFVKK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 557 PTSPEknfevhFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTKdiiagsaSQfgekTHKKGTSFH 636
Cdd:cd14882 463 HSAHE------FSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQ----VRNMRTLAA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 637 LITSLHKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWIL 716
Cdd:cd14882 526 TFRATSLELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL 605
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
118-242 |
2.95e-47 |
|
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: 167.14 E-value: 2.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 118 FCVAINPYKWLPVY-QKEVMAAYKRKRRSEVPPHIFAVANRAFQDMLRNGENQSIVFTGESGSGKTVNTKLIIQYFATMA 196
Cdd:cd01363 1 VLVRVNPFKELPIYrDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 261245016 197 AISEPKKK----------LGNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFGKLIRI 242
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 ... |
97-717 |
5.44e-38 |
|
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: 154.22 E-value: 5.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 97 SVLHTLRRRYDHWMIYTYSGIFCVAINPYKWLPVYQKEVMAAYKRKRRSE-VPPHIFAVANRAFQDMLRNGENQSIVFTG 175
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 176 ESGSGKTVNTKLIIQYFA----------TMAAISEPKKKL--------GNLEDQIVKMNPLLEAFGNAKTQKNDNSSRFG 237
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAyqvkgsrrlpTNLNDQEEDNIHneentdyqFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 238 KLIRIHFGARGTLSFaDIQIYFLEKSRVVYQQPGERNYHIFYQILSGNQELRNMLLVSTNPSDFHICSCGVVAVESLDDA 317
Cdd:cd14938 162 KFCTIHIENEEIKSF-HIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 318 KEFLATEKAIDVLGFLPDEKFGCYKLVGAIMHFGNLKFKRNLREEQL-----------------------EADGTENADK 374
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRKKSLlmgknqcgqninyetilselensEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 375 ----AAFLMGIHASELLKGLIYPRIkVGNEYVTRSQNLQQVTYAVGALSQSIYERMFQWLVARMNQVLDAKLTSHFF--- 447
Cdd:cd14938 321 nlllACKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININtny 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 448 VGILDTTGFEILDYNSLEQLCINFTNEKLQQFFNQQLFILEQEEYRKEGLDWLSIDYGLDVQACIDFIEKPM--GIFSIL 525
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFSLL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 526 EEECMlPKATDQMFKTKLFDHHFGKSAYFQTPTSPEKNFEVhFELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSN 605
Cdd:cd14938 480 ENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 606 KVLANLF-------TKDIIAGS---ASQFGEKTHKKG--TSFHLITSLHKENINKLMTDLKSTAPHFVRCINPNKNK-IP 672
Cdd:cd14938 558 EYMRQFCmfynydnSGNIVEEKrrySIQSALKLFKRRydTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKrEL 637
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 261245016 673 GVMDPFLVLQQLRCNGVLEGIRVCCEAFPSWMLYDDFKQRYWILN 717
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKN 682
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1135-1922 |
2.89e-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: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1135 EDLNERLEEAGGTSlaqmeitkqqearfqKLHHDMEETTRHFEATSASLKkRHAENLAELEGQVEHLQ-QVRLV-----L 1208
Cdd:TIGR02168 155 EERRAIFEEAAGIS---------------KYKERRKETERKLERTRENLD-RLEDILNELERQLKSLErQAEKAerykeL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1209 EQDKSDLQLQVddLLNRVDQMARAKANAEKLCGLYERRLNEANTKLDEvtqlahdLTTQKTKLQSESGEFFKRLEEKEAL 1288
Cdd:TIGR02168 219 KAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQE-------LEEKLEELRLEVSELEEEIEELQKE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1289 ISQLSREKSNFTRQVEELRAQLEEESRSQSALSHALQSAKHDYDLLRE---QYEEEQEVKAELHRALSKGNKETVQWRAK 1365
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEelaELEEKLEELKEELESLEAELEELEAELEE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1366 YEHDAMQRTEDLEEAKKKLA-IRLQEAAEAMEVSNAKnASLERARHRLQlelgdalsdlgKARSVAAALGQKQQHSDKAL 1444
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAqLELQIASLNNEIERLE-ARLERLEDRRE-----------RLQQEIEELLKKLEEAELKE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1445 TSwkQKLDETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQVR------EGIKNLAEVE 1518
Cdd:TIGR02168 438 LQ--AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlegfsEGVKALLKNQ 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1519 KAKKLI-----------EQEKTEVQVRLEETEGAL--ERNESKILRFQLeLSEAKAELERKLSEKEEEAERLREKHQQAM 1585
Cdd:TIGR02168 516 SGLSGIlgvlselisvdEGYEAAIEAALGGRLQAVvvENLNAAKKAIAF-LKQNELGRVTFLPLDSIKGTEIQGNDREIL 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1586 GSLQSNLDLEASSRIEATRLRKKMEGDLKEMEI--QLCAANRQVSQMTRAL------------------GQLQGQMKDLH 1645
Cdd:TIGR02168 595 KNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYrivtldgdlvrpggvitgGSAKTNSSILE 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1646 QQlddsiyQN-KDLKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATERINLFHTQNTSLLSQKKKLEAD 1724
Cdd:TIGR02168 675 RR------REiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1725 VAQVQKEAGEMLQacqkaeekakktaaEAANMSEELKKEQDTNAHLERMRKNMEQTIKDLQKRLDEAEqTAVLGSKKQIQ 1804
Cdd:TIGR02168 749 IAQLSKELTELEA--------------EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-EALDELRAELT 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1805 KLESRVRDLEGELESEVRRSAEAQREARRLERGIKELTYQAEEDKKNLSRMQALSDKLQLKVQSYKQQVEAAEAQANQYL 1884
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
810 820 830
....*....|....*....|....*....|....*...
gi 261245016 1885 SKYKKQQHELNeakeraeAAESQVNKLRAKAKELEKKV 1922
Cdd:TIGR02168 894 SELEELSEELR-------ELESKRSELRRELEELREKL 924
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
838-1610 |
2.41e-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: 118.62 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 838 EEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKSKVELEVKIKELSRQV 917
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 918 EEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQQT 997
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 998 QEQLHIEEEKLSNMSKANLKLAQqidvlegdlERERKARMKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLRKKEFE 1077
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLK---------KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1078 MGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVEReKGDLVQDLEDLNERLEEAGGTSLAQMEITKQ 1157
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV-LSELISVDEGYEAAIEAALGGRLQAVVVENL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1158 QEAR----FQKLHhdmEETTRHFEATSASLKKRHAENLAELEGQVEHLQQVRLVLEQDKSDLQLQVDDLLNRVdQMARAK 1233
Cdd:TIGR02168 556 NAAKkaiaFLKQN---ELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV-LVVDDL 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1234 ANAEKLCGLYERRLNeantkldevtqlahdLTTQKTKLQSESGEFFKRLEEKEALISQLSREKSNFTRQVEELRAQLEEE 1313
Cdd:TIGR02168 632 DNALELAKKLRPGYR---------------IVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAEL 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1314 SRSQSALSHALQSAKHDYDLLREQYEEEQEVKAELHRALSKGNKETVQWRAKYEHDAMQRTEdLEEAKKKLAIRLQEAAE 1393
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE-LEAEIEELEERLEEAEE 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1394 AMEVSNAKNASLERARHRLQLELGDALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEVl 1473
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI- 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1474 tfrqacEESTEAQETLKRQNQDLQEQICSLTNQVregiknlAEVEKAKKLIEQEKTEVQVRLEETEGALERNESKILRFQ 1553
Cdd:TIGR02168 855 ------ESLAAEIEELEELIEELESELEALLNER-------ASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261245016 1554 LELSEAKAELERKLSEKEEEAERLREKHQ---QAMGSLQSNLDLE-ASSRIEATRLRKKME 1610
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERLSEEYSltlEEAEALENKIEDDeEEARRRLKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1021-1734 |
7.56e-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: 7.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1021 QIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVK 1100
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1101 ELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNERLEEAggtslaqMEITKQQEARFQKLHHDMEETTRHFEATS 1180
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL-------KEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1181 ASLKKRhAENLAELEGQVEHLQQVRLVLEQDKSDLQLQVDDLLNRVDQMARAKANAEklcglyerrLNEANTKLDEVTQL 1260
Cdd:TIGR02168 379 EQLETL-RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1261 AHDLTTQKTKLQSESGEFFKRLEEKEALISQLSRE---KSNFTRQVEELRAQLEEESRSQSALSHALQSAKHDYDLLREQ 1337
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERElaqLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1338 YEEEQEVKAELHRALSKGNKETVqwrAKYEHDAMQRTEDLEEAKK--------------KLAIRLQEAAEAMEVSNAKNA 1403
Cdd:TIGR02168 529 ISVDEGYEAAIEAALGGRLQAVV---VENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILKNIEGFLGVAK 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1404 SLERARHRLQLELGDALSDLGKARSVAAALGQKQQHS--------DKALTSWK----QKLDETQELLQASQKETRALSSE 1471
Cdd:TIGR02168 606 DLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRpgyrivtlDGDLVRPGgvitGGSAKTNSSILERRREIEELEEK 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1472 VLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALERNESKILR 1551
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1552 FQLELSEA---KAELERKLSEKEEEAERLREKHQQ---AMGSLQSNLDLEASSRIEATRLRKKMEGDLKEMEIQLCAANR 1625
Cdd:TIGR02168 766 LEERLEEAeeeLAEAEAEIEELEAQIEQLKEELKAlreALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1626 QVSQMTRALGQLQGQMKDLHQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATERIN 1705
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
730 740
....*....|....*....|....*....
gi 261245016 1706 LFHTQntsllsqKKKLEADVAQVQKEAGE 1734
Cdd:TIGR02168 926 QLELR-------LEGLEVRIDNLQERLSE 947
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1065-1841 |
3.91e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.38 E-value: 3.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1065 QKLAEQLRKKEF-----EMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNE 1139
Cdd:TIGR02168 216 KELKAELRELELallvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1140 RLEEAGgtslAQMEITKQQEARFQKlhhdmeettrhfeatsaslkkrhaeNLAELEGQVEHLQQVRLVLEQDKSDLQLQV 1219
Cdd:TIGR02168 296 EISRLE----QQKQILRERLANLER-------------------------QLEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1220 DDLLNRVDQMARAKANAEKLCGLYERRLNEANTKLDEVTQLAHDLTTQKTKLQsesgeffKRLEEKEALISQLSREKSNF 1299
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN-------NEIERLEARLERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1300 TRQVEEL-----RAQLEEESRSQSALSHALQSAKHDYDLLREQYEEEQEVKAELHRALSKGNKETVQWRAKYE--HDAMQ 1372
Cdd:TIGR02168 420 QQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDslERLQE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1373 RTEDLEEAKK-------KLAIRLQEAAEAMEVSNAKNASLERArhrLQLELGDALSDlGKARSVAAALGQKQQHSDKA-- 1443
Cdd:TIGR02168 500 NLEGFSEGVKallknqsGLSGILGVLSELISVDEGYEAAIEAA---LGGRLQAVVVE-NLNAAKKAIAFLKQNELGRVtf 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1444 --LTSWK-QKLDETQELLQASQKETRALSSEVLTFRQA--------------CEESTEAQETLKRQNQdlQEQICSLTNQ 1506
Cdd:TIGR02168 576 lpLDSIKgTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkalsyllggvlvVDDLDNALELAKKLRP--GYRIVTLDGD 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1507 V--REGIKNLAEVEKAKKLIEQEKtevqvRLEETEGALERNESKILRFQLELSEAKAELERKLSEKEEEAERLREKHQQA 1584
Cdd:TIGR02168 654 LvrPGGVITGGSAKTNSSILERRR-----EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1585 MGSLQSNLDLEASSRIEATRLRkKMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNKDLKEQVAL 1664
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIA-QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1665 AEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATERINLFHTQNTSLLSQKKKLEADVAQVQKEAGEMLQACQKAEE 1744
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1745 KAKKTAAEAANMSEELKKEQDTNAHLERMRKNMEQTIKDLQKRLDEAEQTAvlgsKKQIQKLESRVRDLEGELESEVRR- 1823
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI----DNLQERLSEEYSLTLEEAEALENKi 963
|
810 820
....*....|....*....|.
gi 261245016 1824 ---SAEAQREARRLERGIKEL 1841
Cdd:TIGR02168 964 eddEEEARRRLKRLENKIKEL 984
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
98-707 |
2.52e-24 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 111.37 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 98 VLHTLRRRYDHWMIYTYSGIFCVAI-NPYKWL------PVYQKEVMAAYKRKRRSE--VPPHIFAVANRAFQDM------ 162
Cdd:cd14894 3 LVDALTSRFDDDRIYTYINHHTMAVmNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKQSLVRLffdneh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 163 -------------LRNGENQSIVFTGESGSGKTVNTKLIIQYFA------------------------------------ 193
Cdd:cd14894 83 tmplpstissnrsMTEGRGQSLFLCGESGSGKTELAKDLLKYLVlvaqpalskgseetckvsgstrqpkiklftsstkst 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 194 -----------------------------------TMAAISEPKK---------------KLGNLEDQ------------ 211
Cdd:cd14894 163 iqmrteeartialleakgvekyeivlldlhperwdEMTSVSRSKRlpqvhvdglffgfyeKLEHLEDEeqlrmyfknpha 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 212 ------IVKMNPLLEAFGNAKTQKNDNSSRFGKL--IRIHFGARG---TLSFADIQIYFLEKSRVVYQQ------PGERN 274
Cdd:cd14894 243 akklsiVLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 275 YHIFYQILSGNQELRNMLLVStnpSDFHI----CSC------------GVVAVESL--DDAKEFLATEKAIDVLGFLPDE 336
Cdd:cd14894 323 FHILYAMVAGVNAFPFMRLLA---KELHLdgidCSAltylgrsdhklaGFVSKEDTwkKDVERWQQVIDGLDELNVSPDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 337 KFGCYKLVGAIMHFGNLKFkrNLREEQ----LEADGTENA-DKAAFLMGIHASELLKGLIYPR---IKVGNEYVTRSQNL 408
Cdd:cd14894 400 QKTIFKVLSAVLWLGNIEL--DYREVSgklvMSSTGALNApQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEK 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 409 QQVTYAVGALSQSIYERMFQWLVARMNQV--------------LDAKLTSHFFVGIL---DTTGFEILDYNSLEQLCINF 471
Cdd:cd14894 478 GQVNHVRDTLARLLYQLAFNYVVFVMNEAtkmsalstdgnkhqMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCINY 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 472 TNEKLqqFFNQQLFILEQEEYRKEGLdwlsidyGLDVQACIDFI-EKPMGIFSILEEECMLPK-----ATDQMFKTKLFD 545
Cdd:cd14894 558 LSEKL--YAREEQVIAVAYSSRPHLT-------ARDSEKDVLFIyEHPLGVFASLEELTILHQsenmnAQQEEKRNKLFV 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 546 HHFGKSAYFQTPTSPE--KNFEVH---------FELAHYAGVVPYNISGWIGKNKGLLNETVVALLQKSSNKVLANLFTK 614
Cdd:cd14894 629 RNIYDRNSSRLPEPPRvlSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNE 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 615 DIIAG-----SASQFGEKTHKKGTSFHLITSLhKENINKLMTDLKSTAPHFVRCINPNKNKIPGVMDPFLVLQQLRCNGV 689
Cdd:cd14894 709 SSQLGwspntNRSMLGSAESRLSGTKSFVGQF-RSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRL 787
|
810
....*....|....*...
gi 261245016 690 LEGIRVCCEAFPSWMLYD 707
Cdd:cd14894 788 IRQMEICRNSSSSYSAID 805
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
963-1738 |
2.75e-24 |
|
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: 111.69 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 963 EHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQQTQEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERERKARMKCERE 1042
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1043 KRK-------LQDELKMNQEGAENLESSRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELES 1115
Cdd:TIGR02168 304 KQIlrerlanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1116 ERTIRAKVEREKGD-------LVQDLEDLNERLEEAggTSLAQMEITKQQEARFQKLHHDMEETTRHFEATSASLKkRHA 1188
Cdd:TIGR02168 384 LRSKVAQLELQIASlnneierLEARLERLEDRRERL--QQEIEELLKKLEEAELKELQAELEELEEELEELQEELE-RLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1189 ENLAELEGQVEHLQQVRLVLEQDKSDLQLQVD---DLLNRVDQMARA----KANAEKLCGL-------------YERRLN 1248
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDsleRLQENLEGFSEGvkalLKNQSGLSGIlgvlselisvdegYEAAIE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1249 EA------------------------NTKLDEVTQLAHDLTTQkTKLQSESGEFFKRLEEKEALISQLSREKSNFTRQVE 1304
Cdd:TIGR02168 541 AAlggrlqavvvenlnaakkaiaflkQNELGRVTFLPLDSIKG-TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1305 ELRAQLEEESRSQSALshalqsakhdyDLLREQYEEEQEVKAELHR-----ALSKGNKETVQWRAKYEhdamQRTEDLEE 1379
Cdd:TIGR02168 620 YLLGGVLVVDDLDNAL-----------ELAKKLRPGYRIVTLDGDLvrpggVITGGSAKTNSSILERR----REIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1380 AKKKLAIRLQEAAEAMEVSNAKNASLERARHRLQLELGDALSDLGKARSVAAALGQKQQhsdKALTSWKQKLDETQELLQ 1459
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE---QLEERIAQLSKELTELEA 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1460 ASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQ---EQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRLE 1536
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrEALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1537 ETEGALERNESKILRFQLELSEAKAELErKLSEKEEEAERLREKHQQAMGSLQSNLDleassriEATRLRKKMEGDLKEM 1616
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERASLEEALALLRSELE-------ELSEELRELESKRSEL 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1617 EIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSiyQNKDLKEQVALAEQRTVLLQSELEELRTLQEQTER-GR--KLA 1693
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSEE--YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElGPvnLAA 991
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 261245016 1694 EKELLEATERINLFHTQNTSLLSQKKKLEADVAQVQKEAGEMLQA 1738
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1244-1924 |
5.58e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.86 E-value: 5.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1244 ERRLNEANTKLDEVTQLAHDLTTQKTKLQSEsgeffkrleekealisqlsREKsnfTRQVEELRAQLEEesRSQSALSHA 1323
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPLERQ-------------------AEK---AERYRELKEELKE--LEAELLLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1324 LQSAKHDYDLLREQYEEEQEVKAELHRALSKGNKETvqwrakyehdamqrtEDLEEAKKKLAIRLQEAAEAMEVSNAKNA 1403
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAEL---------------EELRLELEELELELEEAQAEEYELLAELA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1404 SLERARHRLQLELGDALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEVLTFRQACEEST 1483
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1484 EAQETLKRQNQDLQEQIcsltnqvREGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALERNESKILRFQLELSEAKAEL 1563
Cdd:COG1196 379 EELEELAEELLEALRAA-------AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1564 ERKLSEKEEEAERLREKHQQAMGSLQSNLDLEASSRIEATRLRkkmegDLKEMEiqlcAANRQVSQMTRALGQLQGQmKD 1643
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL-----LLLEAE----ADYEGFLEGVKAALLLAGL-RG 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1644 LHQQLDDSIyqnkdLKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATERINLfhtqntSLLSQKKKLEA 1723
Cdd:COG1196 522 LAGAVAVLI-----GVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL------DKIRARAALAA 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1724 DVAQVQKEAGEMLQACQKAEEKAKKTAAEaanmsEELKKEQDTNAHLERMRKNMEQTIKDLQKRLDEAEQTAVLGSKKQI 1803
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLG-----DTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1804 QKLEsrvrdlegELESEVRRSAEAQREARRLERGIKELTYQAEEDKKNLSRMQALSDKLQLKVQSYKQQVEAAEAQANQY 1883
Cdd:COG1196 666 SRRE--------LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 261245016 1884 LSKYKKQQHELNEAKERAEAAESQVNKLRAKAKELEKKVRE 1924
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
838-1396 |
2.95e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.47 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 838 EEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKSKVELEVKIKELSRQV 917
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 918 EeeeeinsELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQQT 997
Cdd:COG1196 326 A-------ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 998 QEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLRKKEFE 1077
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1078 MGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESERtiRAKVEREKGDLVQDLEDLNERLEEAGGTSLAQMEITKQ 1157
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG--LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDD 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1158 QEARFQKLHHDMEETTRHFEATSASLKKRHAENLAELEGQV-EHLQQVRLVLEQDKSDLQLQVDDLLNRVDQMARAKANA 1236
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIgAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1237 eklcglyeRRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLSREKSNFTRQVEELRAQLEEESRS 1316
Cdd:COG1196 637 --------RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1317 QSALSHALQSAKHDYDLLREQYEEEQEVKAELHRALSKGNKETVQwrakyehDAMQRTEDLEEAKKKLAiRLQEAAEAME 1396
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL-------EELPEPPDLEELERELE-RLEREIEALG 780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
838-1174 |
2.09e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 95.89 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 838 EEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKSKVELEVKIKELSRQV 917
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 918 EEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQQT 997
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 998 QEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLRKKEFE 1077
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1078 MGQMNSKVENEKNQVSQLQKMVKELqtHILNLKEELESERTIRAKVEREKgdlvQDLEDLNERLEEAGGTSLAQMEITKQ 1157
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEE--YSLTLEEAEALENKIEDDEEEAR----RRLKRLENKIKELGPVNLAAIEEYEE 997
|
330
....*....|....*..
gi 261245016 1158 QEARFQKLHHDMEETTR 1174
Cdd:TIGR02168 998 LKERYDFLTAQKEDLTE 1014
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
838-1851 |
3.57e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.13 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 838 EEIAGLKEECAQLQKALESSESQREELKTKQvSLVQEKNDLRLQLQAEQETLanseEQCESLIKSKVELEVKikelsrqv 917
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLD-LIIDEKRQQLERLRREREKA----ERYQALLKEKREYEGY-------- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 918 eeeeeinsELTARGRKLEDECSELKKEIYDLEAILAKsekgkcaaehkvrnLTEEVHSLNEEVSKLSRVVKDaqetqqqt 997
Cdd:TIGR02169 227 --------ELLKEKEALERQKEAIERQLASLEEELEK--------------LTEEISELEKRLEEIEQLLEE-------- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 998 qeqlhieeeklsnmskanlkLAQQIDVLEGDLERERKARM-KCEREKRKLQDELKMNQEGAENLESSRQKLAEQLRKKEF 1076
Cdd:TIGR02169 277 --------------------LNKKIKDLGEEEQLRVKEKIgELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1077 EMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNERLEEAGGTSLAQMEITK 1156
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1157 QQEARFQKLHHDMEEtTRHFEATSASLKKRHAENLAELEGQVEHLQQVRLVLEQDKSDLQLQVDDLlnrvdqmarakana 1236
Cdd:TIGR02169 417 RLSEELADLNAAIAG-IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV-------------- 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1237 eklcglyERRLNEANTKLDEvtqlahdLTTQKTKLQSESGEFFKRLEEKEA-------LISQLSREKSNFTRQVEelraq 1309
Cdd:TIGR02169 482 -------EKELSKLQRELAE-------AEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGSVGERYATAIE----- 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1310 leeesrsqSALSHALQSAKHDYDLLREQ-YEEEQEVKA------------ELHRALSKGNKET--------VQWRAKYEH 1368
Cdd:TIGR02169 543 --------VAAGNRLNNVVVEDDAVAKEaIELLKRRKAgratflplnkmrDERRDLSILSEDGvigfavdlVEFDPKYEP 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1369 D---AMQRT---EDLEEAKKKLA-IRLQE-AAEAMEVSNAKNASLERARHRlqleLGDALSDLGKARSVAAalgqkqqhs 1440
Cdd:TIGR02169 615 AfkyVFGDTlvvEDIEAARRLMGkYRMVTlEGELFEKSGAMTGGSRAPRGG----ILFSRSEPAELQRLRE--------- 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1441 dkaltswkqKLDETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQIcsltNQVREGIKNLAEVEKA 1520
Cdd:TIGR02169 682 ---------RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE----EKLKERLEELEEDLSS 748
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1521 kklIEQEKTEVQVRLEETEGALERNESKILRFQLELSEAKAELER-KLSEKEEEAERLREKHQQAMGSLQSnldleassr 1599
Cdd:TIGR02169 749 ---LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsRIPEIQAELSKLEEEVSRIEARLRE--------- 816
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1600 ieatrlrkkMEGDLKEMEIQLcaanrqvsqmtralgqlqgqmkdlhQQLDDSIyqnKDLKEQVALAEQRTVLLQSELEEL 1679
Cdd:TIGR02169 817 ---------IEQKLNRLTLEK-------------------------EYLEKEI---QELQEQRIDLKEQIKSIEKEIENL 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1680 RTLQEQTERGRKLAEKELLEaterinlfhtqntsLLSQKKKLEADVAQVQKEAGEMLQACQKAEEKAKKTAAEAANMSEE 1759
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRD--------------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1760 LKKEQDTNAHLERMRKNMEQtikdlqkrldEAEQTAVLGS-KKQIQKLESRVRDLEG-------ELESEVRRSAEAQREA 1831
Cdd:TIGR02169 926 LEALEEELSEIEDPKGEDEE----------IPEEELSLEDvQAELQRVEEEIRALEPvnmlaiqEYEEVLKRLDELKEKR 995
|
1050 1060
....*....|....*....|...
gi 261245016 1832 RRLE---RGIKELTYQAEEDKKN 1851
Cdd:TIGR02169 996 AKLEeerKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1121-1924 |
1.68e-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: 89.36 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1121 AKVEREKGDLVQDLEDLNERLEEAG------GTSLAQMEITKQQEARFQKLHHDMEEttrhFEATSASLKKRhaenlaEL 1194
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDliidekRQQLERLRREREKAERYQALLKEKRE----YEGYELLKEKE------AL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1195 EGQVEHLQQVRLVLEQDKSDLQLQVDDLlnrvdqmarakanaEKLCGLYERRLNEANTKLDEVT---QLA-----HDLTT 1266
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISEL--------------EKRLEEIEQLLEELNKKIKDLGeeeQLRvkekiGELEA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1267 QKTKLQSESGEFFKRLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSALSHALQSAKHDYDLLREQYEEEQEVKA 1346
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1347 ELHRALSKGNKETVQwrAKYEHDAMQRTED-LEEAKKKLAIRLQEAAEAMEVSNAKNASLERARHRLQLELGDALSDLGK 1425
Cdd:TIGR02169 382 ETRDELKDYREKLEK--LKREINELKRELDrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1426 ARSVAAALgqKQQHSDKaltswKQKLDETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTn 1505
Cdd:TIGR02169 460 LAADLSKY--EQELYDL-----KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLG- 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1506 QVREGIKNLAEV--------------EKAKKLIEQEKTEVQVR---LEETEGALERNESKILR------FQLELSEAKAE 1562
Cdd:TIGR02169 532 SVGERYATAIEVaagnrlnnvvveddAVAKEAIELLKRRKAGRatfLPLNKMRDERRDLSILSedgvigFAVDLVEFDPK 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1563 LERKLS---------EKEEEAERLR-------------EKHQQAMGSLQSNLDLEASSRIEATRLRKkMEGDLKEMEIQL 1620
Cdd:TIGR02169 612 YEPAFKyvfgdtlvvEDIEAARRLMgkyrmvtlegelfEKSGAMTGGSRAPRGGILFSRSEPAELQR-LRERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1621 CAANRQVSQMTRALGQLQGQMKDLHQQLddsiyqnKDLKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEA 1700
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKI-------GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1701 TERINLFHTQNTSLLSQKKKLEADVAQ------------VQKEAGEMLQACQKAEEKAKKTAAEAANMSEELKKEQDTNA 1768
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDLEARLSHsripeiqaelskLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1769 HLERMRKNMEQTIKDLQKRLDEAEQtavlgskkQIQKLESRVRDLEGELESEVRRSAEAQREARRLERGIKELTYQAEED 1848
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKKEELEE--------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1849 KKNLSRMQA---------------------------LSDKLQLKVQSYKQQVEAAEAQANQYLSKYKKQQHELNEAKERA 1901
Cdd:TIGR02169 916 RKRLSELKAklealeeelseiedpkgedeeipeeelSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKR 995
|
890 900
....*....|....*....|...
gi 261245016 1902 EAAESQVNKLRAKAKELEKKVRE 1924
Cdd:TIGR02169 996 AKLEEERKAILERIEEYEKKKRE 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1074-1924 |
6.37e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.42 E-value: 6.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1074 KEFEMGQMNSKVENEKNQvSQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLnERLEEAGGTSLAQME 1153
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATE-EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDA-RKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1154 IT--KQQEARFQKLHHDMEETtRHFEATSASLKKRHAENLAELEgQVEHLQQVRLVLEQDKSDLQLQVDDL--LNRVDQM 1229
Cdd:PTZ00121 1155 EIarKAEDARKAEEARKAEDA-KKAEAARKAEEVRKAEELRKAE-DARKAEAARKAEEERKAEEARKAEDAkkAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1230 ARAKANAEKLCGLYERRLNEANTKLDE--VTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLSREKsnftRQVEELR 1307
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEarMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEK----KKADEAK 1308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1308 AQLEEESRSQSALSHAlQSAKHDYDLLREQYEEEQEvKAELHRALSKGNKETVQWRAKYEHDAMQRTEdleEAKKKLAIR 1387
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKA-EEAKKKADAAKKKAEEAKK-AAEAAKAEAEAAADEAEAAEEKAEAAEKKKE---EAKKKADAA 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1388 LQEAAEAMEVSNAKNASLERARHrlqlelGDALSDLGKARSVAAALGQKQQHSDKAlTSWKQKLDETQELLQASQKETRA 1467
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKAEEDKKK------ADELKKAAAAKKKADEAKKKAEEKKKA-DEAKKKAEEAKKADEAKKKAEEA 1456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1468 LSSEVLtfRQACEESTEAQETLKRQNQDLQEQicSLTNQVREGIKNLAEVEKA----KKLIEQEKTEVQVRLEETEGALE 1543
Cdd:PTZ00121 1457 KKAEEA--KKKAEEAKKADEAKKKAEEAKKAD--EAKKKAEEAKKKADEAKKAaeakKKADEAKKAEEAKKADEAKKAEE 1532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1544 RNESKILRFQLELSEA----KAELERKLSEKEEEAERLREKHQQAMGSLQSnldlEASSRIEATRLRKKMEGDLKEMEIQ 1619
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKAdelkKAEELKKAEEKKKAEEAKKAEEDKNMALRKA----EEAKKAEEARIEEVMKLYEEEKKMK 1608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1620 LCAANRQVSQMTRAlgqlqGQMKDLHQQLDDSIYQNKDLKEQVALAEQrtvlLQSELEELRTLQEQTERGRKLAEKELLE 1699
Cdd:PTZ00121 1609 AEEAKKAEEAKIKA-----EELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1700 ATERINlfhtqntsllSQKKKLEadvaQVQKEAGEMLQACQKaeekAKKTAAEAANmSEELKKEQDTNAHL--ERMRKNM 1777
Cdd:PTZ00121 1680 AKKAEE----------DEKKAAE----ALKKEAEEAKKAEEL----KKKEAEEKKK-AEELKKAEEENKIKaeEAKKEAE 1740
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1778 EQTIKDLQKRLDEAEQTAVLGSKKQIQKLESRVR-DLEGELESEVRRSAEAQReaRRLERGIKELTYQAEE-DKKNLSRM 1855
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRkEKEAVIEEELDEEDEKRR--MEVDKKIKDIFDNFANiIEGGKEGN 1818
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261245016 1856 QALSDKLQLKVQSYKQQVEAAEAQANQYlSKYKKQQHELNEAKERAEAAESQVNKLRAKAKELEKKVRE 1924
Cdd:PTZ00121 1819 LVINDSKEMEDSAIKEVADSKNMQLEEA-DAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEE 1886
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1029-1924 |
1.03e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 83.56 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1029 LERERKARMKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLRKKEFEMGQMNSKvENEKNQVSQLQKMVKELQTHILN 1108
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSY-ENELDPLKNRLKEIEHNLSKIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1109 LKEELESERTIRAKVEREKGDLVQDLEDLNERLEEaggtSLAQMEITKQQEAR-----FQKLHHDMEETTRhfEATSASL 1183
Cdd:TIGR00606 267 LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDE----QLNDLYHNHQRTVRekereLVDCQRELEKLNK--ERRLLNQ 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1184 KKRHAEN-LAELEGQVEHLQQVRLVLEQDKSDLQLQVD-DLLNRVDQMARAKANAEKLcgLYERRLNEANTKLDEVTQLA 1261
Cdd:TIGR00606 341 EKTELLVeQGRLQLQADRHQEHIRARDSLIQSLATRLElDGFERGPFSERQIKNFHTL--VIERQEDEAKTAAQLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1262 HDLTT---QKTKLQSESGEFFKRLEEKEALISQLSREKSNFTRQVEELRAQL-------EEESRSQSALSHALQSAKHDY 1331
Cdd:TIGR00606 419 SKERLkqeQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSdrileldQELRKAERELSKAEKNSLTET 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1332 DLLREQYEeeQEVKAELHRALSKGNKETvqwrAKYEHDAMQRTEDLEEAKKKLA----IRLQEAAEAMEVSN-----AKN 1402
Cdd:TIGR00606 499 LKKEVKSL--QNEKADLDRKLRKLDQEM----EQLNHHTTTRTQMEMLTKDKMDkdeqIRKIKSRHSDELTSllgyfPNK 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1403 ASLERARHRLQLELGDALSDLGKARSVAAALGQKQQHSDKALTS--------------------WKQKLDETQELLQASQ 1462
Cdd:TIGR00606 573 KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESkeeqlssyedklfdvcgsqdEESDLERLKEEIEKSS 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1463 KETRALSSEVLTFRQACEESTEAQET-------LKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRL 1535
Cdd:TIGR00606 653 KQRAMLAGATAVYSQFITQLTDENQSccpvcqrVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLA 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1536 EETEGALERNESKILRFQLELSEAKAELERKLSEKEEEAERLrekhQQAMGSLQSNLDLEASSRIEAtrlRKKMEGDLKE 1615
Cdd:TIGR00606 733 PGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLL----GTIMPEEESAKVCLTDVTIME---RFQMELKDVE 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1616 MEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEELRTLQEQtergrklaek 1695
Cdd:TIGR00606 806 RKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQ---------- 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1696 eLLEATERINLFHTQNTSLLSQKKKLEADVAQVQKEAGEMLQACQKAEEKAKKTAAEAanmSEELKKEQDTNAHLERMRK 1775
Cdd:TIGR00606 876 -IGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK---ETSNKKAQDKVNDIKEKVK 951
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1776 NMEQTIKDLQKRLDEaeqtavlGSKKQIQKLESRVRDLEGELESEVRRSAEAQREARRLERGIKELTYQAEEDKKNLSRM 1855
Cdd:TIGR00606 952 NIHGYMKDIENKIQD-------GKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLR 1024
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261245016 1856 QALSDKLQLKVQSYKQQVEAAEAQANQYLSKYKKQQHELNEAKERAEAAESQVNKLRAKAKELEKKVRE 1924
Cdd:TIGR00606 1025 KRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
822-1143 |
1.76e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.81 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 822 GLFFKIKPLAKSVGAGEEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCEslik 901
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE---- 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 902 skvELEVKIKELSRQVEEEEEINSELTARGRKLEDECSELKKEIYDLEAILAksekgkcaaEHKVRNLTEEVHSLNEEVS 981
Cdd:TIGR02169 741 ---ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS---------HSRIPEIQAELSKLEEEVS 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 982 KLSRVVKDAQETQQQTQEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERERKarmkcerEKRKLQDELKMNQEGAENLE 1061
Cdd:TIGR02169 809 RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG-------KKEELEEELEELEAALRDLE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1062 SSRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEEL-ESERTIRAKVEREKGDLvqDLEDLNER 1140
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELsEIEDPKGEDEEIPEEEL--SLEDVQAE 959
|
...
gi 261245016 1141 LEE 1143
Cdd:TIGR02169 960 LQR 962
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
926-1579 |
2.79e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 926 ELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQQTQEQLHIEE 1005
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1006 EKLSNMSKANLKLAQQIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLRKKEFEMGQMNSKV 1085
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1086 ENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNERLEEAggtslaqmeitkqqearfqkl 1165
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL--------------------- 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1166 hhdmeettrhfEATSASLKKRHAENLAELEGQVEHLQQVRLVLEQDKS--DLQLQVDDLLNRVDQMARAKANAEKLCGLY 1243
Cdd:COG1196 455 -----------EEEEEALLELLAELLEEAALLEAALAELLEELAEAAArlLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1244 ERRLNEANTKLDEVTQLAHDLttqktklqsESGEFFKRLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSALSHA 1323
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEAAL---------AAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1324 LQSakhdyDLLREQYEEEQEVKAELHRALSKGNKETVQWRAkyehdamqRTEDLEEAKKKLAIRLQEAAEAMEVSNAKNA 1403
Cdd:COG1196 595 GAI-----GAAVDLVASDLREADARYYVLGDTLLGRTLVAA--------RLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1404 SLERARHRLQLELGDALSDLGKARSVAAALGQKQQhsdkaltswKQKLDETQELLQASQKETRALSSEVLTFRQACEEST 1483
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELE---------EALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1484 EAQETLKRQNQDLQEqicsLTNQVREGIKNLAEVEKAKKLIEQEKTEVQvRL--------EETEGALERNESkiLRFQLE 1555
Cdd:COG1196 733 EREELLEELLEEEEL----LEEEALEELPEPPDLEELERELERLEREIE-ALgpvnllaiEEYEELEERYDF--LSEQRE 805
|
650 660
....*....|....*....|....*.
gi 261245016 1556 -LSEAKAELERKLSEKEEEA-ERLRE 1579
Cdd:COG1196 806 dLEEARETLEEAIEEIDRETrERFLE 831
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
838-1584 |
5.23e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 81.27 E-value: 5.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 838 EEIAGLKEECAQLQKALESSESQREELkTKQVSLVQEKNDLRLQ-----LQAEQETLANSEEQCES--------LIKSKV 904
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEEL-NKKIKDLGEEEQLRVKekigeLEAEIASLERSIAEKEReledaeerLAKLEA 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 905 ELE---VKIKELSRQVEEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVS 981
Cdd:TIGR02169 330 EIDkllAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 982 KLSRVVKDAQETQQQTQEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERERKARMKCEREK-------RKLQDELKMNQ 1054
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELydlkeeyDRVEKELSKLQ 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1055 EGAENLESSRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHI-------LN---LKEELESERTIRAKVE 1124
Cdd:TIGR02169 490 RELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIevaagnrLNnvvVEDDAVAKEAIELLKR 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1125 REKGDL-------VQDLEDLNERLEEAG--GTSLAQMEITKQQEARFQK------LHHDMEETTRH-------------F 1176
Cdd:TIGR02169 570 RKAGRAtflplnkMRDERRDLSILSEDGviGFAVDLVEFDPKYEPAFKYvfgdtlVVEDIEAARRLmgkyrmvtlegelF 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1177 EA----TSASLKKRHAE-NLAELEGQVEHLQQVRLVLEQDKSDLQLQVDDLLNRVDQMARAKANAEKLCGLYERRLNean 1251
Cdd:TIGR02169 650 EKsgamTGGSRAPRGGIlFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE--- 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1252 tkldevtQLAHDLTTQKtklqsesgeffKRLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSALSHALQSAKHDY 1331
Cdd:TIGR02169 727 -------QLEQEEEKLK-----------ERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1332 DllreqYEEEQEVKAElhraLSKGNKETVQWRAKYEHdAMQRTEDLEEAKKKLAIRLQEAAEAMEVSNAKNASLERARHR 1411
Cdd:TIGR02169 789 S-----HSRIPEIQAE----LSKLEEEVSRIEARLRE-IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1412 LQLELGDALSDLGKARSVAAALgqkqqhsDKALTSWKQKLDETQELLQASQKETRALSSEVltfrqacEESTEAQETLKR 1491
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDL-------ESRLGDLKKERDELEAQLRELERKIEELEAQI-------EKKRKRLSELKA 924
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1492 QNQDLQEQICSLTNQVREGIKNLAEVEKAKKlIEQEKTEVQVRLEETE----GALERNESKILRFqLELSEAKAELERKL 1567
Cdd:TIGR02169 925 KLEALEEELSEIEDPKGEDEEIPEEELSLED-VQAELQRVEEEIRALEpvnmLAIQEYEEVLKRL-DELKEKRAKLEEER 1002
|
810
....*....|....*..
gi 261245016 1568 SEKEEEAERLREKHQQA 1584
Cdd:TIGR02169 1003 KAILERIEEYEKKKREV 1019
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1129-1717 |
2.66e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.93 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1129 DLVQdLEDLNERLEEAGGTSLAQMEITKQQEARFQKLHHDMEETTrhfEATSASLKKRHAENLAELEGQVEHLQQVRLVL 1208
Cdd:PRK02224 157 DLLQ-LGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKE---EKDLHERLNGLESELAELDEEIERYEEQREQA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1209 EQDKSDLQLQVDDLLNRVDQMARAKANAEKLcglyERRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEAL 1288
Cdd:PRK02224 233 RETRDEADEVLEEHEERREELETLEAEIEDL----RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1289 ISQLSREKSNFTRQVEELRAQLEEESRSQSALSHALQSAKHDYDLLREQYEEEQEVKAELHRALSKGnKETVQwrakyeh 1368
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA-REAVE------- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1369 DAMQRTEDLEEAKKKLAIRLQEAAEAMEVSNAKNASLERARHRLQLELGDALSDLGKARsvaaalgqkqqhsdkaltswk 1448
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR--------------------- 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1449 QKLDETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQVrEGIKNLAEVEKAKKLIEQEK 1528
Cdd:PRK02224 440 ERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLEERR 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1529 TEVQVRLEETEGALERNESKIlrfqLELSEAKAELERKLSEKEEEAERLR---EKHQQAMGSLQSNLDlEASSRIEATRl 1605
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERA----EELRERAAELEAEAEEKREAAAEAEeeaEEAREEVAELNSKLA-ELKERIESLE- 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1606 rkKMEGDLKEMEiqlcaanrqvsQMTRALGQLQGQMKDLHQQLDDSiyqnkdlKEQVALAEQRTVLLQSELEELRTLQEQ 1685
Cdd:PRK02224 593 --RIRTLLAAIA-----------DAEDEIERLREKREALAELNDER-------RERLAEKRERKRELEAEFDEARIEEAR 652
|
570 580 590
....*....|....*....|....*....|..
gi 261245016 1686 TERGRklAEKELLEATERINLFHTQNTSLLSQ 1717
Cdd:PRK02224 653 EDKER--AEEYLEQVEEKLDELREERDDLQAE 682
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1232-1925 |
3.97e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.64 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1232 AKANAEKLCGLYERRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLSReKSNFTRQVEELRaQLE 1311
Cdd:PTZ00121 1120 AKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAAR-KAEEVRKAEELR-KAE 1197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1312 EESRSQSALSHALQSAKHDYDLLREQYEEEQEVKAELHRALSKGNKETVQWRAKYEHDAMQRTEDLEEAKKKLAIRLQEA 1391
Cdd:PTZ00121 1198 DARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1392 AEAMEVSNAKNA-SLERARHRLQLELGDALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSS 1470
Cdd:PTZ00121 1278 RKADELKKAEEKkKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1471 EVltfrQACEESTEAQETLKRQNQDLQEQICSLTNQVREGiknlaevEKAKKLIEQEKTEVQvrlEETEGALERNESKIL 1550
Cdd:PTZ00121 1358 EA----EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-------DEAKKKAEEDKKKAD---ELKKAAAAKKKADEA 1423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1551 RFQLElSEAKAELERKLSEKEEEAERLREKHQQAMGSlqSNLDLEASSRIEATRLRKKMEGDLKEMEIQLCAAnrqvsqm 1630
Cdd:PTZ00121 1424 KKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKA--EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE------- 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1631 tralgqlqgQMKDLHQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATErinLFHTQ 1710
Cdd:PTZ00121 1494 ---------EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE---LKKAE 1561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1711 NTSLLSQKKKLEADVAQVQKEAGEMLQACQKAEEKAKKTAAEAANM-SEELKKEQDTNAHLERMRKNMEQTIKDLQKRLD 1789
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1790 EAEQTAvlgSKKQIQKLESRVRDLEGEL-----------------ESEVRRSAEAQREARRLERGIKELTYQAEEDKKNL 1852
Cdd:PTZ00121 1642 EAEEKK---KAEELKKAEEENKIKAAEEakkaeedkkkaeeakkaEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA 1718
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261245016 1853 SRMQALSDKLQLKVQSYKQQVEAAEAQANQylskYKKQQHELNEAKERAEAAESQVNKLRakaKELEKKVREE 1925
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAEEDKKKAEE----AKKDEEEKKKIAHLKKEEEKKAEEIR---KEKEAVIEEE 1784
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
948-1716 |
4.78e-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: 78.09 E-value: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 948 LEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQQTQEQLHIEEEKLSNMSKANLKLAqQIDVLEG 1027
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRA-RIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1028 DLERERKARMKCEREKRKLQdeLKMNQEGAENLESSRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQT--- 1104
Cdd:TIGR00618 275 QEAVLEETQERINRARKAAP--LAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhs 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1105 -HILNlKEELESERTIRAKVEREKGD------LVQDLEDLNERLEEAGGTSLAQMEITKQQEARFQ-----KLHHDMEET 1172
Cdd:TIGR00618 353 qEIHI-RDAHEVATSIREISCQQHTLtqhihtLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSafrdlQGQLAHAKK 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1173 TRHFEATSASLKKRHAENLAELEGQVE-HLQQVRLVLEQDKSDLQlQVDDLLNRVDQMARAKANAEKLCGLYERRLNEAN 1251
Cdd:TIGR00618 432 QQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQSLKEREQQLQ-TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSC 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1252 TKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLSREksnfTRQVEELRAQLEEESRSQSALSHALQSAKHDY 1331
Cdd:TIGR00618 511 IHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSE----RKQRASLKEQMQEIQQSFSILTQCDNRSKEDI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1332 DLLR-----------EQYEEEQEVKAELHRALSKGNKETvqwrAKYEHDAMQRTEDLEEAKKKLAIrlqeAAEAMEVSNA 1400
Cdd:TIGR00618 587 PNLQnitvrlqdlteKLSEAEDMLACEQHALLRKLQPEQ----DLQDVRLHLQQCSQELALKLTAL----HALQLTLTQE 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1401 KNASLERARHRLQLELGDalsdlgkarSVAAALgQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEvltFRQACE 1480
Cdd:TIGR00618 659 RVREHALSIRVLPKELLA---------SRQLAL-QKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE---FNEIEN 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1481 ESTEAQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALERNESKILRFQLELSEAK 1560
Cdd:TIGR00618 726 ASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLE 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1561 AELERKLSEKEEEAERLREKHQQAMGSLQSNLDLEASSRIEATRLRKKMEGDLKemeiQLCAANRQVSQMTRALGQLQGq 1640
Cdd:TIGR00618 806 AEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSK----QLAQLTQEQAKIIQLSDKLNG- 880
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261245016 1641 mkdlHQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATERINLFHTQNTSLLS 1716
Cdd:TIGR00618 881 ----INQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADSHVNARKYQGLALLVADAYTGSVRPSATLS 952
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
839-1618 |
6.15e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.87 E-value: 6.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 839 EIAGLKEECAQLQKALESSESQR-EEL-KTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKSKvELEVKIKELSR- 915
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVRKaEELrKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAE-EAKKDAEEAKKa 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 916 -QVEEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKV---RNLTEEVHSLNEEVSKLSRVVKDAQ 991
Cdd:PTZ00121 1246 eEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKaeeKKKADEAKKKAEEAKKADEAKKKAE 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 992 ETQQQTQEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERERKARMKCEREKRKlQDELKMNQEGAENLESSRQKlAEQL 1071
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK-ADAAKKKAEEKKKADEAKKK-AEED 1403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1072 RKKEFEMgqmnSKVENEKNQVSQLQKMVKELQThILNLKEELESERtiRAKVEREKGDLVQDLEDLNERLEEAGGTSLAQ 1151
Cdd:PTZ00121 1404 KKKADEL----KKAAAAKKKADEAKKKAEEKKK-ADEAKKKAEEAK--KADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1152 MEITKQQEArfQKLHHDMEETTRHF-EATSASLKKRHAENLAELEgqvehlqQVRLVLEQDKSDLQLQVDDLlnrvdQMA 1230
Cdd:PTZ00121 1477 KKAEEAKKA--DEAKKKAEEAKKKAdEAKKAAEAKKKADEAKKAE-------EAKKADEAKKAEEAKKADEA-----KKA 1542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1231 RAKANAEKLCGLYERRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLSREKSNFTRQVEELRAQL 1310
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1311 EEESRSQSALSHALQSAKHdydllreqyEEEQEVKAELHRALSKGNKETVQWRAKYEHDAMQRTEDL----EEAKKKLAI 1386
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKK---------EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaeEDEKKAAEA 1693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1387 RLQEAAEAMEVSNAKNASLERARHRLQLELGDalsdlgKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETR 1466
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAE------EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1467 ALSSEVLTFRQACEEsteaqETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRlEETEGALERNe 1546
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDS-AIKEVADSKN- 1840
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261245016 1547 skilrfqLELSEAKAELERKLSEKEEEAErlrEKHQQAMGSLQSNLDLEASSRIEATRLRKKMEGDLKEMEI 1618
Cdd:PTZ00121 1841 -------MQLEEADAFEKHKFNKNNENGE---DGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
831-1397 |
9.69e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.49 E-value: 9.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 831 AKSVGAGEEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKSKVELEVKI 910
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 911 KELSRQVEEEEEINSELT----ARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAE------HKVRNLTEEVHSLNEEV 980
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKkaaeAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaakkkaEEKKKADEAKKKAEEDK 1404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 981 SKLSRVVKDAQETQQQTQEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERERKAR-MKCEREKRKLQDELKMNQEGAEN 1059
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEeAKKKAEEAKKADEAKKKAEEAKK 1484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1060 LESSRQKlAEQLRKKEFEMgqmnSKVENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNE 1139
Cdd:PTZ00121 1485 ADEAKKK-AEEAKKKADEA----KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK 1559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1140 -----------RLEEAGGTSLAQMEITKQ-QEARFQKLHHDMEETtrhfeatsaslKKRHAENLAELEGQVEHLQQVRLV 1207
Cdd:PTZ00121 1560 aeekkkaeeakKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEE-----------KKMKAEEAKKAEEAKIKAEELKKA 1628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1208 LEQDKSDLQLQvddllnrvdqmaraKANAEklcglyERRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEA 1287
Cdd:PTZ00121 1629 EEEKKKVEQLK--------------KKEAE------EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1288 LISQLSREKSNFTRQVEELRAQLEEESRSQSALSHALQSAKHDYDLLREQYEEEQEVKAELHRalSKGNKETVQWRAKYE 1367
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK--DEEEKKKIAHLKKEE 1766
|
570 580 590
....*....|....*....|....*....|
gi 261245016 1368 HDAMQRTEDLEEAKKKLAIRLQEAAEAMEV 1397
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEEELDEEDEKRRMEV 1796
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1226-1924 |
2.00e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 76.26 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1226 VDQMARAKANAEKLCGLYERRLNEANTKLDEVTQLAHDLTTQKTKLQsESGEFFKRLEEKEAliSQLSREKSNFTRQVEE 1305
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEG--YELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1306 LRAQLEEESRSQSALShalqsakhdydllreqyEEEQEVKAELHRALSKGNKETVQWRAKYEHDAMQRTEDLEEAKKKLA 1385
Cdd:TIGR02169 242 IERQLASLEEELEKLT-----------------EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1386 I---RLQEAAEAMEVSNAKNASLERARHRLQLELGDALSDLGKARSVAAALGQkqqhsdkALTSWKQKLDETQELLQASQ 1462
Cdd:TIGR02169 305 SlerSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE-------EYAELKEELEDLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1463 KETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGAL 1542
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1543 ERNESKILRFQLELSEAKAE---LERKLSEKEEEAERL--------------------------------------REKH 1581
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEydrVEKELSKLQRELAEAeaqaraseervrggraveevlkasiqgvhgtvaqlgsvGERY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1582 QQAMGSLQSNL--------DLEASSRIEATRLRK----------------------KMEG------DLKEMEIQLCAANR 1625
Cdd:TIGR02169 538 ATAIEVAAGNRlnnvvvedDAVAKEAIELLKRRKagratflplnkmrderrdlsilSEDGvigfavDLVEFDPKYEPAFK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1626 QVSQMT----------RALGQLQ------------GQMKDLHQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEELRTLQ 1683
Cdd:TIGR02169 618 YVFGDTlvvedieaarRLMGKYRmvtlegelfeksGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSEL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1684 EQTERGRKLAEKELLEATERINLFHTQNTSLLSQKKKLEADVAQVQKEAGEMLQACQKAEEKAKKTAAEAANMSEELKKE 1763
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1764 QDTNAHLERMRKnmEQTIKDLQKRLDEAEqtavlgskKQIQKLESRVRDLEGELESEVRRSAEAQREARRLERGIKELTY 1843
Cdd:TIGR02169 778 EEALNDLEARLS--HSRIPEIQAELSKLE--------EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1844 QAEEDKKNLsrmqalsDKLQLKVQSYKQQVEAAEAQANQYLSKYKKQQHELNEAKERAEAAESQVNKLRAKAKELEKKVR 1923
Cdd:TIGR02169 848 QIKSIEKEI-------ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
.
gi 261245016 1924 E 1924
Cdd:TIGR02169 921 E 921
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
837-1652 |
2.47e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 75.85 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 837 GEEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRlQLQAEQETLANSEEQCESLIKSKVELEVKIKELSRQ 916
Cdd:TIGR00606 199 GQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVK-SYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 917 VEEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHK-VRNLTEEVHSLNEEVSKLsrvvkDAQETQQ 995
Cdd:TIGR00606 278 KKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQReLEKLNKERRLLNQEKTEL-----LVEQGRL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 996 QTQEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLRKKE 1075
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1076 FEMGQMNSKVENEK----NQVSQLQKMVKELQT------HILNLKEEL----------------ESERTIRAKVEREKGD 1129
Cdd:TIGR00606 433 DEKKGLGRTIELKKeileKKQEELKFVIKELQQlegssdRILELDQELrkaerelskaeknsltETLKKEVKSLQNEKAD 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1130 LVQDLEDLNERLEEAG--GTSLAQME-ITKQQEARFQKLHhdmEETTRHFEATSASLKkrHAENLAELEGQVEHLQQVRL 1206
Cdd:TIGR00606 513 LDRKLRKLDQEMEQLNhhTTTRTQMEmLTKDKMDKDEQIR---KIKSRHSDELTSLLG--YFPNKKQLEDWLHSKSKEIN 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1207 VLEQDKSDLQLQVDDLLNRVDQMARAKANAEKLCGLYERRLNEA------NTKLDEVTQLAHDLTTQKTKLQSESG---E 1277
Cdd:TIGR00606 588 QTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsqdeESDLERLKEEIEKSSKQRAMLAGATAvysQ 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1278 FFKRLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSALSHALQSAKHDYDLLREQYEEEQEVKAELHRALSKGNK 1357
Cdd:TIGR00606 668 FITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1358 ETVQWRAKYEHDAMQRTEDLEE---------AKKKLAIRLQEAAEAMEVSNAKNASLERARHRLQLELGDALSDLgkars 1428
Cdd:TIGR00606 748 ELRNKLQKVNRDIQRLKNDIEEqetllgtimPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDR----- 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1429 VAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSS---EVLTFRQACEESTEAQETLKRQNQDLQEQICSLTN 1505
Cdd:TIGR00606 823 TVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIR 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1506 QVREGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALE------RNESKILRFQLELSEAKAE--LERKLSEKE------ 1571
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQdkvndiKEKVKNIHGYMKDIENKIQdgKDDYLKQKEtelntv 982
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1572 ----EEAERLREKHQQAMGSLQSNLDLE--ASSRIEATRLRKKMEGDLKEMEIQLCAANRQVSQMTRAlgqlqgQMKDLH 1645
Cdd:TIGR00606 983 naqlEECEKHQEKINEDMRLMRQDIDTQkiQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVL------QMKQEH 1056
|
....*..
gi 261245016 1646 QQLDDSI 1652
Cdd:TIGR00606 1057 QKLEENI 1063
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1071-1617 |
2.84e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.46 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1071 LRKKEFEMGQMNSKVENEKNQvsQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNERLEEaggtsLA 1150
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREE-----LE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1151 QMeitkqqEARFQKLHHDMEETTRHFEATSASLKKRHaENLAELEGQVEHLQQVRLVLEQDKSDLQLQVDDLLNRVDQMA 1230
Cdd:PRK02224 255 TL------EAEIEDLRETIAETEREREELAEEVRDLR-ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1231 RAkanaeklcgLYERRLN--EANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLSREKSNFTRQVEELRA 1308
Cdd:PRK02224 328 DR---------LEECRVAaqAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1309 QLEEESRSQSALSHALQSAKHDYDLLREQ-------YEEEQEVKAELHRALSKGN-KETVQWRAKYEHdaMQRTEDLEEA 1380
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREReaeleatLRTARERVEEAEALLEAGKcPECGQPVEGSPH--VETIEEDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1381 KKKLAIRLQEAAEAMEVSNAKnasLERArhrlqlelgdalSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQA 1460
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEER---LERA------------EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1461 SQKETRALSSEVLTFRQAC----EESTEAQETLKRQNQDLQEqicsltnqVREGIKNLAEVEKAKKLIEQEKTEVQVRLE 1536
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAaeaeEEAEEAREEVAELNSKLAE--------LKERIESLERIRTLLAAIADAEDEIERLRE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1537 ETEGALERNESKILRFQlELSEAKAELERKLSekEEEAERLREKHQQAMGSLQSNLDLEASSRIEATRLRKKM---EGDL 1613
Cdd:PRK02224 614 KREALAELNDERRERLA-EKRERKRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIgavENEL 690
|
....
gi 261245016 1614 KEME 1617
Cdd:PRK02224 691 EELE 694
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1300-1925 |
4.48e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 74.83 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1300 TRQVEELRAQLEEESRSQSALSHAlQSAKHDYDLLREQYEEEQEVKAELHRALSKGNKETVQWRAKYEhdamQRTEDLEE 1379
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKA-ESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLA----ARKQELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1380 AKKKLAIRLQEAAEamevsnaKNASLERARHRLQLELGDALSDLGKARsvaaALGQKQQHSDKALTSWKQKLDETQELLQ 1459
Cdd:pfam01576 76 ILHELESRLEEEEE-------RSQQLQNEKKKMQQHIQDLEEQLDEEE----AARQKLQLEKVTTEAKIKKLEEDILLLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1460 AS----QKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRL 1535
Cdd:pfam01576 145 DQnsklSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1536 EETEGALERNESKILRFQLELSEAKAELERKLSEKEEEAERLREKHQQaMGSLQSNLDLEASSRIEATRLRKKMEGDLK- 1614
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQ-ISELQEDLESERAARNKAEKQRRDLGEELEa 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1615 ---EMEIQLCAANRQV---SQMTRALGQLQGQMKDLHQQLDDSIyQNKDLKEQVALAEqrtvlLQSELEELRTLQEQTER 1688
Cdd:pfam01576 304 lktELEDTLDTTAAQQelrSKREQEVTELKKALEEETRSHEAQL-QEMRQKHTQALEE-----LTEQLEQAKRNKANLEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1689 GRKLAEKELLEATERINLFHTQNTSLLSQKKKLEADVAQVQKEAGEMLQACQKAEEKAKKTAAEAANMSEELKKEQDTNA 1768
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1769 HLERMRKNMEQTIKDLQKRLDEAEQtavlgskkQIQKLESRVRDLEGELESEVRRSAEAQREARRLERGIKELTYQAEED 1848
Cdd:pfam01576 458 KLSKDVSSLESQLQDTQELLQEETR--------QKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDM 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1849 KKNLSRMQALSD-------KLQLKVQSYKQQVEAAEAQANQYLSKYKKQQHELNEAKERAEAAESQVNKLRAKAKELEKK 1921
Cdd:pfam01576 530 KKKLEEDAGTLEaleegkkRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQM 609
|
....
gi 261245016 1922 VREE 1925
Cdd:pfam01576 610 LAEE 613
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1274-1925 |
8.56e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.41 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1274 ESGEFFKRLEEKEalISQLSREKSNFTRQveELRAQLEEESRSQSALSHALQSAKHDyDLLREQYEEEQEvKAELHRALS 1353
Cdd:PTZ00121 1034 EYGNNDDVLKEKD--IIDEDIDGNHEGKA--EAKAHVGQDEGLKPSYKDFDFDAKED-NRADEATEEAFG-KAEEAKKTE 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1354 KGNKEtvqwRAKYEHDAMQRTED---LEEAKKKLAIRlqEAAEAMEVSNAKNASLER-ARHRLQLELGDALSDLGKARSV 1429
Cdd:PTZ00121 1108 TGKAE----EARKAEEAKKKAEDarkAEEARKAEDAR--KAEEARKAEDAKRVEIARkAEDARKAEEARKAEDAKKAEAA 1181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1430 AAALG-QKQQHSDKALTSWK----QKLDETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLT 1504
Cdd:PTZ00121 1182 RKAEEvRKAEELRKAEDARKaeaaRKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1505 NQVREGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALERNESKILRFQLELSEAKAELERKLSEKEEEAERLREKHQQA 1584
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA 1341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1585 MGSLQSNLDLEASSRIEATRLRKKMEGDLKEMEiqlcaANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNKDLKEQVAl 1664
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE-----EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA- 1415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1665 AEQRTVLLQSELEELRTLQE---QTERGRKLAE--KELLEATERINLfhtqntsllsQKKKLEADVA-QVQKEAGEMLQA 1738
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKADEakkKAEEAKKADEakKKAEEAKKAEEA----------KKKAEEAKKAdEAKKKAEEAKKA 1485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1739 CQKAEEKAKKTAAeaanmSEELKKEQDTNAHLERMRKNMEQTIKDLQKRLDEAEQTAVLGSKKQIQKLESRVRDLEGELE 1818
Cdd:PTZ00121 1486 DEAKKKAEEAKKK-----ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1819 SEVRRSAEAQREARRLERGIK--ELTYQAEEDKKNLSRMQALSDKLQLKVQSYKQQVEAAEAQANQYLSKYKKQQHELNE 1896
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
650 660 670
....*....|....*....|....*....|...
gi 261245016 1897 AKERAEAAESQVNK----LRAKAKELEKKVREE 1925
Cdd:PTZ00121 1641 KEAEEKKKAEELKKaeeeNKIKAAEEAKKAEED 1673
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
843-1538 |
1.35e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 73.23 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 843 LKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQ-----------AEQETLANSEEQCESLIKSKVELEVKIK 911
Cdd:pfam15921 108 LRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQntvheleaakcLKEDMLEDSNTQIEQLRKMMLSHEGVLQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 912 EL-------------------SRQVEEEEEINSELTARGRKLEDECSELKKEIY----DLEAILAKSEKGKCAAEHKVRN 968
Cdd:pfam15921 188 EIrsilvdfeeasgkkiyehdSMSTMHFRSLGSAISKILRELDTEISYLKGRIFpvedQLEALKSESQNKIELLLQQHQD 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 969 LTEEVHSLNE-EVSKLSRVVKDAQETQQQTQEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERE-RKARMKCEREKRKL 1046
Cdd:pfam15921 268 RIEQLISEHEvEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSElREAKRMYEDKIEEL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1047 QDELKM-NQEGAE-------------NLESSRQKLAEQLRKKEFEMgqmnsKVENEKNQ------------VSQLQKMVK 1100
Cdd:pfam15921 348 EKQLVLaNSELTEarterdqfsqesgNLDDQLQKLLADLHKREKEL-----SLEKEQNKrlwdrdtgnsitIDHLRRELD 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1101 ELQTHILNLKEELESERT-IRAKVEREkgdlVQDLEDLNERLEEAGGTSlAQMEITKQ------------------QEAR 1161
Cdd:pfam15921 423 DRNMEVQRLEALLKAMKSeCQGQMERQ----MAAIQGKNESLEKVSSLT-AQLESTKEmlrkvveeltakkmtlesSERT 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1162 FQKLHHDMEETTRHFEATSASLKKRHA------ENLAELEGQVEHLQQVRLVLEQdksdLQLQVDDLLNRVDQMARAKAN 1235
Cdd:pfam15921 498 VSDLTASLQEKERAIEATNAEITKLRSrvdlklQELQHLKNEGDHLRNVQTECEA----LKLQMAEKDKVIEILRQQIEN 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1236 AEKLCGLYERrlnEANTKLDEVTQLAHDLTTQKTKLQSesgefFKRLEEK--------EALISQLSREKSNFTRQVEELR 1307
Cdd:pfam15921 574 MTQLVGQHGR---TAGAMQVEKAQLEKEINDRRLELQE-----FKILKDKkdakirelEARVSDLELEKVKLVNAGSERL 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1308 AQLEEESRSQSALSHALQSAKHDYDLLREQYEeeqevkaelhralskgnketvqwraKYEHDAMQRTEDLEEAKKKLAIR 1387
Cdd:pfam15921 646 RAVKDIKQERDQLLNEVKTSRNELNSLSEDYE-------------------------VLKRNFRNKSEEMETTTNKLKMQ 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1388 LQEAAEAMEVSNAKNASLERAR-HRLQLELGdALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQEllqasqkETR 1466
Cdd:pfam15921 701 LKSAQSELEQTRNTLKSMEGSDgHAMKVAMG-MQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKE-------EKN 772
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261245016 1467 ALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAkkLIEQEKTEVQVRLEET 1538
Cdd:pfam15921 773 KLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDI--IQRQEQESVRLKLQHT 842
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
862-1708 |
1.59e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 73.08 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 862 EELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKSKVELEVKIKEL-SRQVEEEEEINSELTARGRKLEDECSE 940
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLyLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 941 LKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQQTQEQLHIEEEKLSNMSKANLKLAQ 1020
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1021 QIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLRKKEFEMGQMNSKVENEKNQV------SQ 1094
Cdd:pfam02463 336 EIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAqlllelAR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1095 LQKMV--KELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNERLEEAGGTSLAQMEITKQQEARFQKLhhdMEET 1172
Cdd:pfam02463 416 QLEDLlkEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL---LLSR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1173 TRHFEATSASLKKRHAENLAELEG-QVEHLQQVRLVLEQDKSDLQLQVDDLLNRVDQMARAKANAEKLCGLYERRLNEAN 1251
Cdd:pfam02463 493 QKLEERSQKESKARSGLKVLLALIkDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1252 TKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSALSHALQSAKHDY 1331
Cdd:pfam02463 573 LPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGV 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1332 DLLREQYE------EEQEVKAELHRALSKGNKETVQWRAKYEHDAMQRTEDLEEAKKKLAIRLQEAAEAMEVSNAKNAS- 1404
Cdd:pfam02463 653 SLEEGLAEksevkaSLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQd 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1405 -LERARHRLQLELGDALSDLGKARSVAAALGQKQQHsdkaltswkQKLDETQELLQASQKETRALSSEVLTFRQACEEST 1483
Cdd:pfam02463 733 kINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE---------LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1484 EAQETLKRQNQDLQEQICSLTNQVrEGIKNLAEVEKAKKLIEQEKtEVQVRLEETEGALERNESKILRFQLELSEAKAEL 1563
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQE-EKIKEEELEELALELKEEQK-LEKLAEEELERLEEEITKEELLQELLLKEEELEE 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1564 ERKLSEKEEEAERLREKHQQAM-GSLQSNLDLEASSRIEATRLRKK---MEGDLKEMEIQLCAANRQVSQMTRALGQLQG 1639
Cdd:pfam02463 882 QKLKDELESKEEKEKEEKKELEeESQKLNLLEEKENEIEERIKEEAeilLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261245016 1640 QMKDLHQQLDDSIYQNKDLKEQVALAEQrtvllqsELEELRTLQEQTERGRKLAEKELLEATERINLFH 1708
Cdd:pfam02463 962 NKRLLLAKEELGKVNLMAIEEFEEKEER-------YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFL 1023
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1085-1643 |
1.85e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1085 VENEKNQVSQLQKMVKELQTHIlNLKEELESERTIRAKV-----EREKGDLVQDLEDLNERLEEAggtslaqmeitKQQE 1159
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYA-AARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARL-----------EAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1160 ARFQKLHHDMEETTRhfeatsaSLKKRHAEN----LAELEGQVEHLQQVRlvleQDKSDLQLQVDDLLNRVDqmARAKAN 1235
Cdd:COG4913 312 ERLEARLDALREELD-------ELEAQIRGNggdrLEQLEREIERLEREL----EERERRRARLEALLAALG--LPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1236 AEKLcglyERRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLSREKSNFTRQVEELRAQL----- 1310
Cdd:COG4913 379 AEEF----AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALaealg 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1311 ----------------EEESRSQSA------------------------------------------------------- 1319
Cdd:COG4913 455 ldeaelpfvgelievrPEEERWRGAiervlggfaltllvppehyaaalrwvnrlhlrgrlvyervrtglpdperprldpd 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1320 -LSHALQSAKHDY-DLLREQYEEEQEVK-----AELHRA--------LSKGNketvqwRAKYEHDAMQRTE-------DL 1377
Cdd:COG4913 535 sLAGKLDFKPHPFrAWLEAELGRRFDYVcvdspEELRRHpraitragQVKGN------GTRHEKDDRRRIRsryvlgfDN 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1378 EEAKKKLAIRLQEAAEAMEVSNAKNASLERARHRLQlELGDALSDLGKARSVAAALGQKQqhsdKALTSWKQKLDEtqel 1457
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDVASAE----REIAELEAELER---- 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1458 LQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEvQVRLEE 1537
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE-ERFAAA 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1538 TEGALERneskilRFQLELSEAKAELERKLSEKEEEAERLREKHQQAMGSLQSNLDLEASSRIEATRLRKKMEGD-LKEM 1616
Cdd:COG4913 759 LGDAVER------ELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDgLPEY 832
|
650 660
....*....|....*....|....*..
gi 261245016 1617 EIQLcaANRQVSQMTRALGQLQGQMKD 1643
Cdd:COG4913 833 EERF--KELLNENSIEFVADLLSKLRR 857
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1244-1894 |
4.52e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 71.69 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1244 ERRLNEANtKLDEVTQ--LAHDLTTQKTKLQSESgeffkrlEEKEALISQLSREksnfTRQVEELRAQLEEESrsqsals 1321
Cdd:pfam15921 91 QRRLNESN-ELHEKQKfyLRQSVIDLQTKLQEMQ-------MERDAMADIRRRE----SQSQEDLRNQLQNTV------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1322 HALQSAKhdydLLREQYEEEQEVKAELHRALSKGNKETVqwrakyeHDAMQRTEDLEEAKKKlairlqEAAEAMEVSNAK 1401
Cdd:pfam15921 152 HELEAAK----CLKEDMLEDSNTQIEQLRKMMLSHEGVL-------QEIRSILVDFEEASGK------KIYEHDSMSTMH 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1402 NASLERARHRLQLELGDALSDL-GKARSVAAAL-GQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEVLTFR-QA 1478
Cdd:pfam15921 215 FRSLGSAISKILRELDTEISYLkGRIFPVEDQLeALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARsQA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1479 CEESTEA---QETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKA--KKLIEQEKTEVQVRLEETEGALERNEskilrFQ 1553
Cdd:pfam15921 295 NSIQSQLeiiQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMyeDKIEELEKQLVLANSELTEARTERDQ-----FS 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1554 LELSEAKAELERKLSE-KEEEAERLREKHQQamgslQSNLDLEASSRIEATRLRKKMegDLKEMEIQLCAANRQV----- 1627
Cdd:pfam15921 370 QESGNLDDQLQKLLADlHKREKELSLEKEQN-----KRLWDRDTGNSITIDHLRREL--DDRNMEVQRLEALLKAmksec 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1628 -SQMTRALGQLQGQMKDLHQ--QLDDSIYQNKDLKEQVA--LAEQRTVLLQSE--LEELRTLQEQTERGRKLAEKELLEA 1700
Cdd:pfam15921 443 qGQMERQMAAIQGKNESLEKvsSLTAQLESTKEMLRKVVeeLTAKKMTLESSErtVSDLTASLQEKERAIEATNAEITKL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1701 TERINLfhtqNTSLLSQKKKLEADVAQVQKEAGEMLQACQKAEEKAKKTAAEAANMSEELKKEQDTNAHLERMRKNMEQT 1780
Cdd:pfam15921 523 RSRVDL----KLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKE 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1781 IKDlqKRLdEAEQTAVLGSKK--QIQKLESRVRDLEGELESEVRRSAEAQREARRLERGIKELTyqaEEDKKNLSRMQAL 1858
Cdd:pfam15921 599 IND--RRL-ELQEFKILKDKKdaKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLL---NEVKTSRNELNSL 672
|
650 660 670
....*....|....*....|....*....|....*.
gi 261245016 1859 SDKLQLKVQSYKQQVEAAEAQANQYLSKYKKQQHEL 1894
Cdd:pfam15921 673 SEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSEL 708
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1185-1862 |
6.63e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 71.15 E-value: 6.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1185 KRHAENLAELEGQVEHLQQVRLVLEQDKS----------DLQLQVDDLLNRVDQMARAKANAEKLCGLYERRLNEANTKL 1254
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSlhgkaelltlRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1255 DEVTQLaHDLTTQKTKLQSESGEFFKRLEEKEALISQLS--REKSNFTRQV-----------------EELRAQLEEESR 1315
Cdd:TIGR00618 243 AYLTQK-REAQEEQLKKQQLLKQLRARIEELRAQEAVLEetQERINRARKAaplaahikavtqieqqaQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1316 SQSALSHALQSAKHDYDLLREQYEEEQEVKAElHRALSKGNKETVQWRAKY--EHDAMQRTEDLEEAKKKLAIRLQEAAE 1393
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ-EIHIRDAHEVATSIREIScqQHTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1394 AMEVSNAKNASLERARHRLQLELGDALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSsevl 1473
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ---- 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1474 TFRQACEESTEAQETLKRQNQDLQEQICSLTNQVREgiknlaevekakklieqekTEVQVRLEETEGALERNESKILRFQ 1553
Cdd:TIGR00618 477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH-------------------PNPARQDIDNPGPLTRRMQRGEQTY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1554 LELSEAKAELERKLSEKEEEAERLREKHQQAMGSLQSNLDLEASSRIEATRLRKKMEGDLKEMEIQLCAANRQVSQMTRA 1633
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1634 LGQLQGQMKDLHQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEE----LRTLQEQTERGRKLAEKEL----------LE 1699
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhalsIRVLPKELLASRQLALQKMqsekeqltywKE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1700 ATERINL---------------FHTQNTSLLSQKKKLEAD---VAQVQKEAGEMLQ-ACQKAEEKAKKTAAEAANMSEEL 1760
Cdd:TIGR00618 698 MLAQCQTllrelethieeydreFNEIENASSSLGSDLAARedaLNQSLKELMHQARtVLKARTEAHFNNNEEVTAALQTG 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1761 KKEQDTNAHLERMRKNMEQTIKDLQKRLDEAEQTAVLGSKKQIQKLESRVRDLEgELESEVRRSAEAQREARRLERGIKE 1840
Cdd:TIGR00618 778 AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE-QFLSRLEEKSATLGEITHQLLKYEE 856
|
730 740
....*....|....*....|..
gi 261245016 1841 LTYQAEEDKKNLSRMQALSDKL 1862
Cdd:TIGR00618 857 CSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
844-1580 |
1.13e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 70.39 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 844 KEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQL-QAEQETLANSEEQCESLIKSKVELEVKIKELSRQVEEEEE 922
Cdd:pfam02463 221 LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEiEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKS 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 923 INSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQQTQEQLH 1002
Cdd:pfam02463 301 ELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1003 IEEEKLS--------NMSKANLKL--AQQIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLR 1072
Cdd:pfam02463 381 LESERLSsaaklkeeELELKSEEEkeAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1073 KKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVER-------------------EKGDLVQD 1133
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLalikdgvggriisahgrlgDLGVAVEN 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1134 LEDLNERLEEAGGTSLAQMEITKQQEARFQKLHHDMEETTRHFEATSASLKKRHAENLAELEGQVEHLQQ---------V 1204
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKatleadeddK 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1205 RLVLEQDKSDLQLQVDDLLNRVDQMARAKANAEKLCGLYERRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEE 1284
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1285 KEALISqlsreksnfTRQVEELRAQLEEESRSQSALSHALQSAKHDYDLLREQYEEEQEVKAELhraLSKGNKETVQWRA 1364
Cdd:pfam02463 701 IKKKEQ---------REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS---RLKKEEKEEEKSE 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1365 KYEHDAMQRTEDLEEAKKKLAIRLQEAAEAMEVSNAKNASLERARHRLQLELGDALSDLGKARSVAAALGQKQQHSDKAL 1444
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1445 TSWKQKLDETQELLQASQKETRALSSEVLTFRQACEES-TEAQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKL 1523
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDeLESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261245016 1524 IEQEKTEVQVRLEETEGALERNESKILRFQLELS----EAKAELERKLSEKEEEAERLREK 1580
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNkrllLAKEELGKVNLMAIEEFEEKEER 989
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1094-1922 |
1.19e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 70.15 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1094 QLQKMVKELQTHILNLKEELESERTIRakvEREKGDLVQDLEDLNERLEEAGGTSLAQMEITKQQEARFQKLHHDMEETT 1173
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELH---EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1174 RHFEAtSASLKKRHAENLAElegQVEHLQQVRLVLEqdkSDLQLQVDDLLNRVDQMARAKANAEKLCGLYERRLNEAntk 1253
Cdd:pfam15921 152 HELEA-AKCLKEDMLEDSNT---QIEQLRKMMLSHE---GVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSA--- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1254 ldeVTQLAHDLTTQKTKLQsesGEFFKRLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQ-SALSHALQSAKHDYD 1332
Cdd:pfam15921 222 ---ISKILRELDTEISYLK---GRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEiTGLTEKASSARSQAN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1333 LLREQYEEEQEvkaelhralskgnkETVQWRAKYehdaMQRTEDLEEAKKKLAIRLQEAAEAMEvsnAKNASLERarhrl 1412
Cdd:pfam15921 296 SIQSQLEIIQE--------------QARNQNSMY----MRQLSDLESTVSQLRSELREAKRMYE---DKIEELEK----- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1413 QLELGDalSDLGKARSVAAALGQKQQHSDkaltswkqklDETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQ 1492
Cdd:pfam15921 350 QLVLAN--SELTEARTERDQFSQESGNLD----------DQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1493 NQDLQEqicsltnqvregiKNLaEVEKAKKLIEQEKTEVQVRLEETEGALE-RNES--KILRFQLELsEAKAELERKLSE 1569
Cdd:pfam15921 418 RRELDD-------------RNM-EVQRLEALLKAMKSECQGQMERQMAAIQgKNESleKVSSLTAQL-ESTKEMLRKVVE 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1570 KEEEAERLREKHQQAMGSLQSNLDlEASSRIEAT-----RLRKKMegDLKEMEIQlcaanrqvsqmtralgqlqgQMKDL 1644
Cdd:pfam15921 483 ELTAKKMTLESSERTVSDLTASLQ-EKERAIEATnaeitKLRSRV--DLKLQELQ--------------------HLKNE 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1645 HQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEELRTLQEQTER--GRKLAEKELLEATERINLFHTQNTSLLSQKK--- 1719
Cdd:pfam15921 540 GDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRtaGAMQVEKAQLEKEINDRRLELQEFKILKDKKdak 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1720 --KLEADVAQVQKEAGEMLQACQKAEEKAKKTAAEAANMSEELKKEQDtnaHLERMRKNMEQTIKDLQKRLDEAEQTAvl 1797
Cdd:pfam15921 620 irELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRN---ELNSLSEDYEVLKRNFRNKSEEMETTT-- 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1798 gskkqiQKLESRVRDLEGELEsevrrsaEAQREARRLERGIKELTYQAEEDKKNLSRMQALSDKLQLKVQSYKQQVEAAE 1877
Cdd:pfam15921 695 ------NKLKMQLKSAQSELE-------QTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNAN 761
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 261245016 1878 AQANQYLSKYKKQQHELNEAKERAEAAESQVNKLRAKAKELEKKV 1922
Cdd:pfam15921 762 KEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
838-1383 |
1.29e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.05 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 838 EEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKSKVELEVKIKELSRQV 917
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 918 EEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRN----------LTEEVHSLNEEVSKLSRVV 987
Cdd:TIGR04523 155 EKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNlkkkiqknksLESQISELKKQNNQLKDNI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 988 KDAQETQQQTQEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERERKARMKCEREKRKLQDELK-MNQEGAEN----LES 1062
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdLNNQKEQDwnkeLKS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1063 SRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNERLE 1142
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1143 EAGGTSLAQMEITKQQEARFQKLHHDMEETTRHFEATSASLKKRHAEnLAELEGQVEHLQQVRLVLEQDKSDLQLQVDDL 1222
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE-IKDLTNQDSVKELIIKNLDNTRESLETQLKVL 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1223 LNrvdQMARAKANAEKLcglyERRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLSREKSNFTRQ 1302
Cdd:TIGR04523 474 SR---SINKIKQNLEQK----QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1303 VEEL-----RAQLEEESRSQsalSHALQSAKHDYDLLreqyEEEQEVKAELHRALSKGNKETVQWRAKYEHDAMQRTEDL 1377
Cdd:TIGR04523 547 LNKDdfelkKENLEKEIDEK---NKEIEELKQTQKSL----KKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL 619
|
....*.
gi 261245016 1378 EEAKKK 1383
Cdd:TIGR04523 620 EKAKKE 625
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1056-1778 |
5.03e-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: 68.22 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1056 GAENLESSRQKLAEQLRKKEFEMGQMNSKVENEKnqvSQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLE 1135
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQK---FYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1136 DLNERLEEA----------GGTSLAQME----------------ITKQQEARFQKLHHDMEETTRHFEATSASLKKRhae 1189
Cdd:pfam15921 149 NTVHELEAAkclkedmledSNTQIEQLRkmmlshegvlqeirsiLVDFEEASGKKIYEHDSMSTMHFRSLGSAISKI--- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1190 nLAELEGQVEHLQ----QVRLVLEQDKSDLQLQVDDLL----NRVDQMAraKANAEKLCGLYERrlneANTKLDEVTQLA 1261
Cdd:pfam15921 226 -LRELDTEISYLKgrifPVEDQLEALKSESQNKIELLLqqhqDRIEQLI--SEHEVEITGLTEK----ASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1262 HDLTTQKTKLQSESGEFFKRLEEKEALISQLSRE----KSNFTRQVEELRAQLeeeSRSQSALSHALQSakhdydllREQ 1337
Cdd:pfam15921 299 SQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSElreaKRMYEDKIEELEKQL---VLANSELTEARTE--------RDQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1338 YEEE--------QEVKAELHRALSKGNKETVQWRAKYEHDaMQRTEDLEEAKKKLAIRlqeaaeAMEVSNAKnASLERAR 1409
Cdd:pfam15921 368 FSQEsgnlddqlQKLLADLHKREKELSLEKEQNKRLWDRD-TGNSITIDHLRRELDDR------NMEVQRLE-ALLKAMK 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1410 HRLQLELgdalsdlgkARSVAAALGQKQqhSDKALTSWKQKLDETQELLqasqketralssevltfRQACEESTEAQETL 1489
Cdd:pfam15921 440 SECQGQM---------ERQMAAIQGKNE--SLEKVSSLTAQLESTKEML-----------------RKVVEELTAKKMTL 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1490 KRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQvRLEETEGALERNESKILRFQLELSEAKAELErKLSE 1569
Cdd:pfam15921 492 ESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIE-ILRQ 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1570 KEEEAERLREKHQQAMGSLQ---SNLDLEASSR----IEATRLRKKMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQMK 1642
Cdd:pfam15921 570 QIENMTQLVGQHGRTAGAMQvekAQLEKEINDRrlelQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVK 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1643 DLHQQLDDSIYQNKDLKEQV-ALAEQRTVL------------------------LQSELEELRTLQEQTERGRKLAEKEL 1697
Cdd:pfam15921 650 DIKQERDQLLNEVKTSRNELnSLSEDYEVLkrnfrnkseemetttnklkmqlksAQSELEQTRNTLKSMEGSDGHAMKVA 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1698 LEATERINLFHTQNTSLLSQKKKLEADVAQVQKEAGEMLQACQKAEEKAKKTAAEAANMSEELKKEQDTNAHLERMRKNM 1777
Cdd:pfam15921 730 MGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANM 809
|
.
gi 261245016 1778 E 1778
Cdd:pfam15921 810 E 810
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1244-1924 |
6.93e-11 |
|
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: 67.77 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1244 ERRLNEANTKLDEVTQLAHDLTTQKTKL--QSESGEFFKRL--EEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSA 1319
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKSLerQAEKAERYKELkaELRELELALLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1320 LSHALQSAKHDYDLLREQYEEEQEVKAELHRALskgnKETVQWRAKYEHDAM---QRTEDLEEAKKKLAIRLQEAAEAME 1396
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKEL----YALANEISRLEQQKQilrERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1397 VSNAKNASLERARHRLQLELGDALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEVltfr 1476
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL---- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1477 qacEESTEAQETLKRQNQDLQEQIcsLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALERNESKILRFQLEL 1556
Cdd:TIGR02168 410 ---ERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1557 SEAKAE---LERKLSEKEEEAERLRE--KHQQAMGSLQSNLdleaSSRIEATrlrkkmEGDLKEMEIQLCAANRQVSqmt 1631
Cdd:TIGR02168 485 AQLQARldsLERLQENLEGFSEGVKAllKNQSGLSGILGVL----SELISVD------EGYEAAIEAALGGRLQAVV--- 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1632 ralgqlqgqMKDLHQQLDDSIYQNKDLKEQVALAEQrTVLLQSELEELRTLQEQTERGRKLAEKELLEATERI------- 1704
Cdd:TIGR02168 552 ---------VENLNAAKKAIAFLKQNELGRVTFLPL-DSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsyl 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1705 --NLFHTQN-TSLLSQKKKLEADVAQVQKEaGEMLQACQKAEEkakktaaeaanmseelKKEQDTNAHLERmrknmeqti 1781
Cdd:TIGR02168 622 lgGVLVVDDlDNALELAKKLRPGYRIVTLD-GDLVRPGGVITG----------------GSAKTNSSILER--------- 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1782 kdlQKRLDEAEQtavlgskkQIQKLESRVRDLEGELESEVRRSAEAQREARRLERGIKELTYQAEEDKKNLSRMQALSDK 1861
Cdd:TIGR02168 676 ---RREIEELEE--------KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261245016 1862 LQLKVQSYKQQVEAAEAQANQYLSKYKKQQHELNEAKERAEAAESQVNKLRAKAKELEKKVRE 1924
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE 807
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
882-1530 |
9.97e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 9.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 882 LQAEQETLANSEEQCESLIKSKVELEVKIKELSRQVEEEEEINSELTARGRKLEDECSELKKEIYDLEAI---------- 951
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeieeleke 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 952 LAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQQTQEQLHIEE------EKLSNMSKANLKLAQQIDVl 1025
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEfyeeylDELREIEKRLSRLEEEING- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1026 egdLERERKARMKCEREKRKLQDELKMNQEGAENLEsSRQKLAEQLRKKEFEMGQMNSKVENEknQVSQLQKMVKELQTH 1105
Cdd:PRK03918 326 ---IEERIKELEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1106 ilnlKEELESERTiraKVEREKGDLVQDLEDLN---ERLEEAGGT-SLAQMEITKQQEARFqklhhdMEETTRHFeatsa 1181
Cdd:PRK03918 400 ----KEEIEEEIS---KITARIGELKKEIKELKkaiEELKKAKGKcPVCGRELTEEHRKEL------LEEYTAEL----- 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1182 slkKRHAENLAELEgqvEHLQQVRLVLEqdksdlqlQVDDLLNRVDQMARAKANAEKLCGLyERRLNEANT-KLDEVTQL 1260
Cdd:PRK03918 462 ---KRIEKELKEIE---EKERKLRKELR--------ELEKVLKKESELIKLKELAEQLKEL-EEKLKKYNLeELEKKAEE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1261 AHDLTTQKTKLQSESGEFFKRLEEKEALISQLsREKSNFTRQVEELRAQLEEEsrsqsalshalqsakhdydLLREQYEE 1340
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEELKKKL-AELEKKLDELEEELAELLKE-------------------LEELGFES 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1341 EQEVKAELhRALSKGNKETVQWRakyehDAMQRTEDLEEAKKKLAIRLQEAAEAMEVsnaKNASLERARHRLQlELGDAL 1420
Cdd:PRK03918 587 VEELEERL-KELEPFYNEYLELK-----DAEKELEREEKELKKLEEELDKAFEELAE---TEKRLEELRKELE-ELEKKY 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1421 SDLGKARsvaaaLGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQnQDLQEQI 1500
Cdd:PRK03918 657 SEEEYEE-----LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERV-EELREKV 730
|
650 660 670
....*....|....*....|....*....|
gi 261245016 1501 CSLTNQVREGikNLAEVEKAKKLIEQEKTE 1530
Cdd:PRK03918 731 KKYKALLKER--ALSKVGEIASEIFEELTE 758
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
28-73 |
1.67e-10 |
|
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: 57.83 E-value: 1.67e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 261245016 28 DGKKKCWVPDGKNAYIEAEVKESGDDgQVIVETRDGEIMRIKEDKL 73
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGD-KVTVETEDGKTVTVKKDDV 45
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
843-1144 |
2.40e-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: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 843 LKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKSKVELEVKIKELSRQVEEEEE 922
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 923 INSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQQTQEQLH 1002
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1003 IEEEKLSNMSKANLKLAQQIDVLEGDLER--ERKARMKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLRKKEFEMGQ 1080
Cdd:TIGR04523 521 SLKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261245016 1081 MNSKVENEKNQVSQLQKMVKElqthilnLKEELESERTIRAKVEREKGDLVQDLEDLNERLEEA 1144
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEK-------AKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEI 657
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1095-1704 |
4.25e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1095 LQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNERLEEaggtslaqMEITKQQEARFQKLHHDMEETTR 1174
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE--------LPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1175 HFEatsaSLKKRhaenLAELEGQVEHLQQVRLVLEQDKSDLQLQVDDLLNRVDQMARAKANAEKLCGLyERRLNEANTKL 1254
Cdd:PRK03918 239 EIE----ELEKE----LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKL-SEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1255 DEVTQLAHDLTTQKTKLQsesgEFFKRLEEKEALISQLSREKSNFTRQVEEL--RAQLEEESRSQSALSHALQSAKHDYD 1332
Cdd:PRK03918 310 REIEKRLSRLEEEINGIE----ERIKELEEKEERLEELKKKLKELEKRLEELeeRHELYEEAKAKKEELERLKKRLTGLT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1333 L--LREQYEEEQEVKAELHRALSKGNKETVQWRAKyEHDAMQRTEDLEEAKKKLAI--RLQEAAEAMEVSNAKNASLERA 1408
Cdd:PRK03918 386 PekLEKELEELEKAKEEIEEEISKITARIGELKKE-IKELKKAIEELKKAKGKCPVcgRELTEEHRKELLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1409 RHRLQlELGDALSDLGK-ARSVAAALGQKQQHSdkaltswkqKLDETQELLQASQKETRALSSEVLtfrqacEESTEAQE 1487
Cdd:PRK03918 465 EKELK-EIEEKERKLRKeLRELEKVLKKESELI---------KLKELAEQLKELEEKLKKYNLEEL------EKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1488 TLKRQNQDLQEQICSLTNQVREG---IKNLAEVEKAKKLIEQEKTEVQVRLEETE-GALERNESKILRFQ------LELS 1557
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyneyLELK 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1558 EAKAELERKlsekEEEAERLREKHQQAMGSLQsnldlEASSRIEatRLRKKMEGDLKEM-EIQLCAANRQVSQMTRALGQ 1636
Cdd:PRK03918 609 DAEKELERE----EKELKKLEEELDKAFEELA-----ETEKRLE--ELRKELEELEKKYsEEEYEELREEYLELSRELAG 677
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261245016 1637 LQGQMKDLHQQLDDSIYQNKDLKEQVAL---AEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATERI 1704
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLKEELEErekAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1069-1551 |
7.37e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 7.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1069 EQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVE--REKGDLVQDLEDLNERLEEAgg 1146
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEEL-- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1147 tsLAQMEITKQQEARFQKLHHDMEETTRHFEATSASLKKRHAENLAELEGQVEHLQQVRLVLEQDKSDLQLQVDDLLNRV 1226
Cdd:COG4717 152 --EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1227 DQMARAKANAEKlcglyERRLNEANTKL---DEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLSREKSNFTRQV 1303
Cdd:COG4717 230 EQLENELEAAAL-----EERLKEARLLLliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1304 EELRAQLEEESRSQSALSHALQSAKHDYDLLREQYEEEQEVKAELHRALSKGNKETVQWRAKYEHDamQRTEDLEEAKKK 1383
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ--EIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1384 LAIRLQEAAEAMEVSNAKNASLERARHRLQLELGDALSDLGKArsvaaalgqkqqhsdkALTSWKQKLDETQELLQASQK 1463
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL----------------DEEELEEELEELEEELEELEE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1464 ETRALSSEVLTFRQACEEsTEAQETLkrqnQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQvrlEETEGALE 1543
Cdd:COG4717 447 ELEELREELAELEAELEQ-LEEDGEL----AELLQELEELKAELRELAEEWAALKLALELLEEAREEYR---EERLPPVL 518
|
....*...
gi 261245016 1544 RNESKILR 1551
Cdd:COG4717 519 ERASEYFS 526
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
844-1454 |
9.36e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.98 E-value: 9.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 844 KEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQA-------EQETLANSEEQCESLIKSKVELEVKIKELSRQ 916
Cdd:pfam15921 341 EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKlladlhkREKELSLEKEQNKRLWDRDTGNSITIDHLRRE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 917 VEEEEEINSELTARGRKLEDECS-ELKKEIYDLEailaksekGKCAAEHKVRNLTEEVHSLNEEVSKL------------ 983
Cdd:pfam15921 421 LDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQ--------GKNESLEKVSSLTAQLESTKEMLRKVveeltakkmtle 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 984 --SRVVKDAQETQQQTQEQLHIEEEKLSNM-SKANLKLaQQIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAENL 1060
Cdd:pfam15921 493 ssERTVSDLTASLQEKERAIEATNAEITKLrSRVDLKL-QELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQI 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1061 ESSRQKLAEQLRKK---EFEMGQMNSKVENEKNQVSQLQKM-------VKELQTHILNLkeELESERTIRAKVEREKGdl 1130
Cdd:pfam15921 572 ENMTQLVGQHGRTAgamQVEKAQLEKEINDRRLELQEFKILkdkkdakIRELEARVSDL--ELEKVKLVNAGSERLRA-- 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1131 VQDLEDLNERLEEAGGTSLAQM-EITKQQEA---RFQKLHHDMEETTRHF--EATSASLKKRHAEN-LAELEGQVEHLQQ 1203
Cdd:pfam15921 648 VKDIKQERDQLLNEVKTSRNELnSLSEDYEVlkrNFRNKSEEMETTTNKLkmQLKSAQSELEQTRNtLKSMEGSDGHAMK 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1204 VRLVLEQDKSDLQLQVDDLLNRVDQMARAKANAEKlcglyerrlnEANTKLDEVTQLAHDLTTQKTKLQSESGEFfkrle 1283
Cdd:pfam15921 728 VAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANK----------EKHFLKEEKNKLSQELSTVATEKNKMAGEL----- 792
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1284 ekEALISQLSREK---SNFTRQVEELRAQLEE-----ESRSQSALSHALQSAKHDYDLLREQYEEEQEVKAELHRALS-- 1353
Cdd:pfam15921 793 --EVLRSQERRLKekvANMEVALDKASLQFAEcqdiiQRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKPRLLQPASft 870
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1354 --KGNKETVQWRAKY-EHDAMQRTEDLEEAKKKLAIRLQEAAEAmeVSNAKNASLERARHRLQLELGDALSDLGKARSVA 1430
Cdd:pfam15921 871 rtHSNVPSSQSTASFlSHHSRKTNALKEDPTRDLKQLLQELRSV--INEEPTVQLSKAEDKGRAPSLGALDDRVRDCIIE 948
|
650 660
....*....|....*....|....*
gi 261245016 1431 AALGQKQQH-SDKALTSWKQKLDET 1454
Cdd:pfam15921 949 SSLRSDICHsSSNSLQTEGSKSSET 973
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
838-1329 |
1.27e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.50 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 838 EEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSE------EQCESLIKSKVElevKIK 911
Cdd:TIGR04523 138 KNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKnkllklELLLSNLKKKIQ---KNK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 912 ELSRQVEEEEEINSELTARGRKLEDECSELKKEIYD----LEAILAKSEKGKCA----------AEHKVRNLTEEVHSLN 977
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtqtqLNQLKDEQNKIKKQlsekqkeleqNNKKIKELEKQLNQLK 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 978 EEVSKLSRV-----VKDAQETQQQTQEQLHIEEEKLSNMSKANLKLAQQIDVLEgdlererKARMKCEREKRKLQDELKM 1052
Cdd:TIGR04523 295 SEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK-------KELTNSESENSEKQRELEE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1053 NQEGAENLESSRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQ 1132
Cdd:TIGR04523 368 KQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1133 DLEDLNERLEEAGGTSLAQMEITKQQEARFQKLHHDMEETTRHFEATSASLKKRHAEN------LAELEGQVEHLQQVRL 1206
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKkeleekVKDLTKKISSLKEKIE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1207 VLEQDKSDLQLQVDDLLNRVDQMarakaNAEKLCGLYERRLNEANTKLDEVTQlahdlttQKTKLQSESGEFFKRLEEKE 1286
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKD-----DFELKKENLEKEIDEKNKEIEELKQ-------TQKSLKKKQEEKQELIDQKE 595
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 261245016 1287 ALISQLSREKSNFTRQVEELRAQL---EEESRSQSALSHALQSAKH 1329
Cdd:TIGR04523 596 KEKKDLIKEIEEKEKKISSLEKELekaKKENEKLSSIIKNIKSKKN 641
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1243-1700 |
1.30e-09 |
|
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: 63.82 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1243 YERRLNEANTKLDEVTQLAHDLTTQKTKLqsesgeffkrLEEKEALIsqlsreksnftrqveELRAQLEEESRSQSALSH 1322
Cdd:COG3096 273 YMRHANERRELSERALELRRELFGARRQL----------AEEQYRLV---------------EMARELEELSARESDLEQ 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1323 ALQSAKHDYDLLREqyeeeqevkaelhralskgnkeTVQWRAKYEHdamqRTEDLEEakkkLAIRLQEAAEAMEVSNAKN 1402
Cdd:COG3096 328 DYQAASDHLNLVQT----------------------ALRQQEKIER----YQEDLEE----LTERLEEQEEVVEEAAEQL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1403 ASLERARHRLQLE---LGDALSDLGKARSVAAA-LGQKQQhsdkALtswkQKLDETQELLQASQKETRALSSEVLTFRQA 1478
Cdd:COG3096 378 AEAEARLEAAEEEvdsLKSQLADYQQALDVQQTrAIQYQQ----AV----QALEKARALCGLPDLTPENAEDYLAAFRAK 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1479 CEESTEAQETLkRQNQDLQEQICSLTNQVREGIKNLA-EVEKAKKLieQEKTEVQVRLEETEGALERNESkiLRFQLels 1557
Cdd:COG3096 450 EQQATEEVLEL-EQKLSVADAARRQFEKAYELVCKIAgEVERSQAW--QTARELLRRYRSQQALAQRLQQ--LRAQL--- 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1558 eakAELERKLSEKEEEAERLREKHQQAMGSLQSNLDLEassrieatRLRKKMEGDLKEMEIQLCAANRQVSQMTRALGQL 1637
Cdd:COG3096 522 ---AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELE--------ELLAELEAQLEELEEQAAEAVEQRSELRQQLEQL 590
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261245016 1638 QGQMKDLHQQ------LDDSIYQnkdLKEQVALA----EQRTVLLQSELEELRtlQEQTERGRKLAEKELLEA 1700
Cdd:COG3096 591 RARIKELAARapawlaAQDALER---LREQSGEAladsQEVTAAMQQLLERER--EATVERDELAARKQALES 658
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1003-1569 |
1.84e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.14 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1003 IEEEKLSNMSKANLKLAQQIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAENLESsrqkLAEQLRKKEFEMGQMN 1082
Cdd:PRK02224 196 IEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET----LEAEIEDLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1083 SKVENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNERLEE-------AGGTSLAQMEIT 1155
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEcrvaaqaHNEEAESLREDA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1156 KQQEARFQKLHHDMEETTRHFEATSASLKKRhAENLAELEGQVEHLQQVRLVLEQDKSDLQLQVDDLLNRVDQMARAKAN 1235
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDR-REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1236 AEKLCGLYERRLNEANTKLDE--VTQLAHDLttqktklqsESGEFFKRLEEKEALISQLSREKSNFTRQVEELRA---QL 1310
Cdd:PRK02224 431 LEATLRTARERVEEAEALLEAgkCPECGQPV---------EGSPHVETIEEDRERVEELEAELEDLEEEVEEVEErleRA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1311 EEESRSQSALSHALQSAKHDYDLL---REQYEEEQEVKAELHRALSKGNKETVQWRAKYEhDAMQRTEDLEEAKKKLAIR 1387
Cdd:PRK02224 502 EDLVEAEDRIERLEERREDLEELIaerRETIEEKRERAEELRERAAELEAEAEEKREAAA-EAEEEAEEAREEVAELNSK 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1388 LQEAAEAMEvsnaknaSLERARHRLQlELGDALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETra 1467
Cdd:PRK02224 581 LAELKERIE-------SLERIRTLLA-AIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEE-- 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1468 LSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQvregIKNLAEVEKAKKLIEqektEVQVRLEETEGALERNES 1547
Cdd:PRK02224 651 AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENE----LEELEELRERREALE----NRVEALEALYDEAEELES 722
|
570 580
....*....|....*....|...
gi 261245016 1548 KILRFQLELSEAKAE-LERKLSE 1569
Cdd:PRK02224 723 MYGDLRAELRQRNVEtLERMLNE 745
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
825-1413 |
1.92e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 825 FKIKPLAKSVGAGEEIAGLKEEcaqLQKALESSESQREELKTKQVSLVQEKNDLR---LQLQAEQETLANSEEQCESLIK 901
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKE---KEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 902 SKVELEVKIKELSRQVeeeeeinseltargRKLEDECSELKKEIYDLEAILAKSE------KGKCAAEHKVRNLTEEVHS 975
Cdd:PRK03918 253 SKRKLEEKIRELEERI--------------EELKKEIEELEEKVKELKELKEKAEeyiklsEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 976 LNEEVSKLSRVVKDAQETQQQTQEQLHIEEEKLSNMS--KANLKLAQQIDVLEGDLERERKARMkcEREKRKLQDELkmn 1053
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYEEAKAKKEELERLKKRLT--GLTPEKLEKEL--- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1054 qegaENLESSRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESErtIRAKVEREKGDLVQD 1133
Cdd:PRK03918 394 ----EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKE--LLEEYTAELKRIEKE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1134 LEDLNERLEEAgGTSLAQMEITKQQEARFQKLHhdmeETTRHFEATSASLKKRHAENLAELEGQVEHLQQVRLVLEQDKS 1213
Cdd:PRK03918 468 LKEIEEKERKL-RKELRELEKVLKKESELIKLK----ELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1214 DLQlqvdDLLNRVDQMARAKANAEKLCGLYERRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLS 1293
Cdd:PRK03918 543 SLK----KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREE 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1294 REKSNFTRQVEELRAQLEEESRSQSALSHALQSAKHDYDllREQYEEEQEVKAELHRALSKGNKEtvqwrakyehdaMQR 1373
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAE------------LEE 684
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 261245016 1374 TEDLEEAKKKLAIRLQEAAEAMEVSNAKNASLERARHRLQ 1413
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1208-1584 |
2.18e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1208 LEQDKSDLQLQVDDLLNRVDQMARAKANAEKLcglyERRLNEANTKLDEVTQL--AHDLTTQKTKLQSESGEF---FKRL 1282
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEEL----EAELEELREELEKLEKLlqLLPLYQELEALEAELAELperLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1283 EEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSALSH-ALQSAKHDYDLLREQYEEEQEVKAELHRALSKGNKETVQ 1361
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1362 WRAKYEHDAMQRTedLEEAKKKLAIR-------------------------LQEAAEAMEVSNAKNASLERARHRLQLEL 1416
Cdd:COG4717 232 LENELEAAALEER--LKEARLLLLIAaallallglggsllsliltiagvlfLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1417 GDALSDLGKAR--SVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEVLTFRQA---------CEESTEA 1485
Cdd:COG4717 310 LPALEELEEEEleELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAallaeagveDEEELRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1486 QETLKRQNQDLQEQICSLTNQVREGIKNLAEVekakkLIEQEKTEVQVRLEETEGALERNESKILRFQLELSEAKAELER 1565
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEEL-----LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420
....*....|....*....|....
gi 261245016 1566 -----KLSEKEEEAERLREKHQQA 1584
Cdd:COG4717 465 leedgELAELLQELEELKAELREL 488
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1455-1828 |
2.20e-09 |
|
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: 62.40 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1455 QELLQASQKETRALSSEVLTFRQA------CEESTEAQET-------LKRQNQDLQE-------QICSLTNQVREGIKNL 1514
Cdd:pfam05622 103 NEELTSLAEEAQALKDEMDILRESsdkvkkLEATVETYKKkledlgdLRRQVKLLEErnaeymqRTLQLEEELKKANALR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1515 AEVEKAKKLIeqekTEVQVRLEETEGALERNESKILRFQLELSEAKAELERKLSEKE---EEAERLREKHQQAMGSLQSN 1591
Cdd:pfam05622 183 GQLETYKRQV----QELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDtlrETNEELRCAQLQQAELSQAD 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1592 LDLEASSRIEATRLRKKMEGDLKEMEIQLCAANRQVSQmtRALGQLQGQMKDLHQQLDDSIYQNKDLKEQVALAEQRTVL 1671
Cdd:pfam05622 259 ALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRL--GQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILE 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1672 LQSELEEL-RTLQEQTER--GRKLAEKELLEATERINLFHTQNTSLLSQKKKLEADV-AQVQKEAGEMLQACQkaeekak 1747
Cdd:pfam05622 337 LQQQVEELqKALQEQGSKaeDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQdSNLAQKIDELQEALR------- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1748 ktaaeaanmseelKKEQDTNAHLERMRKNMEQ---TIKDLQKRLDEAEQTAVLGSKKQIQKLESRVRDLEGELE-SEVRR 1823
Cdd:pfam05622 410 -------------KKDEDMKAMEERYKKYVEKaksVIKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEkSKLQR 476
|
....*
gi 261245016 1824 SAEAQ 1828
Cdd:pfam05622 477 EQEEK 481
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1489-1924 |
4.98e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1489 LKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALERNESKILRFQLELSEAKAELERKLS 1568
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1569 EKEEEaerlrekhqqamgslqsnldleassrieatrLRKKMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQL 1648
Cdd:TIGR04523 303 QKEQD-------------------------------WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1649 DDSIYQNKDLKEQVALAEQRTVLL----QSELEELRTLQEQT---ERGRKLAEKELLEATERINLFHTQNTSLLSQKKKL 1721
Cdd:TIGR04523 352 TNSESENSEKQRELEEKQNEIEKLkkenQSYKQEIKNLESQIndlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1722 EADVAQVQKEAGEMlqacQKAEEKAKKTAAEAANMSEELKKEQDTnahLERMRKNMEQTIKDLQKRLDEAEQTaVLGSKK 1801
Cdd:TIGR04523 432 KETIIKNNSEIKDL----TNQDSVKELIIKNLDNTRESLETQLKV---LSRSINKIKQNLEQKQKELKSKEKE-LKKLNE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1802 QIQKLESRVRDLEGELESEVRRSAEAQREARRLERGIKELTYQAEEDKKNLSRmqalsDKLQLKVQSYKQQVEAAEAQAN 1881
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK-----ENLEKEIDEKNKEIEELKQTQK 578
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 261245016 1882 QYLSKYKKQQHELNEAKERAEAAESQVNKLRAKAKELEKKVRE 1924
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1340-1874 |
5.60e-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: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1340 EEQEVKAELHRALSKGNKETVQWRAKYEHDAMQRTEDLEEAKKKLAIRlQEAAEAMEVSNAKNAslerarhrLQLELG-- 1417
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQ-RKAIQELQFENEKVS--------LKLEEEiq 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1418 ---DALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEVLTFRQACEES--------TEAQ 1486
Cdd:pfam05483 142 enkDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENArlemhfklKEDH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1487 ETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKK----LIE---------QEKTEVQ---------------VRLEET 1538
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKdltfLLEesrdkanqlEEKTKLQdenlkeliekkdhltKELEDI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1539 EGALERNESKILRFQLELSEAKAELERKLSEKE---EEAERLREKHQQAMGSLQSNL-DLEASSRIEATRLRKKmEGDLK 1614
Cdd:pfam05483 302 KMSLQRSMSTQKALEEDLQIATKTICQLTEEKEaqmEELNKAKAAHSFVVTEFEATTcSLEELLRTEQQRLEKN-EDQLK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1615 EMEIQLCAANRQVSQMTRALGQLQGQMKDLH------QQLDDSIYQNKDLKEQVALAEQR-TVLLQSELEELRTLQEQ-- 1685
Cdd:pfam05483 381 IITMELQKKSSELEEMTKFKNNKEVELEELKkilaedEKLLDEKKQFEKIAEELKGKEQElIFLLQAREKEIHDLEIQlt 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1686 -TERGRKLAEKELLEATERINLFHTQNTSLLSQKKKLEADVAQVQKEAGEMLQACQKAEEKAKKTAAEAANMSEELKKEQ 1764
Cdd:pfam05483 461 aIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1765 DTNAH----LERMRKNMEQTIKDLQKRLDEAEQTA------VLGSKKQIQKLESRVRDLEGELESEVRRSAEAQREARRL 1834
Cdd:pfam05483 541 EKEMNlrdeLESVREEFIQKGDEVKCKLDKSEENArsieyeVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL 620
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 261245016 1835 ERgikeltyQAEEDKKNLSRMQALSDKLQLKVQSYKQQVE 1874
Cdd:pfam05483 621 KK-------KGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1277-1924 |
6.34e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1277 EFFKR--LEEKEALiSQLSREKSNFtRQVEELRAQLEEESRSQSALSHALQSAKhDYDLLREQYEEEQEVKAEL-----H 1349
Cdd:COG4913 211 DFVREymLEEPDTF-EAADALVEHF-DDLERAHEALEDAREQIELLEPIRELAE-RYAAARERLAELEYLRAALrlwfaQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1350 RALSKGNKETVQWRAKYEhDAMQRTEDLEEAKKKLAIRLQEAAEAM-EVSNAKNASLERARHRLQLELGDALSDLGKARS 1428
Cdd:COG4913 288 RRLELLEAELEELRAELA-RLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1429 VAAALGQKQQHSDKALTSWKQKLDETQELLQASQKEtralssevltFRQACEESTEAQETLKRQNQDLQEQIcsltNQVR 1508
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEA----------LEEALAEAEAALRDLRRELRELEAEI----ASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1509 EGIKNL-AEVEKAKKLIEQE--KTE---------VQVRLEET--EGALERneskILR-FQLEL---SEAKAELERKLsek 1570
Cdd:COG4913 433 RRKSNIpARLLALRDALAEAlgLDEaelpfvgelIEVRPEEErwRGAIER----VLGgFALTLlvpPEHYAAALRWV--- 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1571 eeEAERLREKHQqaMGSLQSNLDLEASSRIEATRLRKKME------GDLKEMEIQ-----LCAAN-RQVSQMTRALgQLQ 1638
Cdd:COG4913 506 --NRLHLRGRLV--YERVRTGLPDPERPRLDPDSLAGKLDfkphpfRAWLEAELGrrfdyVCVDSpEELRRHPRAI-TRA 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1639 GQMKDLHQ--QLDDSIYQNKDL------KEQVALAEQRTVLLQSELEELRTLQEQtergrklAEKELLEATERINLFHTq 1710
Cdd:COG4913 581 GQVKGNGTrhEKDDRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEA-------LEAELDALQERREALQR- 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1711 ntslLSQKKKLEADVAQVQKEagemlqacqkaeekakktaaeaanmseelkkeqdtnahlermrknmeqtIKDLQKRLDE 1790
Cdd:COG4913 653 ----LAEYSWDEIDVASAERE-------------------------------------------------IAELEAELER 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1791 AEQtavlgSKKQIQKLESRVRDLEGELESEVRRSAEAQREARRLERGIKELTYQAEEDKKNLSRMqalsdklqlkvqsyk 1870
Cdd:COG4913 680 LDA-----SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--------------- 739
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 261245016 1871 qqVEAAEAQANQYLSKYKKQQHELNEAKERAEAAESQVNKLRAKAKELEKKVRE 1924
Cdd:COG4913 740 --EDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELER 791
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
838-1261 |
6.89e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 838 EEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQ--ETLANSEEQCESLIKSKVELEVKIKELSR 915
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 916 QVEEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKSEKgkcAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQ 995
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE---ELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 996 QTQEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERERKARMKC------------EREKRKLQDELKMNQEGAENLESS 1063
Cdd:COG4717 238 AAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLvlgllallflllAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1064 RQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEE--------------LESERTIRAKVE--REK 1127
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEeleqeiaallaeagVEDEEELRAALEqaEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1128 GDLVQDLEDLNERLEEAGGTSLAQMEITKQQEarfqkLHHDMEETTRHFEATSASLKKRHAEnLAELEGQVEHLQQvrlv 1207
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREE-LAELEAELEQLEE---- 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 261245016 1208 lEQDKSDLQLQVDDLLNRVDQMARAKANAEKLCGLYERRLNEA-NTKLDEVTQLA 1261
Cdd:COG4717 468 -DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYrEERLPPVLERA 521
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
826-1177 |
7.75e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 7.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 826 KIKPLAKSVGAGEEIAGLKEECAQLQKALESSESQR--EELKTKQVSLVQEKNDLRLQLQAEQ--ETLANSEEQCESLIK 901
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAKKADEA 1527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 902 SKVELEVKIKELSRQVEEEEEINSELTARGRKLED--ECSELKKEIYDLEAILAKSEKGKCAAEHKVrnltEEVHSLNEE 979
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEkkKAEEAKKAEEDKNMALRKAEEAKKAEEARI----EEVMKLYEE 1603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 980 VSKLSRVVKDAQETQQQTQEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERERKARMKCEREKRKLQDElKMNQEGAEN 1059
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED-KKKAEEAKK 1682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1060 LESSRQKLAEQLRKKEFE---MGQMNSKVENEKNQVSQLQKM--VKELQTHILNLKEELESERTIRAKVEREKGDLVQDL 1134
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEakkAEELKKKEAEEKKKAEELKKAeeENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHL 1762
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 261245016 1135 EDLNERLEE---AGGTSLAQMEITKQQEARFQKLHHDMEETTRHFE 1177
Cdd:PTZ00121 1763 KKEEEKKAEeirKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFA 1808
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
838-1362 |
8.75e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 838 EEIAGLKEECAQLQKALESSESQREelktkQVSLVQEKNDLRLQLQAE-QETLANSEEQCESLIKSKVELEVKIKELSRQ 916
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQRE-----QARETRDEADEVLEEHEErREELETLEAEIEDLRETIAETEREREELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 917 VEEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDaqetqqq 996
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADD------- 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 997 tqeqlhIEEEklsnmskaNLKLAQQIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLRKKEF 1076
Cdd:PRK02224 354 ------LEER--------AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1077 EMGQMNSKVENEKNQVSQLQKMVKELQTHILNLK--------------EELESERTIRAKVEREKGDLVQDLEDLNERLE 1142
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1143 EAGGTSLAQMEITKQQEAR--FQKLHHDMEETTRHFEATSASLKKRHAENLAELEGQVEHLQQVRL----------VLEQ 1210
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERRedLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEeaeeareevaELNS 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1211 DKSDLQLQVDDLLNRVDQMARAKANAEKLCGLYERR--LNEANT--------KLDEVTQLAHDLTTQK-TKLQSESGEFF 1279
Cdd:PRK02224 580 KLAELKERIESLERIRTLLAAIADAEDEIERLREKReaLAELNDerrerlaeKRERKRELEAEFDEARiEEAREDKERAE 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1280 KRLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSALShALQSAKHDYDLLREQYEEEQEVKAELHRALSKGNKET 1359
Cdd:PRK02224 660 EYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERRE-ALENRVEALEALYDEAEELESMYGDLRAELRQRNVET 738
|
...
gi 261245016 1360 VQW 1362
Cdd:PRK02224 739 LER 741
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1214-1793 |
9.05e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 9.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1214 DLQLQVDDLLNRVDQMARAKANAEKLcglyeRRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEffKRLEEKEALISQLS 1293
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQIELL-----EPIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1294 REKSNFTRQVEELRAQLEEESRSQSALSHALQSAkhdydllreQYEEEQEVKAELHRAlskgnketvqwrakyehdamqr 1373
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGN---------GGDRLEQLEREIERL---------------------- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1374 TEDLEEAKKKLAiRLQEAAEAMEVSNAKNAS-LERARHRLQLELGDALSDLGKARSVAAALGQKQQHSDKALTSWKQKLD 1452
Cdd:COG4913 351 ERELEERERRRA-RLEALLAALGLPLPASAEeFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1453 EtqelLQASQKetrALSSEVLTFRQACEESTEAQET----------LKRQNQDLQEQICSLTNQVREGI----KNLAEVE 1518
Cdd:COG4913 430 S----LERRKS---NIPARLLALRDALAEALGLDEAelpfvgelieVRPEEERWRGAIERVLGGFALTLlvppEHYAAAL 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1519 KAkklIEQEKTEVQVRLEETEGALERNESKIL-------RFQLELSEAKAELERKLSEKE-----EEAERLRE------- 1579
Cdd:COG4913 503 RW---VNRLHLRGRLVYERVRTGLPDPERPRLdpdslagKLDFKPHPFRAWLEAELGRRFdyvcvDSPEELRRhpraitr 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1580 ----KHQQAMGSLQSNLDLEASSRI--EATRLRKKMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQmKDLHQQLDDSIY 1653
Cdd:COG4913 580 agqvKGNGTRHEKDDRRRIRSRYVLgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSW 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1654 QNKDLK---EQVALAEQRTVLLQSELEELRTLQEQTERgrklAEKELLEATERINLFHTQNTSLLSQKKKLEADVAQVQK 1730
Cdd:COG4913 659 DEIDVAsaeREIAELEAELERLDASSDDLAALEEQLEE----LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261245016 1731 EAGEMLQACQKAEEKAKktaaeaanmsEELKKEQDTNAHLERMRKNMEQTIKDLQKRLDEAEQ 1793
Cdd:COG4913 735 RLEAAEDLARLELRALL----------EERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1375-1890 |
1.54e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1375 EDLEEAKKKLaIRLQEAAEAMEVSNAKNASLERARHRLqlelgDALSDLGKARSVAAAlGQKQQHSDKALTSWKQKLDET 1454
Cdd:COG4913 235 DDLERAHEAL-EDAREQIELLEPIRELAERYAAARERL-----AELEYLRAALRLWFA-QRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1455 QELLQASQKETRALSSEVLTFRQACEES-TEAQETLKRQNQDLQEQicsltnqvregiknLAEVEKAKKLIEQEKTEVQV 1533
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERE--------------LEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1534 RLEETEGALERNESKILRFQLELSEAKAELERKLSEKEEEAERLREKHQQAMGSLQSnldLEAS-SRI--EATRLRKKME 1610
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS---LERRkSNIpaRLLALRDALA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1611 GDLKEMEIQLC-----------------AANR--------------QVSQMTRAL------GQLQGQ--MKDLHQQL--- 1648
Cdd:COG4913 451 EALGLDEAELPfvgelievrpeeerwrgAIERvlggfaltllvppeHYAAALRWVnrlhlrGRLVYErvRTGLPDPErpr 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1649 --DDSIYQNKDLKEQVA-------LAEQRTVLLQSELEELR------TLQEQTERGRKLAEKELLEATERINLFHTQNTs 1713
Cdd:COG4913 531 ldPDSLAGKLDFKPHPFrawleaeLGRRFDYVCVDSPEELRrhpraiTRAGQVKGNGTRHEKDDRRRIRSRYVLGFDNR- 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1714 llSQKKKLEADVAQVQKE---AGEMLQACQKAEEKAKKTAAEAANMSEELKKEQDTNAHLERMRKNMEQ---------TI 1781
Cdd:COG4913 610 --AKLAALEAELAELEEElaeAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAElerldassdDL 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1782 KDLQKRLDEAEQtAVLGSKKQIQKLESRVRDLEGELESEVRRSAEAQREARRLE-RGIKELTYQAEEDKKNLS---RMQA 1857
Cdd:COG4913 688 AALEEQLEELEA-ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdLARLELRALLEERFAAALgdaVERE 766
|
570 580 590
....*....|....*....|....*....|...
gi 261245016 1858 LSDKLQLKVQSYKQQVEAAEAQANQYLSKYKKQ 1890
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1107-1859 |
2.15e-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: 59.58 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1107 LNLKEELESERTIRAKVEREKGDLVQDLEDLNER---LE---EAGGTSLAQ-MEITKQQE--ARFQKlhhDMEETTRHFE 1177
Cdd:COG3096 288 LELRRELFGARRQLAEEQYRLVEMARELEELSAResdLEqdyQAASDHLNLvQTALRQQEkiERYQE---DLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1178 ATSASLKKRHaENLAELEGQVEHLQQVRLVLEQDKSDLQLQVDDLLNRV---DQMARAKANAEKLCGL-------YERRL 1247
Cdd:COG3096 365 EQEEVVEEAA-EQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiqyQQAVQALEKARALCGLpdltpenAEDYL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1248 NEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLSREKSNFTRQveelraQLEEESRSQSALSHALQSA 1327
Cdd:COG3096 444 AAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTAR------ELLRRYRSQQALAQRLQQL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1328 KHDYDLLREQYEEEQEVKaELHRALSKGNKETVQwrakyehDAMQRTEDLEEAKKKLAIRLQEAAEAMEVSNAKNASLER 1407
Cdd:COG3096 518 RAQLAELEQRLRQQQNAE-RLLEEFCQRIGQQLD-------AAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1408 ARHRLQlelgdALSDLGKA-RSVAAALGQKQQHSDKALTSWKQKLDETQELLQAsQKETRALSSEVLTFRQACE------ 1480
Cdd:COG3096 590 LRARIK-----ELAARAPAwLAAQDALERLREQSGEALADSQEVTAAMQQLLER-EREATVERDELAARKQALEsqierl 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1481 ------ESTEAQETLKRQNQDLQEQI------------CSLTNQVREGI--KNLAEVEKAKK----------LIEQEKT- 1529
Cdd:COG3096 664 sqpggaEDPRLLALAERLGGVLLSEIyddvtledapyfSALYGPARHAIvvPDLSAVKEQLAgledcpedlyLIEGDPDs 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1530 ---EVQVRLEETEGALERNESKILRFQLELSEA---KAELERKLSEKEEEAERLREKHQQAMGSLQSNLDLEAS-SRIEA 1602
Cdd:COG3096 744 fddSVFDAEELEDAVVVKLSDRQWRYSRFPEVPlfgRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAfSQFVG 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1603 TRLRKKMEGDlKEMEIQlcAANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQ----NKDLKEQVALAE----QRTVLLQS 1674
Cdd:COG3096 824 GHLAVAFAPD-PEAELA--ALRQRRSELERELAQHRAQEQQLRQQLDQLKEQlqllNKLLPQANLLADetlaDRLEELRE 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1675 ELEEL----RTLQEQTERGRKLAEK----------------ELLEATERI---------------NLFH----------T 1709
Cdd:COG3096 901 ELDAAqeaqAFIQQHGKALAQLEPLvavlqsdpeqfeqlqaDYLQAKEQQrrlkqqifalsevvqRRPHfsyedavgllG 980
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1710 QNTSLLSQ-KKKLEaDVAQVQKEAGEMLQACQKAEEKAKKTAAeaanmseELKKEQDTNAhleRMRKNMEQTIKDLQKRL 1788
Cdd:COG3096 981 ENSDLNEKlRARLE-QAEEARREAREQLRQAQAQYSQYNQVLA-------SLKSSRDAKQ---QTLQELEQELEELGVQA 1049
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261245016 1789 D-EAEQTAvLGSKKQIQKLESRVRDLEGELESEVRR----SAEAQREARRLERGIKELTYQAEEDKKNLSRMQALS 1859
Cdd:COG3096 1050 DaEAEERA-RIRRDELHEELSQNRSRRSQLEKQLTRceaeMDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLA 1124
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
843-1495 |
2.41e-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: 59.35 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 843 LKEECAQLQKALESSESQREElkTKQVsLVQEKNDLRLQLQAEQETLANSEeqcesliKSKVELEVKIKELSRQVEE-EE 921
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREE--TRQV-YMDLNNNIEKMILAFEELRVQAE-------NARLEMHFKLKEDHEKIQHlEE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 922 EINSELTARGRK---LEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQQTQ 998
Cdd:pfam05483 230 EYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSM 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 999 EQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERERKAR----MKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLRKK 1074
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHsfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1075 EFEMGQMNSKVENEKNQVSQLQKMVKELQThILNLKEELESERTIRAKVEREKGDLVQDLEDLNERLEeaggtslAQMEI 1154
Cdd:pfam05483 390 SSELEEMTKFKNNKEVELEELKKILAEDEK-LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLE-------IQLTA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1155 TKQQEARFQKLHHDMEETTRHFEATSASLKKRHAENLAELEGQVEHLQQVRLVLEQDKSDL---QLQVDDLLNRVDQMAR 1231
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIincKKQEERMLKQIENLEE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1232 AKANA----EKLCGLYERRLNEANTKLDEVTQLAHDLTTQKTK-------LQSESGEFFKRLEEKEALISQLSREKSNFT 1300
Cdd:pfam05483 542 KEMNLrdelESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKkekqmkiLENKCNNLKKQIENKNKNIEELHQENKALK 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1301 RQVEELRAQLEEESRSQSALSHALQSAKHDYDLLREQYEEEQEVKAELHRALskgnketvqwrakyehdamqrTEDLEEA 1380
Cdd:pfam05483 622 KKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKL---------------------LEEVEKA 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1381 KKKL--AIRLQEAAEamevsnaknaslERARHRLqlelgdalsdlgkARSVAAALGQKQQHS------DKALTSWKQKLD 1452
Cdd:pfam05483 681 KAIAdeAVKLQKEID------------KRCQHKI-------------AEMVALMEKHKHQYDkiieerDSELGLYKNKEQ 735
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 261245016 1453 ETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQD 1495
Cdd:pfam05483 736 EQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1472-1732 |
2.75e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1472 VLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALERNESKILR 1551
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1552 FQLELSEAKAELERKlseKEEEAERLREkhQQAMGSlQSNLDLEASSrieatrlrkkmegdlkemeiqlcaanRQVSQMT 1631
Cdd:COG4942 88 LEKEIAELRAELEAQ---KEELAELLRA--LYRLGR-QPPLALLLSP--------------------------EDFLDAV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1632 RALGQLQGQMKDLHQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATERINLFHTQN 1711
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
250 260
....*....|....*....|.
gi 261245016 1712 TSLLSQKKKLEADVAQVQKEA 1732
Cdd:COG4942 216 AELQQEAEELEALIARLEAEA 236
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1277-1874 |
3.09e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1277 EFFKRLEEKEALISQlsreKSNFTRQVEELRAQLEEESRSQSALSHALQSAKHDYDLLREQYEEEQEVKAELHralskgn 1356
Cdd:PRK03918 173 EIKRRIERLEKFIKR----TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE------- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1357 ketvqwrakyehDAMQRTEDLEEAKKKLAIRLQEAAEAMEVSNAKNASLERARHRLQ--LELGDALSDLGKARSvaaALG 1434
Cdd:PRK03918 242 ------------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYE---EYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1435 QKQQHSDKALTSWKQKLDETQELLQ------ASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQVR 1508
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKeleekeERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1509 EGIKN-LAEVEKAKKLIEQEKTEVQVRLEETEGALERNESKILrfqlELSEAKAELE---RKLSEkeEEAERLREKHQQA 1584
Cdd:PRK03918 387 EKLEKeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----ELKKAKGKCPvcgRELTE--EHRKELLEEYTAE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1585 MGSLQSNLdleassrIEATRLRKKMEGDLKEMEIQLCAANRqvsqmTRALGQLQGQMKDLHQQLddSIYQNKDLKEQVAL 1664
Cdd:PRK03918 461 LKRIEKEL-------KEIEEKERKLRKELRELEKVLKKESE-----LIKLKELAEQLKELEEKL--KKYNLEELEKKAEE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1665 AEQRTVLLQSELEELRTLQEQTERGRKLaEKELLEATERInlfHTQNTSLLSQKKKLEADVAQVQKEAGEMLQACQKAEE 1744
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEEL-KKKLAELEKKL---DELEEELAELLKELEELGFESVEELEERLKELEPFYN 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1745 KAKKTAAEAANMSEELKKEQDTNAHLERMRKNMEQT---IKDLQKRLDEAEQT----AVLGSKKQIQKLESRVRDLEGEL 1817
Cdd:PRK03918 603 EYLELKDAEKELEREEKELKKLEEELDKAFEELAETekrLEELRKELEELEKKyseeEYEELREEYLELSRELAGLRAEL 682
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 261245016 1818 ESEVRRSAEAQREARRLERGIKELTyQAEEDKKNLSRMQALSDKLQLKVQSYKQQVE 1874
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEERE-KAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1334-1919 |
3.89e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1334 LREQYEEEQEvkAELHRALSKGNKETVQWRAKYEHDAMQR---TEDLEEAKKKLAI------RLQEAAEAMEVSNAKNAS 1404
Cdd:PRK02224 192 LKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQReqaRETRDEADEVLEEheerreELETLEAEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1405 LERARHRLQLELGD---ALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEvltFRQACEE 1481
Cdd:PRK02224 270 TEREREELAEEVRDlreRLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA---HNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1482 STEAQETLKRQNQDLQEQICSLTnqvregiknlAEVEKAKKLIEQEKTEvqvrLEETEGALERNESKILRFQLELSEAKA 1561
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELE----------SELEEAREAVEDRREE----IEELEEEIEELRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1562 ELERKLSEKEEEAERLREkhqqamgslqsnldLEASSRIEATRLRKKmEGDLKEMEIQLCAANRQVSQMTRALGQLQGQM 1641
Cdd:PRK02224 413 FLEELREERDELREREAE--------------LEATLRTARERVEEA-EALLEAGKCPECGQPVEGSPHVETIEEDRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1642 KDLHQQLDDSIYQNKDLKEQVALAEQrtvlLQSELEELRTLQEQtergRKLAEKELLEATERINLFHTQNTSLLSQKKKL 1721
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAED----LVEAEDRIERLEER----REDLEELIAERRETIEEKRERAEELRERAAEL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1722 EADVAQVQKEAGEMLQACQKAEEKAKKTAAEAANMSEELKKEQDTNAHLERmRKNMEQTIKDLQKRLDE-AEQTAVlgSK 1800
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLREKREAlAELNDE--RR 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1801 KQIQKLESRVRDLEGELESEvrRSAEAQREARRLErgikelTYQAEEDKKnLSRMQALSDKLQLKVQSYKQQVEaaeaqa 1880
Cdd:PRK02224 627 ERLAEKRERKRELEAEFDEA--RIEEAREDKERAE------EYLEQVEEK-LDELREERDDLQAEIGAVENELE------ 691
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 261245016 1881 nqylskykkqqhELNEAKERAEAAESQVNKLRA---KAKELE 1919
Cdd:PRK02224 692 ------------ELEELRERREALENRVEALEAlydEAEELE 721
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1185-1847 |
4.60e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 58.66 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1185 KRHAENLAELEGQVEHLQQVRLVLEQDKSDLQlqvddllnrvdQMARAKANAEKLCGLYERRLNEANTKLDEVTQLAHDL 1264
Cdd:PRK10246 167 KERAELLEELTGTEIYGQISAMVFEQHKSART-----------ELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1265 TTQKTKLQSEsgefFKRLEEKEALISQLSREKSnftrQVEELRAQLEEESRSQSALSHALQSAKhdydlLREQYEEEQEV 1344
Cdd:PRK10246 236 LTAQQQQQQS----LNWLTRLDELQQEASRRQQ----ALQQALAAEEKAQPQLAALSLAQPARQ-----LRPHWERIQEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1345 KAELHRALSKGNK------ETVQWRAKYEHDAMQRTEDLEEAKKKLAIRLQEAAEAMEVSN------AKNASLERARHRL 1412
Cdd:PRK10246 303 SAALAHTRQQIEEvntrlqSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNelagwrAQFSQQTSDREQL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1413 QLELG---------DALSDLG---KARSVAAALGQkqQHSDKALtswKQKLDETQELLQASQKETRALSSevlTFRQACE 1480
Cdd:PRK10246 383 RQWQQqlthaeqklNALPAITltlTADEVAAALAQ--HAEQRPL---RQRLVALHGQIVPQQKRLAQLQV---AIQNVTQ 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1481 ESTEAQETLKRQNQDLQEQicsltNQVREGIKNLAEVEKAKKLIEQEKTEVQVRLE------------ETEGALERNESK 1548
Cdd:PRK10246 455 EQTQRNAALNEMRQRYKEK-----TQQLADVKTICEQEARIKDLEAQRAQLQAGQPcplcgstshpavEAYQALEPGVNQ 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1549 ILRFQLE-----LSEAKA-------ELERKLSEKEEEAERLREKHQQAMGSLQS-----NLDLEASSRI-----EATRLR 1606
Cdd:PRK10246 530 SRLDALEkevkkLGEEGAalrgqldALTKQLQRDESEAQSLRQEEQALTQQWQAvcaslNITLQPQDDIqpwldAQEEHE 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1607 KKME--GDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEELRTLQE 1684
Cdd:PRK10246 610 RQLRllSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQQRQNELTALQN 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1685 QTERGRKL-----AEKELLEATERINL-----FHTQNTSLLSQKKKLEADVAQVQKEAGEMLQacQKAEEKAKKTAAEAA 1754
Cdd:PRK10246 690 RIQQLTPLletlpQSDDLPHSEETVALdnwrqVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQA--QFDTALQASVFDDQQ 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1755 NMSEELKKEQdTNAHLERMRKNMEQTIKDLQKRLDEAEQT----------------AVLGSKKQIQKLESRVRD---LEG 1815
Cdd:PRK10246 768 AFLAALLDEE-TLTQLEQLKQNLENQRQQAQTLVTQTAQAlaqhqqhrpdgldltvTVEQIQQELAQLAQQLREnttRQG 846
|
730 740 750
....*....|....*....|....*....|..
gi 261245016 1816 ELESEVRRSAEAQREARRLERGIKELTYQAEE 1847
Cdd:PRK10246 847 EIRQQLKQDADNRQQQQALMQQIAQATQQVED 878
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
756-1202 |
5.31e-08 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 58.42 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 756 FKAFILDQLEERR---------DEKISKVFTLFQarargklmRITFQKILEERDALALIQENIRAFIAVKNCPWMGLFFK 826
Cdd:pfam15818 5 FKTSLLEALEELRmrreaetqyEEQIGKIIVETQ--------ELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 827 IKPLAKSVGAGE----EIAGLKEECAQLQKALESSEsqreelktKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKS 902
Cdd:pfam15818 77 EEEKGKYQLATEikekEIEGLKETLKALQVSKYSLQ--------KKVSEMEQKLQLHLLAKEDHHKQLNEIEKYYATITG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 903 KVEL--EVKIKeLSRQVEEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKSekgKCAAEHKVR----NLTEEVHSL 976
Cdd:pfam15818 149 QFGLvkENHGK-LEQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKS---KVTCQYKMGeeniNLTIKEQKF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 977 NEEVSKLSrvvKDAQETQQQTQEQLHIEEEKLSNMSKAN--LKLAQQIDVLEGDLERERKA----RMKCEREKRKLQDEL 1050
Cdd:pfam15818 225 QELQERLN---MELELNKKINEEITHIQEEKQDIIISFQhmQQLLQQQTQANTEMEAELKAlkenNQTLERDNELQREKV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1051 KMNQEGAENLESSRQKlAEQLRKKEFEmgQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESErtirakvEREKGDL 1130
Cdd:pfam15818 302 KENEEKFLNLQNEHEK-ALGTWKKHVE--ELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFE-------EDKKFQN 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261245016 1131 VQDLEDLNERLEEAGGTSLAQMEITKQQEARfqklhhdmEETTRHFEATSASLKKRHAENLAELEGQVEHLQ 1202
Cdd:pfam15818 372 VPEVNNENSEMSTEKSENLIIQKYNSEQEIR--------EENTKSFCSDTEYRETEKKKGPPVEEIIIEDLQ 435
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1450-1925 |
8.26e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1450 KLDETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEK- 1528
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKe 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1529 --TEVQVRLEETEGALERNESKILRFQLELSEAKAELErKLSEKEEEAERLREKHQQ--AMGSLQSNLdLEASSRIE--A 1602
Cdd:PRK03918 239 eiEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-ELEEKVKELKELKEKAEEyiKLSEFYEEY-LDELREIEkrL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1603 TRLRKKMEGDLKEMEiqlcaanrQVSQMTRALGQLQGQMKDLHQQLDDsiyqnkdLKEQVALAEqRTVLLQSELEELRTL 1682
Cdd:PRK03918 317 SRLEEEINGIEERIK--------ELEEKEERLEELKKKLKELEKRLEE-------LEERHELYE-EAKAKKEELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1683 Q-----EQTERGRKLAEKELLEATERINLFHTQNTSLLSQKKKLEADVAQVQK---------------EAGEMLQACQKA 1742
Cdd:PRK03918 381 LtgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteeHRKELLEEYTAE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1743 EEKAKKTAAEAANMSEELKKEQ-------DTNAHLERMRKNMEQtIKDLQKRLDEAEQTAVLGSKKQIQKLESRVRDLEG 1815
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELrelekvlKKESELIKLKELAEQ-LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKG 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1816 E---LESEVRRSAEAQREARRLERGIKELTYQAEEDKKNLSRMQALS-DKLQLKVQS----YKQQVEA--AEAQANQYLS 1885
Cdd:PRK03918 540 EiksLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKElepfYNEYLELkdAEKELEREEK 619
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 261245016 1886 KYKKQQHELNEAKERAEAAESQVNKLRAKAKELEKKVREE 1925
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE 659
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1651-1888 |
9.21e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1651 SIYQNKDLKEQVALAEQRTVLLQSELEELRT-LQEqtergrklAEKELLEATERINLFHT--QNTSLLSQKKKLEADVAQ 1727
Cdd:COG3206 159 EAYLEQNLELRREEARKALEFLEEQLPELRKeLEE--------AEAALEEFRQKNGLVDLseEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1728 VQKEAGEmLQAcqkaeekAKKTAAEAANMSEELKKEQDTNAHLERMRknmeQTIKDLQKRLDEAEQTavLGSK-KQIQKL 1806
Cdd:COG3206 231 ARAELAE-AEA-------RLAALRAQLGSGPDALPELLQSPVIQQLR----AQLAELEAELAELSAR--YTPNhPDVIAL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1807 ESRVRDLEGELESEVRRS-AEAQREARRLERGIKELTYQAEEDKKNLSRMQALSDKLQlkvqSYKQQVEAAEAQANQYLS 1885
Cdd:COG3206 297 RAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR----RLEREVEVARELYESLLQ 372
|
...
gi 261245016 1886 KYK 1888
Cdd:COG3206 373 RLE 375
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1369-1604 |
9.56e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 9.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1369 DAMQRTEDLEEAKKKLAIRLQEAAEAMEVSNAKNASLERARHRLQLELGDALSDLGKARSVAAALGQKQQHSDKALTSWK 1448
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1449 QKLdetQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEK 1528
Cdd:COG4942 104 EEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261245016 1529 TEVQVRLEETEGALERNESKILRfqleLSEAKAELERKLSEKEEEAERLREKHQQAMGSLQSNLDLEASSRIEATR 1604
Cdd:COG4942 181 AELEEERAALEALKAERQKLLAR----LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
838-1143 |
1.33e-07 |
|
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: 56.95 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 838 EEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKSKVELEVKIKELSRQV 917
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 918 EEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKSekgkcaaehkvrNLTEEVHSLNEEVSKLSRVVKDAQETQQQT 997
Cdd:TIGR04523 520 SSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKE------------NLEKEIDEKNKEIEELKQTQKSLKKKQEEK 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 998 QEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLErerkarmKCEREKRKLQDELKmnqegaeNLESSRQKLAEQLRKKEFE 1077
Cdd:TIGR04523 588 QELIDQKEKEKKDLIKEIEEKEKKISSLEKELE-------KAKKENEKLSSIIK-------NIKSKKNKLKQEVKQIKET 653
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261245016 1078 MgqmnSKVENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNERLEE 1143
Cdd:TIGR04523 654 I----KEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDLPKLEEKYKE 715
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1508-1787 |
1.50e-07 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 55.59 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1508 REGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALERNESKI---LRFQLELSEAKAELERKLSEKEEEAERLREK---- 1580
Cdd:pfam15905 69 LKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLnaaVREKTSLSASVASLEKQLLELTRVNELLKAKfsed 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1581 -HQQAMGSLQsnldleassrIEATRLRKKMEGDLKE-------MEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSI 1652
Cdd:pfam15905 149 gTQKKMSSLS----------MELMKLRNKLEAKMKEvmakqegMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1653 YQNKDLKEqvalaeqrtvllqsELEELRTLQEQtergrklAEKELLEATERINLFHTQNTSLLSQKKKLEADVAQVQKEA 1732
Cdd:pfam15905 219 SETEKLLE--------------YITELSCVSEQ-------VEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQI 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 261245016 1733 GEMLQACQKAEEKAKKTaaeaanMSEELKKEQDTNAHLERMRKNM---EQTIKDLQKR 1787
Cdd:pfam15905 278 KDLNEKCKLLESEKEEL------LREYEEKEQTLNAELEELKEKLtleEQEHQKLQQK 329
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1040-1791 |
1.66e-07 |
|
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: 56.57 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1040 EREKRKLQDELKMNQEGAENLESSRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESERTI 1119
Cdd:TIGR04523 39 EKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1120 RAKVEREKGDLVQDLEDLNERLEEAGGtslaqmEITKqQEARFQKLHHDMEETTRhfeatsaslkkrhaenlaelegQVE 1199
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLT------EIKK-KEKELEKLNNKYNDLKK----------------------QKE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1200 HLQQVRLVLEQDKSDLQLQVDDLLNRVDQMARAKANAEKlcglYERRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFF 1279
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKK----KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1280 KRLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSALSHALQSAKHDYDLLREQYEEEqevkaelhraLSKGNKet 1359
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD----------WNKELK-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1360 vqwrakyehdamqrtEDLEEAKKKLairlqeaaeamevsnaknaslerarhrlqlelgdalsdlgkarsvaaalgqkqQH 1439
Cdd:TIGR04523 314 ---------------SELKNQEKKL-----------------------------------------------------EE 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1440 SDKALTSWKQKLDETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEK 1519
Cdd:TIGR04523 326 IQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1520 AKKLIEQEKTEVQVRLEETEGALERNESKILRFQLELSeakaELERKLSEKEEEAERLREKHQQamgsLQSNLDleassr 1599
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK----DLTNQDSVKELIIKNLDNTRES----LETQLK------ 471
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1600 iEATRLRKKMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEEL 1679
Cdd:TIGR04523 472 -VLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1680 rtlqeQTERGRKLAEKELLEATERINLFHTQNTSLLSQKKKLEADVAQVQKEAGEMLQACQKAEEKAKKTAAEAANMSEE 1759
Cdd:TIGR04523 551 -----DFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
730 740 750
....*....|....*....|....*....|..
gi 261245016 1760 LKKEQDTNAHLERMRKNMEQTIKDLQKRLDEA 1791
Cdd:TIGR04523 626 NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEI 657
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
838-1249 |
1.81e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 838 EEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKSKVELEVKIKELS--- 914
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatl 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 915 RQVEEEEEINSELTARGRkledeCSELKKEIYDLEAILAKSEKgkcaaEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETq 994
Cdd:PRK02224 436 RTARERVEEAEALLEAGK-----CPECGQPVEGSPHVETIEED-----RERVEELEAELEDLEEEVEEVEERLERAEDL- 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 995 qqtqeqlhIEEEKLSNMSKANLKLAQQ-IDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAENLESSRQKLAEqlrk 1073
Cdd:PRK02224 505 --------VEAEDRIERLEERREDLEElIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE---- 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1074 kefEMGQMNSKVENEKNQVSQLQKmVKELQTHILNLKEELESERTIRAKVErEKGDLVQD-LEDLNERLEEAGGT-SLAQ 1151
Cdd:PRK02224 573 ---EVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALA-ELNDERRErLAEKRERKRELEAEfDEAR 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1152 MEITKQQEARFQKLHHDMEETTRHFEATSASLKKR------HAENLAELEGQVEHLQQVRLVLE---QDKSDLQLQVDDL 1222
Cdd:PRK02224 648 IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigavenELEELEELRERREALENRVEALEalyDEAEELESMYGDL 727
|
410 420
....*....|....*....|....*..
gi 261245016 1223 lnRVDQMARakaNAEKLcglyERRLNE 1249
Cdd:PRK02224 728 --RAELRQR---NVETL----ERMLNE 745
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1006-1576 |
1.88e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1006 EKLSNMSKANLKLAQQIDVLEgDLERERKARMKCEREKRKLQDELKMNQegAENLESSRQKLAEQLRKKEFEMGQMNSKV 1085
Cdd:COG4913 235 DDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1086 ENEKNQVSQLQKMVKELQTHILN--------LKEELESERTIRAKVEREKGDLVQDLEDLNERLEEAGGTSLAQMEITKQ 1157
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1158 QEARFQKLHHDMEETTRHFEATSASLKKRHAE---NLAELEGQV----EHLQQVRLVLEQ----DKSDLQ-----LQVDD 1221
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELREleaEIASLERRKsnipARLLALRDALAEalglDEAELPfvgelIEVRP 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1222 LlNRVDQMArakanAEKLCG---LY----ERRLNEANTKLDEvTQLAHDLTTQK-------------------TKLQSES 1275
Cdd:COG4913 472 E-EERWRGA-----IERVLGgfaLTllvpPEHYAAALRWVNR-LHLRGRLVYERvrtglpdperprldpdslaGKLDFKP 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1276 GEFF----KRLEEKEALI-----SQLSRE----------KSNFTR---------------------QVEELRAQLEEESR 1315
Cdd:COG4913 545 HPFRawleAELGRRFDYVcvdspEELRRHpraitragqvKGNGTRhekddrrrirsryvlgfdnraKLAALEAELAELEE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1316 SQSALSHALQSAKHDYDLLREQyeeeqevkAELHRALskgnkETVQWRAKyehdamqrteDLEEAKKKLAiRLQEAAEAM 1395
Cdd:COG4913 625 ELAEAEERLEALEAELDALQER--------REALQRL-----AEYSWDEI----------DVASAEREIA-ELEAELERL 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1396 EVSNAKNASLERARHRLQLELGDALSDLGKARSVAAALGQKqqhsdkaLTSWKQKLDETQELLQASQKETRALSSEVLT- 1474
Cdd:COG4913 681 DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAAEDLARLELRALLEe 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1475 -FRQACEESTEAQ--ETLKRQNQDLQEQICSLTNQVREGIknlaevEKAKKLIEQEKTEVQVRLE------------ETE 1539
Cdd:COG4913 754 rFAAALGDAVERElrENLEERIDALRARLNRAEEELERAM------RAFNREWPAETADLDADLEslpeylalldrlEED 827
|
650 660 670
....*....|....*....|....*....|....*...
gi 261245016 1540 GaLERNESKILRFQLELSEA-KAELERKLSEKEEEAER 1576
Cdd:COG4913 828 G-LPEYEERFKELLNENSIEfVADLLSKLRRAIREIKE 864
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1513-1727 |
2.25e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1513 NLAEVEKAKKLIEQEKTEVQVRLEETEGALE--RNESKILRFQLE---LSEAKAELERKLSEKEEEAERLREKHQQAMGS 1587
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEaklLLQQLSELESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1588 LQSNLDleASSRIEATRLRKKMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNK-DLKEQVALAE 1666
Cdd:COG3206 249 LGSGPD--ALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQ 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261245016 1667 QRTVLLQSELEELRTLQEQTERgrklAEKELLEATERINLFHTQNTSLLSQKKKLEADVAQ 1727
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1448-1924 |
2.30e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1448 KQKLDETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLtNQVREGIKNLAEVEKAKKLIEQE 1527
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1528 KTEVQVRLEETEGALERNESKILRFQlELSEAKAELERKLSEKEEEAERLREKHQQAMGSLQSNLDLEASSRIEATRLRK 1607
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELE-EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1608 KMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLhqqlDDSIYQNKDLKEQVALA------EQRTVLLQSELEEL-- 1679
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL----KKAIEELKKAKGKCPVCgrelteEHRKELLEEYTAELkr 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1680 --RTLQEQTERGRKLAEKE-----LLEATERINLFHTQNTSLLSQKKKLEA-DVAQVQKEAGEMlqacQKAEEKAKKTAA 1751
Cdd:PRK03918 464 ieKELKEIEEKERKLRKELrelekVLKKESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEY----EKLKEKLIKLKG 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1752 EAANMSEELKKEQDtnahLERMRKNMEQTIKDLQKRLDEAEQTAVLGSKKQIQKLESRVRDLEgELESEVRRSAEAQREA 1831
Cdd:PRK03918 540 EIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKEL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1832 RRLERGIKELTYQAEEDKKNLSRMQALSDKLQLKVQSYKQQ--VEAAEAQANQYLSK---YKKQQHELNEAKERAEAAES 1906
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEELREEYLELsreLAGLRAELEELEKRREEIKK 694
|
490
....*....|....*...
gi 261245016 1907 QVNKLRAKAKELEKKVRE 1924
Cdd:PRK03918 695 TLEKLKEELEEREKAKKE 712
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1242-1738 |
3.06e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 55.52 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1242 LYERRLNEANTKLDEVTQLAhdlttqKTKLQSESGeFFKRLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSALS 1321
Cdd:pfam05557 59 LLEKREAEAEEALREQAELN------RLKKKYLEA-LNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1322 HALQSAKHDYDLLREQYEEEQEVKAELHRALSKGN------KETVQWRAKYEHDAmqrtEDLEEAKKKLA--IRLQEAAE 1393
Cdd:pfam05557 132 SELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAeaeqriKELEFEIQSQEQDS----EIVKNSKSELAriPELEKELE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1394 AMEVSNAKNASLERARHRLQLELGDALSDLG---KARSVAAALGQKQQHSDKALTSWKqKLDETQELlqaSQKETRALSS 1470
Cdd:pfam05557 208 RLREHNKHLNENIENKLLLKEEVEDLKRKLEreeKYREEAATLELEKEKLEQELQSWV-KLAQDTGL---NLRSPEDLSR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1471 EVltfrqaceesteaqETLKRQNQDLQEQICSLTNQVRegiknlaEVEKAKKLIEQEKTEVQVRLEETEGALERNESKIL 1550
Cdd:pfam05557 284 RI--------------EQLQQREIVLKEENSSLTSSAR-------QLEKARRELEQELAQYLKKIEDLNKKLKRHKALVR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1551 RFQLELSEAKAElerklsekeeeaerlREKHQQAMGSLQSNLDLEASSRIEATRLRkKMEGDLKEMEIQLCAANRQVSQM 1630
Cdd:pfam05557 343 RLQRRVLLLTKE---------------RDGYRAILESYDKELTMSNYSPQLLERIE-EAEDMTQKMQAHNEEMEAQLSVA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1631 TRALGQLQGQMKDLHQQLdDSIYQNKDLKEQVALAEQRTVLLQsELEELRTLQEQTERGRKLAEKElLEATERINLFHTQ 1710
Cdd:pfam05557 407 EEELGGYKQQAQTLEREL-QALRQQESLADPSYSKEEVDSLRR-KLETLELERQRLREQKNELEME-LERRCLQGDYDPK 483
|
490 500
....*....|....*....|....*...
gi 261245016 1711 NTSLLSQKKKLEADVAQVQKEAGEMLQA 1738
Cdd:pfam05557 484 KTKVLHLSMNPAAEAYQQRKNQLEKLQA 511
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1438-1592 |
3.50e-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: 53.39 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1438 QHSDKALTSWKQKLDETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQVREGIKN---- 1513
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1514 --LAEVEKAKKLI---EQEKTEVQVRLEETEGALERNESKILRFQLELSEAKAELERKLSEKEEEAERLREKHQQAMGSL 1588
Cdd:COG1579 93 alQKEIESLKRRIsdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
....
gi 261245016 1589 QSNL 1592
Cdd:COG1579 173 PPEL 176
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1491-1921 |
4.52e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1491 RQNQDLQEQICSLTNQVREgiknLAEVEKAKKLIEQEKTEVQVRLEETEGALERNEskILRFQLELSEAKAELERKLSEK 1570
Cdd:COG4717 71 KELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLE--KLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1571 EEEAERLREKHQQamgslqsnldleassRIEATRLRKKMEGDLKEMEIQLCAANRQVSQMTRAlgqlqgQMKDLHQQLDD 1650
Cdd:COG4717 145 PERLEELEERLEE---------------LRELEEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1651 SIYQNKDLKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATERINLFHTQNTSLLSQKKKLEADVAQVQK 1730
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1731 EAGEMLQACQKAEEKAKKTAAEAANMSEELKK--EQDTNAHLERMRKNMEQTIKDLQKRLDEAEQTAVLGSKKQIQKLES 1808
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1809 RVRDLEGEL-----------ESEVRRSAEAQREARRLERGIKELTYQAEEDKKNLSRMQALSDK--LQLKVQSYKQQVEA 1875
Cdd:COG4717 364 QLEELEQEIaallaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEE 443
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 261245016 1876 AEAQANQYLSKYKKQQHELNEAKERAE--AAESQVNKLRAKAKELEKK 1921
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
873-1130 |
5.32e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 873 QEKNDLRLQLQAEQETLANSEEQCESLIKSKVELEVKIKELSRQVeeeeeinseltargRKLEDECSELKKEIYDLEAIL 952
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI--------------RALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 953 AKSEKgkcaaehkvrNLTEEVHSLNEEVSKLSRVVKDAQETQQQTQEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERE 1032
Cdd:COG4942 93 AELRA----------ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1033 RKARMKCEREKRKLQDELKmnqegaeNLESSRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEE 1112
Cdd:COG4942 163 AALRAELEAERAELEALLA-------ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250 260
....*....|....*....|
gi 261245016 1113 LE--SERTIRAKVEREKGDL 1130
Cdd:COG4942 236 AAaaAERTPAAGFAALKGKL 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1062-1274 |
5.65e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1062 SSRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNERL 1141
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1142 EEAGGtSLAQMEITKQQEARFQKLH-----HDMEETTRHFEATSASLKKRhAENLAELEGQVEHLQQVRLVLEQDKSDLQ 1216
Cdd:COG4942 100 EAQKE-ELAELLRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPAR-REQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 261245016 1217 LQVDDLLNRVDQMARAKANAEKLCGLYERRLNEANTKLDEVTQLAHDLTTQKTKLQSE 1274
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1448-1805 |
5.88e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.74 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1448 KQKLDETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKliEQE 1527
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQ--EER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1528 KTEV-QVRLEETEGALERNEsKILRFQLELSE----AKAELERKLSEKEEEAERLREKHQQAMGSLQSNLDLEASSRIEA 1602
Cdd:pfam17380 359 KRELeRIRQEEIAMEISRMR-ELERLQMERQQknerVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1603 TRLRKKMEgdlKEMEiqlcaaNRQVSQMTRalgqlQGQMKDLHQQLDD----SIYQNKDLKEQVALAEQRTVLLQSELEE 1678
Cdd:pfam17380 438 RRLEEERA---REME------RVRLEEQER-----QQQVERLRQQEEErkrkKLELEKEKRDRKRAEEQRRKILEKELEE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1679 LRTLQEQTERGRKLAEKELLEaterinlfhTQNTSLLSQKKKLEADVAQVQKEAGEMLQacqkaeekakktaaeaanMSE 1758
Cdd:pfam17380 504 RKQAMIEEERKRKLLEKEMEE---------RQKAIYEEERRREAEEERRKQQEMEERRR------------------IQE 556
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 261245016 1759 ELKKEQDTNAHLERMRKNME--QTIKDLQKRLDEAEQTAVLGSKKQIQK 1805
Cdd:pfam17380 557 QMRKATEERSRLEAMEREREmmRQIVESEKARAEYEATTPITTIKPIYR 605
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
838-1136 |
6.21e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 54.73 E-value: 6.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 838 EEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKSKVELEVKIKELSRQV 917
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDEL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 918 EEeeeINSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQQT 997
Cdd:pfam05483 551 ES---VREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 998 QEQLHIEEEKLSNM----SKANLKLAQQIDVLEGDLE----RERKARMKCEREKRKLQDELKMNQEGAEN---------- 1059
Cdd:pfam05483 628 NKQLNAYEIKVNKLelelASAKQKFEEIIDNYQKEIEdkkiSEEKLLEEVEKAKAIADEAVKLQKEIDKRcqhkiaemva 707
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261245016 1060 -LESSRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLED 1136
Cdd:pfam05483 708 lMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1214-1863 |
6.40e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.84 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1214 DLQLQVDDLLNRVDqmARAKANAEKLCGLYErrlnEANTKLDEVTQlahDLTTQKTKLQSESGEFfKRLEEKEALISQLS 1293
Cdd:pfam12128 269 SDETLIASRQEERQ--ETSAELNQLLRTLDD----QWKEKRDELNG---ELSAADAAVAKDRSEL-EALEDQHGAFLDAD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1294 REKSNF-TRQVEELRAQLEEESRSQSALSHALQSAKHDYDLLReqyeeeQEVKAELHRALSKGNKETvqwrakyehDAMQ 1372
Cdd:pfam12128 339 IETAAAdQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRR------SKIKEQNNRDIAGIKDKL---------AKIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1373 RTEDLEEAKKKLAIRLQEAaEAMEVSNAKNASLERARHRLQLELGDALSDLGKARSVAAALGQKQQHSDKaltswkqkLD 1452
Cdd:pfam12128 404 EARDRQLAVAEDDLQALES-ELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDER--------IE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1453 ETQELLQASQKETRALSSEVLTFRQACEESTEA-----QETLKRQN--QDLQEQICSLTNQVREGIKNLAEV--EKAKKL 1523
Cdd:pfam12128 475 RAREEQEAANAEVERLQSELRQARKRRDQASEAlrqasRRLEERQSalDELELQLFPQAGTLLHFLRKEAPDweQSIGKV 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1524 IEQE---KTEVQVRLEETEGALERNeskilrfqleLSEAKAELER-KLSEKEEEAERLREKHQQAMGSLQSNLDLEASSR 1599
Cdd:pfam12128 555 ISPEllhRTDLDPEVWDGSVGGELN----------LYGVKLDLKRiDVPEWAASEEELRERLDKAEEALQSAREKQAAAE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1600 IEATRLRKKMEGDLKEMEIqlcaANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNKDLKEQ--VALAEQRTVL---LQS 1674
Cdd:pfam12128 625 EQLVQANGELEKASREETF----ARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANErlNSLEAQLKQLdkkHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1675 ELEELRTLQEQTERGRKLAEKELLEATErinlfhtqntsllSQKKKLEADVAQVQKEAGEMLQACQKAeekakktaaeaa 1754
Cdd:pfam12128 701 WLEEQKEQKREARTEKQAYWQVVEGALD-------------AQLALLKAAIAARRSGAKAELKALETW------------ 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1755 nMSEELKK---EQDTNAHLERMRKNMEQTIKDLQKRLDEAEQTAVLGSKK---QIQKLESRVRDLEgelesevrrsaeaq 1828
Cdd:pfam12128 756 -YKRDLASlgvDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETwlqRRPRLATQLSNIE-------------- 820
|
650 660 670
....*....|....*....|....*....|....*
gi 261245016 1829 REARRLERGIKELTYQAEEDKKNLSRMQALSDKLQ 1863
Cdd:pfam12128 821 RAISELQQQLARLIADTKLRRAKLEMERKASEKQQ 855
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
832-1419 |
8.06e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.41 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 832 KSVGAGEEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESL------IKSKVE 905
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLqaqlsdMKKKLE 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 906 --------LEVKIKELSRQVEEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRN----LTEE- 972
Cdd:pfam01576 535 edagtleaLEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKfdqmLAEEk 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 973 --VHSLNEEVSKLSRVVKDAQETQQQTQEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERERKARMKCEREKRKLQDEL 1050
Cdd:pfam01576 615 aiSARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQV 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1051 KMNQEGAENLESSRQKLAEQLRKKEFEMGQMNSKVENE--------KNQVSQLQKMVKELQThilnlkeELESERTIRAK 1122
Cdd:pfam01576 695 EEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDlqardeqgEEKRRQLVKQVRELEA-------ELEDERKQRAQ 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1123 VEREKGDLVQDLEDLNERLEEAGGTSLAQMEITKQQEARFQKLHHDMEEtTRHFEATSASLKKRHAENLAELEGQVEHLQ 1202
Cdd:pfam01576 768 AVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEE-ARASRDEILAQSKESEKKLKNLEAELLQLQ 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1203 QVRLVLEQDKSDLQLQVDDLLNRVdqmarAKANAEKLCGLYERRLNEAntkldEVTQLAHDLTTQKTKLQSESGEFFKRL 1282
Cdd:pfam01576 847 EDLAASERARRQAQQERDELADEI-----ASGASGKSALQDEKRRLEA-----RIAQLEEELEEEQSNTELLNDRLRKST 916
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1283 EEKEALISQLSREKS----------NFTRQVEELRAQL-EEESRSQSALSHALQSAKHDYDLLREQYEEEQEVKAELHRA 1351
Cdd:pfam01576 917 LQVEQLTTELAAERStsqksesarqQLERQNKELKAKLqEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKL 996
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261245016 1352 LSKGNKETVQWRAKYEhDAMQRTEDLEEAKKKLAIRLQEAAEAMEVSNAKNASLERARHRLQLELGDA 1419
Cdd:pfam01576 997 VRRTEKKLKEVLLQVE-DERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDA 1063
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1266-1835 |
9.35e-07 |
|
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: 53.99 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1266 TQKTKLQSESGEFFKRLEEKEALISQLS-REKSNFTRQVEELRAQLEEESRSQsALSHALQSAKHDYDLLREQYEE-EQE 1343
Cdd:pfam07111 62 SQQAELISRQLQELRRLEEEVRLLRETSlQQKMRLEAQAMELDALAVAEKAGQ-AEAEGLRAALAGAEMVRKNLEEgSQR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1344 VKAELHRALSKGNKETVQWRAKYEHDAMQRTEDLEEAKKKLAIRLQEAAEAMEVSNAKNASLERARHRLQLELGDALSDL 1423
Cdd:pfam07111 141 ELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1424 GKARSVAAALGQKQQHSdKALTSWKQKLDETQELLQASQKETRAlSSEVLTFR-QACEESTEAQE---TLKRQNQDLQE- 1498
Cdd:pfam07111 221 ESLRKYVGEQVPPEVHS-QTWELERQELLDTMQHLQEDRADLQA-TVELLQVRvQSLTHMLALQEeelTRKIQPSDSLEp 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1499 ----QICSLTNQVREGIKNLAEVEKAKKLIEQEKTE---VQVRLEETEGALERNESKILRFQLELSEAKAELER----KL 1567
Cdd:pfam07111 299 efpkKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKqlrGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERmsakGL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1568 SEKEEEAERLREKHQQAMGSLQSNLDLEASSRIEATRLRKKMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQ 1647
Cdd:pfam07111 379 QMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVAL 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1648 LDDSIYQNKDLKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATERinlFHTQNTSLLSQKKKLEADVAQ 1727
Cdd:pfam07111 459 AQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQQEVGRAREQ---GEAERQQLSEVAQQLEQELQR 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1728 VQKEAGEMLQACQKAEEKAKKTAAEAANMSEELKKEQDTNAH-----LERMRKNMEQTIKDLQKRLDEA--EQTAVLGSK 1800
Cdd:pfam07111 536 AQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQalqekVAEVETRLREQLSDTKRRLNEArrEQAKAVVSL 615
|
570 580 590
....*....|....*....|....*....|....*..
gi 261245016 1801 KQIQKLESRVRDLEGELE--SEVRRSAEAQREARRLE 1835
Cdd:pfam07111 616 RQIQHRATQEKERNQELRrlQDEARKEEGQRLARRVQ 652
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1018-1652 |
9.52e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.07 E-value: 9.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1018 LAQQIDVLEGDLERERKARMKCEREKRKLQDELKMNQEgaENLESSRQKLaeqlrkkefemgqmnskvENEKNQVSQLQK 1097
Cdd:pfam12128 299 WKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLD--ADIETAAADQ------------------EQLPSWQSELEN 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1098 MVKElqthilnLKEELESERTIRAKVEREKG----DLVQDLEDLNERLEEAGGTSLAQM-EITKQQEARFQKLHHDMEET 1172
Cdd:pfam12128 359 LEER-------LKALTGKHQDVTAKYNRRRSkikeQNNRDIAGIKDKLAKIREARDRQLaVAEDDLQALESELREQLEAG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1173 TRHFEATsaslKKRHAENLAELEGQVEHLQQVRLVLEQdksdlQLQVDDLLNRVDQmARAKANAEKLCGLYER-----RL 1247
Cdd:pfam12128 432 KLEFNEE----EYRLKSRLGELKLRLNQATATPELLLQ-----LENFDERIERARE-EQEAANAEVERLQSELrqarkRR 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1248 NEANTKLDE----VTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQ-----LSREKSNFTRQVEELRAQLEEESRSQS 1318
Cdd:pfam12128 502 DQASEALRQasrrLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQsigkvISPELLHRTDLDPEVWDGSVGGELNLY 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1319 ALSHALQSAKHDydllrEQYEEEQEVKAELHRAlskgnKETVQwrakyehDAMQRTEDLEEAKKKLAIRLQEAAEAMEVS 1398
Cdd:pfam12128 582 GVKLDLKRIDVP-----EWAASEEELRERLDKA-----EEALQ-------SAREKQAAAEEQLVQANGELEKASREETFA 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1399 nakNASLERARHRLQLELGDALSD-LGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEVLTFRQ 1477
Cdd:pfam12128 645 ---RTALKNARLDLRRLFDEKQSEkDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQ 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1478 ACEESTEAQETLKRQNQD-LQEQICSLTNQVREGIKN-LAEVEKAKKLIEQEKTEVQvRLEETEGALERNESKILRFQL- 1554
Cdd:pfam12128 722 VVEGALDAQLALLKAAIAaRRSGAKAELKALETWYKRdLASLGVDPDVIAKLKREIR-TLERKIERIAVRRQEVLRYFDw 800
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1555 ----------ELSEAKAELERKLSEKEEEAERLREKHQQAMGSLQSNLDLEASSRIEA----TRLRKKMEG--------D 1612
Cdd:pfam12128 801 yqetwlqrrpRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLsenlRGLRCEMSKlatlkedaN 880
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 261245016 1613 LKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSI 1652
Cdd:pfam12128 881 SEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVI 920
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1104-1700 |
1.02e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1104 THILnlkEELESERTIRAKVErekgdLVQDLEDLNERLEEAggtsLAQMEITKQQEARFQKLHHDMEETTRHFEATSASL 1183
Cdd:COG4913 215 EYML---EEPDTFEAADALVE-----HFDDLERAHEALEDA----REQIELLEPIRELAERYAAARERLAELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1184 KKRHAENLAELEGQVEHLQQVRLVLEQDKSDLQLQVDDLLNRVDQmarakanaeklcgLYERRLNEANTKLDEVTQLAHD 1263
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE-------------LEAQIRGNGGDRLEQLEREIER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1264 LTTQKTKLQSESGEFFKRLEekeALISQLSREKSNFTRQVEELRAQLEEESRSQSALSHALQSAKhdyDLLREQYEEEQE 1343
Cdd:COG4913 350 LERELEERERRRARLEALLA---ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE---AALRDLRRELRE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1344 VKAELhRALSKGnketvqwRAKYEHDAMQRTEDLEEAKKKLAIRLQEAAEAMEVSNA----KNAsLERARHRLQLELgda 1419
Cdd:COG4913 424 LEAEI-ASLERR-------KSNIPARLLALRDALAEALGLDEAELPFVGELIEVRPEeerwRGA-IERVLGGFALTL--- 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1420 LSDLGKARSVAAALgqKQQHSDKALTSwkQKLDETQELLQASQKETRALSSEVLTfrqaceESTEAQETLKRQNQDLQEQ 1499
Cdd:COG4913 492 LVPPEHYAAALRWV--NRLHLRGRLVY--ERVRTGLPDPERPRLDPDSLAGKLDF------KPHPFRAWLEAELGRRFDY 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1500 ICSltnqvrEGIKNLAEVEKA---KKLIEQEKT--EVQVRLEETEGAL--ERNESKILRFQLELseakAELERKLSEKEE 1572
Cdd:COG4913 562 VCV------DSPEELRRHPRAitrAGQVKGNGTrhEKDDRRRIRSRYVlgFDNRAKLAALEAEL----AELEEELAEAEE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1573 EAERLREKHQQAMGSLQSNLDLEASSRIEAtrlrkkmegDLKEMEIQLCAANRQVSQMTRA---LGQLQGQMKDLHQQLD 1649
Cdd:COG4913 632 RLEALEAELDALQERREALQRLAEYSWDEI---------DVASAEREIAELEAELERLDASsddLAALEEQLEELEAELE 702
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 261245016 1650 DSIYQNKDLKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEA 1700
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1640-1880 |
1.04e-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: 53.23 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1640 QMKDLHQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATERINlfhtqntSLLSQKK 1719
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1720 KLEADVAQVQKEAGEMLQACQKAEEKAKKtaaeaanmseELKKEQDTNAHLERMRKNMEQTIKDLQKRLDEAeqtavlgs 1799
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPL----------ALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1800 KKQIQKLESRVRDLEGELESEVRRSAEAQREARRLERGIKELTYQAEEDKKNLSRMQALSDKLQLKVQSYKQQVEAAEAQ 1879
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
.
gi 261245016 1880 A 1880
Cdd:COG4942 236 A 236
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1215-1582 |
1.35e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 52.76 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1215 LQLQVDDLLNRVDQMARA--KANAEKLCglYERRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQL 1292
Cdd:pfam19220 25 LKADFSQLIEPIEAILRElpQAKSRLLE--LEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1293 SREKSNFTRQVEELRAQLEEESRSQSALSHALQSAKHDYDLLREQYEEEQEVKAELHRALSkgnketvqwrakyehDAMQ 1372
Cdd:pfam19220 103 EAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELA---------------TARE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1373 RTEDLEEAKKKLAIRLQEAAEAMEVSNAKNASLERARHRLQLELGDALSDL-----GKARSVAAALGQKQQHSdKALTSW 1447
Cdd:pfam19220 168 RLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLaaeqaERERAEAQLEEAVEAHR-AERASL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1448 KQKLDE-------TQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQvregiknLAEVEKA 1520
Cdd:pfam19220 247 RMKLEAltaraaaTEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQ-------FQEMQRA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261245016 1521 KKLIEQEKTEVQVRLEETEGALERNESKILRFQLELSEAKAELERKLSEKEEEAERLREKHQ 1582
Cdd:pfam19220 320 RAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRLKEELQ 381
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1369-1685 |
1.45e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.76 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1369 DAMQRTEDLEEAKKKLAIRLQEAAE---AMEVSNAKNASLERARHRLQLELGDALSDLGKARSVAAALgQKQQHSDKALT 1445
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE-TRETLSTLSLR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1446 SWKQKLDETQELLQASQKETRALSSEVLTFRQACEestEAQETLKRQNQDLQeQICSLTNQVREGIKNLAEVEKAKKLIE 1525
Cdd:PRK11281 125 QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPE---RAQAALYANSQRLQ-QIRNLLKGGKVGGKALRPSQRVLLQAE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1526 QEKTEVQVRLEETEgaLERNESKILRFQL---ELSEAKAELERKLSEKEEE--AERLREKHQQAmgslQSNLDLEASSRI 1600
Cdd:PRK11281 201 QALLNAQNDLQRKS--LEGNTQLQDLLQKqrdYLTARIQRLEHQLQLLQEAinSKRLTLSEKTV----QEAQSQDEAARI 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1601 EATRLRKkmegdlKEMEIqlcaaNRQVSQ----MTRALGQLQGQMKDLHQQLDDSIYQNKDLKEQVAlAEQRTVLLQsel 1676
Cdd:PRK11281 275 QANPLVA------QELEI-----NLQLSQrllkATEKLNTLTQQNLRVKNWLDRLTQSERNIKEQIS-VLKGSLLLS--- 339
|
....*....
gi 261245016 1677 eelRTLQEQ 1685
Cdd:PRK11281 340 ---RILYQQ 345
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1455-1735 |
1.74e-06 |
|
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: 52.98 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1455 QELLQASQKETRALSSEVLTFRQACEESTE----AQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTE 1530
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKErykrDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1531 VQvrlEETEGALERNESKILRFqLELSEAKAELERKLSEKEEEAERLREKHQQAMGSLQsnldleassriEATRLRKKME 1610
Cdd:pfam07888 113 LS---EEKDALLAQRAAHEARI-RELEEDIKTLTQRVLERETELERMKERAKKAGAQRK-----------EEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1611 GDLKEMEIQLCAANRQVSQMTRALGQLQGQMkdlhQQLDDSIYQnkdLKEQVALAEQRTVLLQSELEELRTLQeqtergr 1690
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQV----LQLQDTITT---LTQKLTTAHRKEAENEALLEELRSLQ------- 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 261245016 1691 klaekELLEATER-INLFHTQNTSLLSQKKKLEADVAQVQKEAGEM 1735
Cdd:pfam07888 244 -----ERLNASERkVEGLGEELSSMAAQRDRTQAELHQARLQAAQL 284
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1758-1858 |
2.12e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.94 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1758 EELKKEQDTNAHLERMRKNMEQTIKDLQKRLDEAE------QTAVLGSKKQIQKLESRVRDLEGELESEVRRSAEA---Q 1828
Cdd:COG2433 392 EEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEaeveelEAELEEKDERIERLERELSEARSEERREIRKDREIsrlD 471
|
90 100 110
....*....|....*....|....*....|
gi 261245016 1829 REARRLERGIKELTYQAEEDKKNLSRMQAL 1858
Cdd:COG2433 472 REIERLERELEEERERIEELKRKLERLKEL 501
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1514-1691 |
2.17e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.08 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1514 LAEVEKAKKLIEQEKTEVQVRLEETEGALERNESKILRFQLELSEAKAELeRKLSEKEEEAERLREKHQQAMGSLQSNLD 1593
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-KRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1594 LEA-SSRIEATRLRK-KMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNKdlKEQVALAEQRTVL 1671
Cdd:COG1579 91 YEAlQKEIESLKRRIsDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE--AELEELEAEREEL 168
|
170 180
....*....|....*....|
gi 261245016 1672 LQSELEELRTLQEQTERGRK 1691
Cdd:COG1579 169 AAKIPPELLALYERIRKRKN 188
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1190-1795 |
2.38e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1190 NLAELEGQVEHLQQVRLVLEQDKSDLQlqvdDLLNRVDQMARAKANAEKLCGLYERRLNEANTKLDEVTQLAHDLTTQKT 1269
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLE----KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1270 KLQSESGEFF---KRLEEKEALISQLSREKSNFTRQVEELRAQLEEeSRSQSALSHALQSAKHDYDLLREQYEEEQEVKA 1346
Cdd:PRK03918 232 ELEELKEEIEeleKELESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1347 ELHRALSK------GNKETVQWRAKYEHDAMQRTEDLEEAKKKLAiRLQEAAEAMEVSNAKNASLERARHRLQ-LELGDA 1419
Cdd:PRK03918 311 EIEKRLSRleeeinGIEERIKELEEKEERLEELKKKLKELEKRLE-ELEERHELYEEAKAKKEELERLKKRLTgLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1420 LSDLGKARsvaaalgqkqqhsdkaltswKQKLDETQELLQASQKeTRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQ 1499
Cdd:PRK03918 390 EKELEELE--------------------KAKEEIEEEISKITAR-IGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1500 icSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALERnESKILRFQL---ELSEAKAELER----KLSEKEE 1572
Cdd:PRK03918 449 --HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKElaeQLKELEEKLKKynleELEKKAE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1573 EAERLREKHQQAMGSLqSNLDLEASSRIEATRLRKKMEGDLKEMEIQLCAANRQ--------VSQMTRALGQLQG----- 1639
Cdd:PRK03918 526 EYEKLKEKLIKLKGEI-KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEleelgfesVEELEERLKELEPfyney 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1640 -QMKDLHQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEELRtlQEQTERGRKLAEKELLEATERINLFHTQNTSLLSQK 1718
Cdd:PRK03918 605 lELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELR--KELEELEKKYSEEEYEELREEYLELSRELAGLRAEL 682
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261245016 1719 KKLEADVAQVQKEAGEMlqacqkaeekakktaaeaANMSEELKKEQDTNAHLERMRKNMEQTIKDLQKRLDEAEQTA 1795
Cdd:PRK03918 683 EELEKRREEIKKTLEKL------------------KEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERA 741
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
874-1500 |
2.58e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.72 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 874 EKNDLRLQLQAEQETLANSEEQCESLIKSKVELEVKIKELSRQVEeeeeinsELTARGRKLEDECSELKKEIYDLEAILA 953
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIK-------ILEQQIKDLNDKLKKNKDKINKLNSDLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 954 KSekgkcAAEHKVRNltEEVHSLNEEVSKLSRVVKDAQETQQQTQEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLErer 1033
Cdd:TIGR04523 107 KI-----NSEIKNDK--EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELN--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1034 karmKCEREKRKLQDELKmnqeGAENLESSRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEEL 1113
Cdd:TIGR04523 177 ----LLEKEKLNIQKNID----KIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1114 EsertiraKVEREKGDLVQDLEDLNERLEEAGGTSLAQMEITKQQEARFQKLHHDMEEttrhfeatsasLKKRHAENL-A 1192
Cdd:TIGR04523 249 S-------NTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD-----------LNNQKEQDWnK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1193 ELEGQVEHLQQVRLVLEQDKSDLQLQVDDLLNRVDQMARAKANAEKLCGLYERRLNEANTKL-------DEVTQLAHDLT 1265
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIeklkkenQSYKQEIKNLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1266 TQKTKLQSESGEFFKRLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSALSHALQSAKHDYDLLrEQYEEEQEVK 1345
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL-DNTRESLETQ 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1346 AELHRALSKGNKETVQWRAKYEHDAMQRTEDLEEAKKKLAIRLQEAAEAMEVSNAKNASLERARHRLQLELGDALSDLGK 1425
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1426 ARSV--AAALGQKQQHSDKALTSWKQ-------KLDETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDL 1496
Cdd:TIGR04523 550 DDFElkKENLEKEIDEKNKEIEELKQtqkslkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKL 629
|
....
gi 261245016 1497 QEQI 1500
Cdd:TIGR04523 630 SSII 633
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1443-1668 |
2.82e-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: 51.69 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1443 ALTSWKQKLDETQELLQASQKETRALSSEVltfrqacEESTEAQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKK 1522
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKEL-------AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1523 LIEQEKTEVQVRLEETEGALerneSKILRFQLELSEAKAELERKLSEKEEEAER-------LREKHQQAMGSLQSNLDLE 1595
Cdd:COG4942 87 ELEKEIAELRAELEAQKEEL----AELLRALYRLGRQPPLALLLSPEDFLDAVRrlqylkyLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261245016 1596 ASSRIEATRLRKKMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNKDLKEQVALAEQR 1668
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
881-1617 |
3.01e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 881 QLQAEQETLANSEEQCESLIKSKVELEVKIKELSRQVEEEEEINSELTARGRKLEDECSELKKeiydleaILAKSEKGKC 960
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKE-------TCARSAEKTK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 961 AAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQQTQEQLHieeeklsnmskanlklaqqidvlegdlererkarMKCE 1040
Cdd:pfam05483 173 KYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMH----------------------------------FKLK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1041 REKRKLQDELKMNQEGAENLESSRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKeLQTHilNLKEELESERTIR 1120
Cdd:pfam05483 219 EDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTK-LQDE--NLKELIEKKDHLT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1121 AKVEREKGDLVQDL---EDLNERLEEAGGTSLAQMEITKQQEARFQKLHHDMEETTRHFEATSASLKKRHAENLAELEGQ 1197
Cdd:pfam05483 296 KELEDIKMSLQRSMstqKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1198 VEHLQQVRLVLEQDKSDLQlqvddllnrvdQMARAKANAEKLCGLYERRLNEANTKLDE---VTQLAHDLTTQKTKLQSE 1274
Cdd:pfam05483 376 EDQLKIITMELQKKSSELE-----------EMTKFKNNKEVELEELKKILAEDEKLLDEkkqFEKIAEELKGKEQELIFL 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1275 SGEFFKRLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSALShalqsaKHDYDLLREQYEEEQEVKAELHRAlsK 1354
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELT------AHCDKLLLENKELTQEASDMTLEL--K 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1355 GNKETVQWRAKYEHDAMQRTEDLEEAKKKLAIRLQEAAEAM-----EVSNAKNASLERARhRLQLELGDALSDLGKARSV 1429
Cdd:pfam05483 517 KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFiqkgdEVKCKLDKSEENAR-SIEYEVLKKEKQMKILENK 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1430 AAALGQKQQHSDKALTSWKQkldETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQIcsLTNQVRE 1509
Cdd:pfam05483 596 CNNLKKQIENKNKNIEELHQ---ENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEI--EDKKISE 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1510 GiKNLAEVEKAKKLIEqEKTEVQVRLEetegalERNESKILRFQLELSEAKAELERKLSEKEEEAERLREKHQQaMGSLQ 1589
Cdd:pfam05483 671 E-KLLEEVEKAKAIAD-EAVKLQKEID------KRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE-QSSAK 741
|
730 740
....*....|....*....|....*....
gi 261245016 1590 SNLDLEASS-RIEATRLRKKMEGDLKEME 1617
Cdd:pfam05483 742 AALEIELSNiKAELLSLKKQLEIEKEEKE 770
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1487-1924 |
3.22e-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: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1487 ETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALERN---ESKILRFQLELSEAKAEL 1563
Cdd:TIGR04523 155 EKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNkslESQISELKKQNNQLKDNI 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1564 ERKLSEKEEEAERLREKHQQAMGSLQSNldleassrieatrlrKKMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQMKD 1643
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQ---------------NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1644 LHQQLDDSIyqNKDLKEQvalaeqrtvlLQSELEELRTLQEQtergrklaekeLLEATERINLFHTQNTSLLSQKKKLEA 1723
Cdd:TIGR04523 300 LNNQKEQDW--NKELKSE----------LKNQEKKLEEIQNQ-----------ISQNNKIISQLNEQISQLKKELTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1724 DVAQVQKEAGEMLQacqkaeekakktaaeaanmseELKKEQDTNAHLERMRKNMEQTIKDLQKRLDEAEQTAvlgskkqi 1803
Cdd:TIGR04523 357 ENSEKQRELEEKQN---------------------EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN-------- 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1804 QKLESRVRDLEGELESevrrsaeaqrearrLERGIKELTYQAEEDKKNLSRMQALSDKLQLKVQSYKQQVEAAEAQANQY 1883
Cdd:TIGR04523 408 QQKDEQIKKLQQEKEL--------------LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVL 473
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 261245016 1884 LSKYKKQQHELNEAKERAEAAESQVNKLRAKAKELEKKVRE 1924
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD 514
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1531-1737 |
3.88e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1531 VQVRLEETEGALERneskilrfqleLSEAKAELERKLSEKEEEAERLREKHQQAMGSLQSNLDLEASSRIEAtrlrkkme 1610
Cdd:COG3206 166 LELRREEARKALEF-----------LEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELES-------- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1611 gDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLhqqLDDSIYQNkdLKEQVA-----LAEQRTVL---------LQSEL 1676
Cdd:COG3206 227 -QLAEARAELAEAEARLAALRAQLGSGPDALPEL---LQSPVIQQ--LRAQLAeleaeLAELSARYtpnhpdviaLRAQI 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261245016 1677 EELRT-LQEQTERGRKLAEKELLEATERINlfhtqntSLLSQKKKLEADVAQVQKEAGEMLQ 1737
Cdd:COG3206 301 AALRAqLQQEAQRILASLEAELEALQAREA-------SLQAQLAQLEARLAELPELEAELRR 355
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
843-1298 |
4.23e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 51.75 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 843 LKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLaNSEEQCESLIKSKVElevkikELSRQVEEEEE 922
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESL-TAKEQRAAILQTEVD------ALRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 923 INSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQQTQEQLH 1002
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1003 IEEEKLSNMSKANLKLAQQIDVLEGDLERERKARMKCEREKRK----LQDELKMNQEGAENLESSRQKLAEQLRKKEFEM 1078
Cdd:pfam10174 440 TLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEkvsaLQPELTEKESSLIDLKEHASSLASSGLKKDSKL 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1079 GQMNSKVENEKNQVSQLQKMVKELQthilnlkeelESERTIRAKVEREkgDLVQDLEDLNERLEEAGGTSLAQ----MEI 1154
Cdd:pfam10174 520 KSLEIAVEQKKEECSKLENQLKKAH----------NAEEAVRTNPEIN--DRIRLLEQEVARYKEESGKAQAEverlLGI 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1155 TKQQEARfqklHHDMEETTRHFEatsaSLKKRHAENLAELEGQVEHLQQvrlvleQDKSDLQLQVDDLLNRVDQMAR--A 1232
Cdd:pfam10174 588 LREVENE----KNDKDKKIAELE----SLTLRQMKEQNKKVANIKHGQQ------EMKKKGAQLLEEARRREDNLADnsQ 653
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261245016 1233 KANAEKLCGLYER---RLNEANTKLDEVTQLAHDLTTQKTKLQSESGeffKRLEE-----KEALISQLSREKSN 1298
Cdd:pfam10174 654 QLQLEELMGALEKtrqELDATKARLSSTQQSLAEKDGHLTNLRAERR---KQLEEilemkQEALLAAISEKDAN 724
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1060-1459 |
5.44e-06 |
|
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: 51.05 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1060 LESSRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVEREKgdlvQDLEDLNE 1139
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKY----KELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1140 RLEEAGGTSLAQMEitkQQEARFQKLHHDmeettrhfeatSASLKKRHAENLAELE---GQVEHLQQVRLVLEQDKSDLQ 1216
Cdd:pfam07888 112 ELSEEKDALLAQRA---AHEARIRELEED-----------IKTLTQRVLERETELErmkERAKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1217 LqvdDLLNRVDQMARAKANAEKLCGLYERRLNEANTKLDEVTQLAHDLTTQKtklqsesgeffKRLEEKEALISQLS--R 1294
Cdd:pfam07888 178 A---KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH-----------RKEAENEALLEELRslQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1295 EKSNFT-RQVEELRAQLEE----ESRSQSALSHA-LQSAKHDYDLlreqyeEEQEVKAELHRALSKGNKETVQWRAKYEH 1368
Cdd:pfam07888 244 ERLNASeRKVEGLGEELSSmaaqRDRTQAELHQArLQAAQLTLQL------ADASLALREGRARWAQERETLQQSAEADK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1369 DamqRTEDLEEAKKKLAIRLQEaaEAMEVSNAKnASLERARHRLQLELGDALSDLGKARSvAAALGQKQQhsdkaltswK 1448
Cdd:pfam07888 318 D---RIEKLSAELQRLEERLQE--ERMEREKLE-VELGREKDCNRVQLSESRRELQELKA-SLRVAQKEK---------E 381
|
410
....*....|.
gi 261245016 1449 QKLDETQELLQ 1459
Cdd:pfam07888 382 QLQAEKQELLE 392
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1243-1685 |
5.68e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1243 YERRLNEANTKLDEVTQLAHDLTTQKTKLQSESgeffKRLEEKEALISQLSREKSNFTRQVEELRAQLeeeSRSQSALSH 1322
Cdd:PRK04863 274 YMRHANERRVHLEEALELRRELYTSRRQLAAEQ----YRLVEMARELAELNEAESDLEQDYQAASDHL---NLVQTALRQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1323 ALQSAKHDYDL--LREQYEEEQEVKAELHRAlskgnketvqwRAKYEHDAMQRTEDLEEAKKKLAiRLQEAAE-----AM 1395
Cdd:PRK04863 347 QEKIERYQADLeeLEERLEEQNEVVEEADEQ-----------QEENEARAEAAEEEVDELKSQLA-DYQQALDvqqtrAI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1396 EVSNAKNAsLERARHRLQLelgDALsDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKE---TRALSSEV 1472
Cdd:PRK04863 415 QYQQAVQA-LERAKQLCGL---PDL-TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAyqlVRKIAGEV 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1473 ltfrQACEESTEAQETLKR--QNQDLQEQICSLTNQVREgiknlaevekAKKLIEQEKTeVQVRLEETEGALERNESKIL 1550
Cdd:PRK04863 490 ----SRSEAWDVARELLRRlrEQRHLAEQLQQLRMRLSE----------LEQRLRQQQR-AERLLAEFCKRLGKNLDDED 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1551 RFQLELSEAKAELERKLSEKEEEAERLREKHQQamgslQSNLDleassrIEATRLRKKMEGDLKEMEiqlcAANRQVSQM 1630
Cdd:PRK04863 555 ELEQLQEELEARLESLSESVSEARERRMALRQQ-----LEQLQ------ARIQRLAARAPAWLAAQD----ALARLREQS 619
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261245016 1631 TRALGQLQGQMKDLHQQLDD--SIYQNKDLKE--QVALAEQRTVLLQ---SELEELRTLQEQ 1685
Cdd:PRK04863 620 GEEFEDSQDVTEYMQQLLERerELTVERDELAarKQALDEEIERLSQpggSEDPRLNALAER 681
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
838-1617 |
6.45e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 838 EEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDL----------------RLQLQAEQETLANSEEQCESLIK 901
Cdd:PRK04863 279 NERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELneaesdleqdyqaasdHLNLVQTALRQQEKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 902 skvELEVKIKELSRQVEEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLtEEVHSLNE--- 978
Cdd:PRK04863 359 ---ELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQAL-ERAKQLCGlpd 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 979 -EVSKLSRVVKDAQETQQQTQEQLHIEEEKLSNMSKAN---LKLAQQIDVLEGDLERE---RKARMKCeREKRKLQDElk 1051
Cdd:PRK04863 435 lTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHsqfEQAYQLVRKIAGEVSRSeawDVARELL-RRLREQRHL-- 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1052 mnqegAENLESSRQKLAEqlrkkefemgqmnskVENEKNQVSQLQKMVKEL-QTHILNLKEELEsertirakVEREKGDL 1130
Cdd:PRK04863 512 -----AEQLQQLRMRLSE---------------LEQRLRQQQRAERLLAEFcKRLGKNLDDEDE--------LEQLQEEL 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1131 VQDLEDLNERLEEAGGTSLAQMEITKQQEARFQKL-------HHDMEETTRHFEATSASLKKRHA--ENLAELEGQVEHL 1201
Cdd:PRK04863 564 EARLESLSESVSEARERRMALRQQLEQLQARIQRLaarapawLAAQDALARLREQSGEEFEDSQDvtEYMQQLLEREREL 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1202 QQVRLVLEQDKSDLQLQVDDLLNR-VDQMARAKANAEKLCG-----LYE-----------------------RRLNEANT 1252
Cdd:PRK04863 644 TVERDELAARKQALDEEIERLSQPgGSEDPRLNALAERFGGvllseIYDdvsledapyfsalygparhaivvPDLSDAAE 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1253 KLDEVTQLAHDLTTQKTKLQS------ESGEFFKRL----------------------EEKEALISQLSREKSNFTRQVE 1304
Cdd:PRK04863 724 QLAGLEDCPEDLYLIEGDPDSfddsvfSVEELEKAVvvkiadrqwrysrfpevplfgrAAREKRIEQLRAEREELAERYA 803
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1305 ELRAQLEEESRSQSALSH------ALQSAKHDYDLLREQYEEEQEVKAELHRALSKGNKETVQWRAKYEH-DAMQRTEDL 1377
Cdd:PRK04863 804 TLSFDVQKLQRLHQAFSRfigshlAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGlSALNRLLPR 883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1378 EE--AKKKLAIRLQEAAEamEVSNAKNASLERARHrlqlelGDALSDLGKarsVAAALGQKQQHSDKAltswKQKLDETQ 1455
Cdd:PRK04863 884 LNllADETLADRVEEIRE--QLDEAEEAKRFVQQH------GNALAQLEP---IVSVLQSDPEQFEQL----KQDYQQAQ 948
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1456 ELLQASQKETRALSSEV-----LTFRQA---CEESTEAQETLKRQNQDLQ-------EQICSLTNQVREGIKNLAEVEKA 1520
Cdd:PRK04863 949 QTQRDAKQQAFALTEVVqrrahFSYEDAaemLAKNSDLNEKLRQRLEQAEqertrarEQLRQAQAQLAQYNQVLASLKSS 1028
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1521 KKLIEQEKTEVQVRLEE-----TEGALERNESKILRFQLELSEA---KAELERKLSEKEEEAERL--------------R 1578
Cdd:PRK04863 1029 YDAKRQMLQELKQELQDlgvpaDSGAEERARARRDELHARLSANrsrRNQLEKQLTFCEAEMDNLtkklrklerdyhemR 1108
|
890 900 910
....*....|....*....|....*....|....*....
gi 261245016 1579 EKHQQAMGSLQSNLDLEASSRIEAtRLRKKMEGDLKEME 1617
Cdd:PRK04863 1109 EQVVNAKAGWCAVLRLVKDNGVER-RLHRRELAYLSADE 1146
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1433-1875 |
7.79e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1433 LGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSsevltfrqacEESTEAQETLKRQNQDLQE---QICSLTNQVRE 1509
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLK----------DEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1510 GIKNLAEVEKAK-----KLIEQEKTEVQVRLEETEGALERNESKILRFQLELSEAKAELERKLSEKEEEAERLREKHQQA 1584
Cdd:TIGR04523 293 LKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEI 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1585 M-------GSLQSNLDLEASSRIEATRLRKKmEGDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNKD 1657
Cdd:TIGR04523 373 EklkkenqSYKQEIKNLESQINDLESKIQNQ-EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1658 LKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATERINlfhtqntSLLSQKKKLEADVAQVQKEAGEMLQ 1737
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK-------KLNEEKKELEEKVKDLTKKISSLKE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1738 ACQKAEEKAKKTAAEAANMSEELKKEQDTNAhlermRKNMEQTIKDLQKRLDEAEQTAVLGSKKQ------IQKLESRVR 1811
Cdd:TIGR04523 525 KIEKLESEKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEELKQTQKSLKKKQeekqelIDQKEKEKK 599
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261245016 1812 DLEGELESevrrsaeaqrearrLERGIKELTYQAEEDKKNLSRMQALSDKLQLKVQSYKQQVEA 1875
Cdd:TIGR04523 600 DLIKEIEE--------------KEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
761-1048 |
1.07e-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: 50.84 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 761 LDQLEERRDEKISKVFTLFQA--RARGKLMRIT--FQKILEERDALALIQENIRAFIAVKNCPWMGLFFKIKPLAKSVGA 836
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQElsDASRKIGEIEkeIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 837 GEE-IAGLKEECA------------QLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKSK 903
Cdd:TIGR02169 770 LEEdLHKLEEALNdlearlshsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 904 VELEVKIKELSRQVEEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAE-------HKVRNLTEEVHSL 976
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiekkrKRLSELKAKLEAL 929
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261245016 977 NEEVSKLSRVVKDAQETQQQTQEQLHIE------EEKLSNMSKANLKLAQQIDVLEGDLERERKARMKCEREKRKLQD 1048
Cdd:TIGR02169 930 EEELSEIEDPKGEDEEIPEEELSLEDVQaelqrvEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1528-1924 |
1.07e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1528 KTEVQVRLEETEGALERNESKILRF-QLELSEAKAELERKLSEKEEEAERLREKHQQAMGSLQsnldlEASSRIEATRLR 1606
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKeEKDLHERLNGLESELAELDEEIERYEEQREQARETRD-----EADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1607 KKmegDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNKDLKEQVAL--AEQRTVLLQseLEELRTLQE 1684
Cdd:PRK02224 250 RE---ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLddADAEAVEAR--REELEDRDE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1685 QTERgrklaekELLEATERINLFHTQNTSLLSQKKKLEADVAQVQKEAGEMLQACQkaeekakktaaeaaNMSEELKKEQ 1764
Cdd:PRK02224 325 ELRD-------RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELE--------------EAREAVEDRR 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1765 DTNAHLERMRKNMEQTIKDLQKRLDEAEqtavlGSKKQIQKLESRVRDLEGELESEVRRSAEAQREARRLERGIK----- 1839
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGNAE-----DFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecg 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1840 ------ELTYQAEEDKKNLSRMQALSDKLQLKVQSYKQQVEAA------EAQANQYLSKYKKQQHELNEAKERAEAAESQ 1907
Cdd:PRK02224 459 qpvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAedlveaEDRIERLEERREDLEELIAERRETIEEKRER 538
|
410
....*....|....*..
gi 261245016 1908 VNKLRAKAKELEKKVRE 1924
Cdd:PRK02224 539 AEELRERAAELEAEAEE 555
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1083-1319 |
1.21e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1083 SKVENEKNQVSQLQKMVKELQTHILNLKEELESertirakVEREKGDLVQDLEDLNERLEEAggtslaQMEITKQQEaRF 1162
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEE-------LNEEYNELQAELEALQAEIDKL------QAEIAEAEA-EI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1163 QKLHHDMEETTRHFEATSASLKKR----HAENLAELegqVEHLQQVRLVLEQDKSDLQLQVDDllnrVDQMARAKANAEK 1238
Cdd:COG3883 82 EERREELGERARALYRSGGSVSYLdvllGSESFSDF---LDRLSALSKIADADADLLEELKAD----KAELEAKKAELEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1239 lcglyerrlneantKLDEVTQLAHDLTTQKTKLQSEsgeffkrLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQS 1318
Cdd:COG3883 155 --------------KLAELEALKAELEAAKAELEAQ-------QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
.
gi 261245016 1319 A 1319
Cdd:COG3883 214 A 214
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1235-1893 |
1.33e-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: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1235 NAEKLCGLYERRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLE--EKEALISQLSREKSNFTRQVEELRAQLEe 1312
Cdd:pfam10174 117 NFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEmlQSKGLPKKSGEEDWERTRRIAEAEMQLG- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1313 esrsqsalshalqsakHDYDLLREQYEEEQEVKAELHRALSKGNKETvqwrakyEHDAMQRTEDLEEAKK---KLAIRLQ 1389
Cdd:pfam10174 196 ----------------HLEVLLDQKEKENIHLREELHRRNQLQPDPA-------KTKALQTVIEMKDTKIsslERNIRDL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1390 EAAEAMEVSNAKNASLERARHRLQLE------------LGDALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQEL 1457
Cdd:pfam10174 253 EDEVQMLKTNGLLHTEDREEEIKQMEvykshskfmknkIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKES 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1458 LQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQVREgIKNLAEVEKAKKLIEQEKTE-VQVRLE 1536
Cdd:pfam10174 333 LTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRD-LKDMLDVKERKINVLQKKIEnLQEQLR 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1537 ETEGALERNESKILRFQLELSE---AKAELERKLSEKEEEAERLREKHqqamgslqsnlDLEASSRIEATRLRKKMEGDL 1613
Cdd:pfam10174 412 DKDKQLAGLKERVKSLQTDSSNtdtALTTLEEALSEKERIIERLKEQR-----------EREDRERLEELESLKKENKDL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1614 KEmeiqlcaanrqvsqmtrALGQLQGQMKDLHQQLDDsiyqnkdLKEQVALAEQRTVLLQSELEELR-TLQEQTERGRKL 1692
Cdd:pfam10174 481 KE-----------------KVSALQPELTEKESSLID-------LKEHASSLASSGLKKDSKLKSLEiAVEQKKEECSKL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1693 aEKELLEATErINLFHTQNTSLLSQKKKLEADVAQVQKEAGEmlqaCQKAEEKAKKTAAEAANmsEELKKEQDTnAHLER 1772
Cdd:pfam10174 537 -ENQLKKAHN-AEEAVRTNPEINDRIRLLEQEVARYKEESGK----AQAEVERLLGILREVEN--EKNDKDKKI-AELES 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1773 M--RKNMEQTIKDLQKRLDEAEQTavlgsKKQIQKLESRVRdlegELESEVRRSAEAQREarrlergikELTYQAEEDKK 1850
Cdd:pfam10174 608 LtlRQMKEQNKKVANIKHGQQEMK-----KKGAQLLEEARR----REDNLADNSQQLQLE---------ELMGALEKTRQ 669
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 261245016 1851 NLsrmqalsDKLQLKVQSYKQQVEAAEAQANQYLSKYKKQQHE 1893
Cdd:pfam10174 670 EL-------DATKARLSSTQQSLAEKDGHLTNLRAERRKQLEE 705
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1419-1604 |
1.39e-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: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1419 ALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEVLTFRQ----ACEESTEAQETLKRQNQ 1494
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAeiaeAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1495 DLQEQICSLTN-QVREGIKNLAE-----------VEKAKKLIEQEKTEvQVRLEETEGALERNESKILRFQLELSEAKAE 1562
Cdd:COG3883 94 ALYRSGGSVSYlDVLLGSESFSDfldrlsalskiADADADLLEELKAD-KAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 261245016 1563 LERKLSEKEEEAERLREKHQQAMGSLQSNLDLEASSRIEATR 1604
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1716-1924 |
1.57e-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: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1716 SQKKKLEADVAQVQKEAgemlqacQKAEEKAKKTAAEAANMSEELKKEQDTNAHLERMRKNMEQTIKDLQKRLDEAEqta 1795
Cdd:COG4942 20 DAAAEAEAELEQLQQEI-------AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1796 vlgskKQIQKLESRVRDLEGELESEVRR------------------SAEAQREARRLERGIKELTYQAEEDKKNLSRMQA 1857
Cdd:COG4942 90 -----KEIAELRAELEAQKEELAELLRAlyrlgrqpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261245016 1858 LSDKLQLKVQSYKQQVEAAEAQANQYLSKYKKQQHELNEAKERAEAAESQVNKLRAKAKELEKKVRE 1924
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1244-1474 |
1.72e-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: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1244 ERRLNEANTKLDEVTQLAHDLTTQKTKLQSEsgeffkrLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSALSHA 1323
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQ-------LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1324 LQSAKHDY-DLLREQYEEEQEVKAELhrALSKGNKETVQWRAKYEHDAMQRTEDLEEAKKKLAIRLQEAAEAMEvsnAKN 1402
Cdd:COG4942 99 LEAQKEELaELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE---AER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261245016 1403 ASLERARHRLQLELGDALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEVLT 1474
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
755-1423 |
2.07e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 755 FFKAFILDqlEERRDEKISKVFTLFQA--RARGKLmritfQKILEERDALALIQENIRAFIAVKNCpwMGLFFKIKPLAK 832
Cdd:COG4913 212 FVREYMLE--EPDTFEAADALVEHFDDleRAHEAL-----EDAREQIELLEPIRELAERYAAARER--LAELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 833 SVGAGEEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQL-QAEQETLANSEEQCESLIKSKVELEVKIK 911
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 912 ELSRQVeeeEEINSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQ 991
Cdd:COG4913 363 RLEALL---AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 992 ETQQQTQEQLhieEEKLsNMSKANLK-LAQQIDVLEGDL---------------------ERERKARMKCEREKRKLQ-- 1047
Cdd:COG4913 440 ARLLALRDAL---AEAL-GLDEAELPfVGELIEVRPEEErwrgaiervlggfaltllvppEHYAAALRWVNRLHLRGRlv 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1048 -DELKMNQEGAENLESSRQKLAEQLRKK--------EFEMGQMNS--KVENEKnqvsQLQK---------MVKELQT-HI 1106
Cdd:COG4913 516 yERVRTGLPDPERPRLDPDSLAGKLDFKphpfrawlEAELGRRFDyvCVDSPE----ELRRhpraitragQVKGNGTrHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1107 LNLKEELESERTI----RAKVERekgdLVQDLEDLNERLEEAGgtslAQMEITKQQEARFQKLHHDMEETTRHFEAtsas 1182
Cdd:COG4913 592 KDDRRRIRSRYVLgfdnRAKLAA----LEAELAELEEELAEAE----ERLEALEAELDALQERREALQRLAEYSWD---- 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1183 lkkrhAENLAELEGQVEHLQQVRLVLEQDKSD---LQLQVDDLLNRVDQMARAKANAEKLCGLYERRLNEANTKLDEVTQ 1259
Cdd:COG4913 660 -----EIDVASAEREIAELEAELERLDASSDDlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1260 LAHDLTTQKTKLQSESGEffKRLEEkEALISQLSREKSNFTRQVEELRAQLEeesRSQSALSHALQSAKHDYDL----LR 1335
Cdd:COG4913 735 RLEAAEDLARLELRALLE--ERFAA-ALGDAVERELRENLEERIDALRARLN---RAEEELERAMRAFNREWPAetadLD 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1336 EQYEEEQEVKAELHRalskgnketvqwrakyehdamQRTEDLEEAKKKLAIRLQEAAEAmEVSN---AKNASLERARHRL 1412
Cdd:COG4913 809 ADLESLPEYLALLDR---------------------LEEDGLPEYEERFKELLNENSIE-FVADllsKLRRAIREIKERI 866
|
730
....*....|.
gi 261245016 1413 QlELGDALSDL 1423
Cdd:COG4913 867 D-PLNDSLKRI 876
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
832-1295 |
2.09e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 832 KSVGAGEEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKSKVELEV--K 909
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDidN 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 910 IKELSRQVEEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKD 989
Cdd:TIGR00618 523 PGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 990 AQETQQQTQEQLHIEEEKLSnmskanlklaQQIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGA-ENLESSRQKLA 1068
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKLQ----------PEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVrEHALSIRVLPK 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1069 EQLRKKEFEMGQMNSKVEneknqvsQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNERLEeaggts 1148
Cdd:TIGR00618 673 ELLASRQLALQKMQSEKE-------QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARED------ 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1149 LAQMEITKQQEARFQKLHHDMEETTRHFEATSASLKKrhAENLAELEGQVEHLQQVRLVLEQDKSDLQLQVDDLLNRVDQ 1228
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQT--GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261245016 1229 MARAKanaeklCGLYERRLNEANTKLDEVTQLAHDLTTQKTKLQsESGEFFKRLEEKEALISQLSRE 1295
Cdd:TIGR00618 818 ILNLQ------CETLVQEEEQFLSRLEEKSATLGEITHQLLKYE-ECSKQLAQLTQEQAKIIQLSDK 877
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1280-1696 |
2.35e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1280 KRLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSALSHALQsakhdydlLREQYEEEQEVKAELHRALSKgnKET 1359
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ--------LLPLYQELEALEAELAELPER--LEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1360 VQWRAKYEHDAMQRTEDLEEAKKKLAIRLQEAAEamEVSNAKNASLERARHRLQlELGDALSDLGKARSVAAALGQKQQH 1439
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLE--QLSLATEEELQDLAEELE-ELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1440 SDKALTSWKQKLDETQELLQASQkeTRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQIC-SLTNQVREGIKNLAEVE 1518
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARL--LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAlLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1519 KAKKLIEQEKTEvQVRLEETEGALERNESKILRFQLELSEAKAELERKLSEKEEEAERLREKHQQA-----MGSLQSNLD 1593
Cdd:COG4717 306 ELQALPALEELE-EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeiaalLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1594 LEASSRIEATRLRKKMEGDLKEMEIQLCAANRQVSQMTRALG--QLQGQMKDLHQQLDDSIYQNKDLKEQVALAEQRTVL 1671
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420
....*....|....*....|....*..
gi 261245016 1672 LQS--ELEELRTLQEQTERGRKLAEKE 1696
Cdd:COG4717 465 LEEdgELAELLQELEELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1144-1404 |
3.14e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1144 AGGTSLAQMEITKQQEARFQKLHHDMEETTRHFEATSASlKKRHAENLAELEGQVEHLQQVRLVLEQDKSDLQLQVDDLL 1223
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1224 NrvdQMARAKANAEKLCGLYERRLNEA--NTKLDEVTQLAHdlttqktklQSESGEFFKRLEekeaLISQLSREKSNftr 1301
Cdd:COG4942 90 K---EIAELRAELEAQKEELAELLRALyrLGRQPPLALLLS---------PEDFLDAVRRLQ----YLKYLAPARRE--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1302 QVEELRAQLEEESRSQSALSHALQSAKHDYDLLREQYEEEQEVKAELHRALSKGNKETVQWRAKYEhDAMQRTEDLEEAK 1381
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA-ELQQEAEELEALI 229
|
250 260
....*....|....*....|...
gi 261245016 1382 KKLAIRLQEAAEAMEVSNAKNAS 1404
Cdd:COG4942 230 ARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1448-1828 |
3.28e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1448 KQKLDETQELLQASQKETRALSSEVLTFRQACE--ESTEAQETLKRQNQDLQEQIcsltNQVREGIKNLAEVEKAKKLIE 1525
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERL----EELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1526 QEKTEVQVRLEETEGALERNESKILRfqlELSEAKAELERKLSEKEEEAERLREKHQQAMGSLQsnldleassRIEATRL 1605
Cdd:COG4717 170 AELAELQEELEELLEQLSLATEEELQ---DLAEELEELQQRLAELEEELEEAQEELEELEEELE---------QLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1606 RKKMEGDLKEMEIQLCAANRQVS-------------------------------QMTRALGQLQGQMKDLHQQLDDSIYQ 1654
Cdd:COG4717 238 AAALEERLKEARLLLLIAAALLAllglggsllsliltiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1655 NKDLKEQVALAEQRTVLLQSELEELrtLQEQTERGRKLAEKELLEATERINLFHTQNTSLLSQKK-KLEADVAQVQKEAG 1733
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLEL--LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGvEDEEELRAALEQAE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1734 EMLQACQKAEEKAKKTAAEAANMSEELKKEQDTN-----AHLERMRKNMEQTIKDLQKRLDEAE-QTAVLGSKKQIQKLE 1807
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEALDEEEleeelEELEEELEELEEELEELREELAELEaELEQLEEDGELAELL 475
|
410 420
....*....|....*....|.
gi 261245016 1808 SRVRDLEGELESEVRRSAEAQ 1828
Cdd:COG4717 476 QELEELKAELRELAEEWAALK 496
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1428-1663 |
3.64e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1428 SVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQV 1507
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1508 REGIKNLAEVEK--AKKLIEQEKTEVQVRLEETEGALERNES-KILRFQLELSEAKAELERKLSEKEEEAERLREKHQQA 1584
Cdd:COG4942 93 AELRAELEAQKEelAELLRALYRLGRQPPLALLLSPEDFLDAvRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261245016 1585 MGSLQSNLDleassriEATRLRKKMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNKDLKEQVA 1663
Cdd:COG4942 173 RAELEALLA-------ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1562-1925 |
4.30e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1562 ELERKLSEKEEEAERLREKHQQAMGSLQSNLDLEASSRIEATRLRKKMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQM 1641
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1642 KDLHQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATERINLFHTQNTSLLSQKKKL 1721
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1722 EADVAQVQKEAGEMLQACQKAEEKAKKTAAEAANMSEELKKEQDTNAHLERMRKNMEQTIkDLQKRLDEAEQTAVLGSKK 1801
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE-AKDSLEAKLGLALSALLDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1802 QIQKLESRVRDLEGELESEVRRSAEAQREARRLERGIKELTYQAEEDKKNLSRMQALSDKLQLKVQSYKQQVEAAEAQAN 1881
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 261245016 1882 QYLSKYKKQQHELNEAKERAEAAESQVNKLRAKAKELEKKVREE 1925
Cdd:COG4372 322 LELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1518-1704 |
4.46e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1518 EKAKKLIEQEKTEVQVRLEEtegalernesKILRFQLELSEAKAELERKLSEKEEEAERLREKHQQamgslqsnldleas 1597
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKE----------ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQ-------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1598 sRIEatRLRKKMEgDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQlddsiyQNKDLKEQVAL--AEQRTVLLQSE 1675
Cdd:PRK12704 94 -KEE--NLDRKLE-LLEKREEELEKKEKELEQKQQELEKKEEELEELIEE------QLQELERISGLtaEEAKEILLEKV 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 261245016 1676 LEELRT---------LQEQTERGRKLAEKELLEATERI 1704
Cdd:PRK12704 164 EEEARHeaavlikeiEEEAKEEADKKAKEILAQAIQRC 201
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1437-1841 |
5.84e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1437 QQHSDKALTSWKQKLDETQELLQASQKETRALSSEVLTFRQAceesTEAQETLKRQNQDLQEQICSLTNQVR--EGIKNL 1514
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELEklEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1515 AEVEKAKKLIEQEKTEVQVRLEETEG---ALERNESKILRFQLELSEAKAELERKLS----EKEEEAERLREKHQQAMGS 1587
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1588 LQSNLDLEASSRIEATRLRKKMEGDLKEMEI-QLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNKDLKEQVALAE 1666
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAaALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1667 QRTVLLQSELEELRTLQEQTE---RGRKLAEKELLEATERINLFHTQNTSLLSQKKKLEADVAQVQKEAGEM---LQACQ 1740
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQalpALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELeeeLQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1741 KAEEKAKKTAAEAANMSEELKKEQDTNAHLERMRKNMEQTIKDLQKRLDEAEQTAVLGSKKQiqkLESRVRDLEGELESE 1820
Cdd:COG4717 368 LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE---LEEELEELEEELEEL 444
|
410 420
....*....|....*....|.
gi 261245016 1821 VRRSAEAQREARRLERGIKEL 1841
Cdd:COG4717 445 EEELEELREELAELEAELEQL 465
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1602-1847 |
8.42e-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: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1602 ATRLRKKMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEE-LR 1680
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1681 TLQEQTERGRKLAE-------KELLEATERINLFHTQNTSLLSQKKKLEADVAQVQKEAgemlqacqkaeekakktaaea 1753
Cdd:COG3883 94 ALYRSGGSVSYLDVllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAEL--------------------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1754 anmSEELKKEQDTNAHLERMRKNMEQTIKDLQKRLDEAEQtavlgskkQIQKLESRVRDLEGELESEVRRSAEAQREARR 1833
Cdd:COG3883 153 ---EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA--------EEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
250
....*....|....
gi 261245016 1834 LERGIKELTYQAEE 1847
Cdd:COG3883 222 AAAAAAAAAAAAAA 235
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1453-1895 |
9.15e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1453 ETQELLQASQKETRALSSEVLTFRQACEESTEAQE---TLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKT 1529
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAkkkSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1530 EVQVRLEETEGALERNESKI---LRFQLELSEAKAELErKLSEKEEEAERLREKHQQAMGSLQSNLDLEASSRIEA---- 1602
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQeeqLKKQQLLKQLRARIE-ELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQqaqr 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1603 --TRLRKKMEGDLKEMEIQLCAANRQVS--QMTRALGQLQGQMKDLHQQ-------LDDSIYQNKDLKEQVALAEQRTVL 1671
Cdd:TIGR00618 312 ihTELQSKMRSRAKLLMKRAAHVKQQSSieEQRRLLQTLHSQEIHIRDAhevatsiREISCQQHTLTQHIHTLQQQKTTL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1672 LQ-SELEELRTLQEQTERGRKLAEkELLEATERINLFHTQNTSLLSQKKKLE-----ADVAQVQKEAGEMLQACQKAEEK 1745
Cdd:TIGR00618 392 TQkLQSLCKELDILQREQATIDTR-TSAFRDLQGQLAHAKKQQELQQRYAELcaaaiTCTAQCEKLEKIHLQESAQSLKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1746 AKKTAAEAANMSEELKK-----EQDTNAHLERMRKNMEQTIKDLQKRLD----EAEQTAVLGSKKQIQKLESRVRDLEGE 1816
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRkkavvLARLLELQEEPCPLCGSCIHPNPARQDidnpGPLTRRMQRGEQTYAQLETSEEDVYHQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1817 LESEVRRSAEAQREARRLERGIKELTYQAEEDKKNLSRMQALSDKLQ------------LKVQSYKQQVEAAEAQANQYL 1884
Cdd:TIGR00618 551 LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQdlteklseaedmLACEQHALLRKLQPEQDLQDV 630
|
490 500
....*....|....*....|....
gi 261245016 1885 SKYKKQ-------------QHELN 1895
Cdd:TIGR00618 631 RLHLQQcsqelalkltalhALQLT 654
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1523-1919 |
1.17e-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: 47.12 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1523 LIEQEKTEVQVRLE---ETEGALERNESKILRFQLELSEAK-AELERKLSEKEEEAErlrekhqqamgSLQSNLDLEASS 1598
Cdd:pfam10174 201 LDQKEKENIHLREElhrRNQLQPDPAKTKALQTVIEMKDTKiSSLERNIRDLEDEVQ-----------MLKTNGLLHTED 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1599 RIEatrlrkkmegDLKEMEIQLCAAN---RQVSQMTRALGQLQGQMKDLHQQLDDSIYQNKD-------LKEQVALAEQR 1668
Cdd:pfam10174 270 REE----------EIKQMEVYKSHSKfmkNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqhievLKESLTAKEQR 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1669 TVLLQSELEELR--------TLQEQTERGRKLAE------------KELLEATER-INLFHTQNTSLLSQKKKLEadvaq 1727
Cdd:pfam10174 340 AAILQTEVDALRlrleekesFLNKKTKQLQDLTEekstlageirdlKDMLDVKERkINVLQKKIENLQEQLRDKD----- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1728 vqKEAGEMLQACQKAEEKAKKTAAEAANMSEELKKEQDTnahLERMRknmEQTIKDLQKRLDEAEQtavlgSKKQIQKLE 1807
Cdd:pfam10174 415 --KQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERI---IERLK---EQREREDRERLEELES-----LKKENKDLK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1808 SRVRDLEGELESEVRRSAEAQREARRL-------ERGIKELTYQAEEDKKNLSRMQAlsdklqlkvQSYKQQVEAAEAQA 1880
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKEHASSLassglkkDSKLKSLEIAVEQKKEECSKLEN---------QLKKAHNAEEAVRT 552
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 261245016 1881 N-QYLSKYKKQQHELNEAKERAEAAESQVNKLRAKAKELE 1919
Cdd:pfam10174 553 NpEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVE 592
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1058-1251 |
1.34e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1058 ENLESSRQKLAEQLRKKEFEMGQMNSKVENEknQVSQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQD--LE 1135
Cdd:COG3206 189 KELEEAEAALEEFRQKNGLVDLSEEAKLLLQ--QLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQ 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1136 DLNERLEEAggtslaQMEITkQQEARFQKLHHDMEETTRHFEATSASLKKRHAENLAELEGQVEHLQQVRLVLEQDKSDL 1215
Cdd:COG3206 267 QLRAQLAEL------EAELA-ELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQL 339
|
170 180 190
....*....|....*....|....*....|....*....
gi 261245016 1216 QLQVDDLLNRVDQMARAKANAEKLCGLYE---RRLNEAN 1251
Cdd:COG3206 340 EARLAELPELEAELRRLEREVEVARELYEsllQRLEEAR 378
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1308-1920 |
1.41e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.99 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1308 AQLEEESRSQSALSHALQSAKHDYDLLREQYEEEQEVKAE-LHRALSKGNKETVQWRA-KYEHDAMQRTEDLEEAKKKLa 1385
Cdd:COG5022 806 LGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEvLIQKFGRSLKAKKRFSLlKKETIYLQSAQRVELAERQL- 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1386 IRLQEAAEamEVSNAKNASLErarhrLQLELgdalsdLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKET 1465
Cdd:COG5022 885 QELKIDVK--SISSLKLVNLE-----LESEI------IELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYV 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1466 RalSSEVLTFRQACEEsteaqetLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIeQEKTEVQVRLEETEGALERN 1545
Cdd:COG5022 952 K--LPELNKLHEVESK-------LKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL-AELSKQYGALQESTKQLKEL 1021
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1546 ESKILRFQLE---LSEAKAELERKLSEKEEEAERLREKHQQAMGSLQSNLDLEASSRIEA-TRLRKKMEGDLKEMEI-QL 1620
Cdd:COG5022 1022 PVEVAELQSAskiISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKqLYQLESTENLLKTINVkDL 1101
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1621 CAANRQVSQMTRALGQLQGQMK--DLHQQLDDSIYQNKDLKEQValaEQRTVLLQSELEELRTLQEQTERGRKLAEKELL 1698
Cdd:COG5022 1102 EVTNRNLVKPANVLQFIVAQMIklNLLQEISKFLSQLVNTLEPV---FQKLSVLQLELDGLFWEANLEALPSPPPFAALS 1178
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1699 EATERIN-LFHTQNTSLLSQKKKLEADV-AQVQKEAGEMLQACQKAEEKAKKTAAEAANMS------EELKKEQDTNAHL 1770
Cdd:COG5022 1179 EKRLYQSaLYDEKSKLSSSEVNDLKNELiALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSlkgfnnLNKKFDTPASMSN 1258
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1771 ERMRKNMEQTIKDLQ--KRLDEAEQTAVLGSKKQI-----QKLESRVRDLEGELESEVRRSAEAQREARRlERGIKELTY 1843
Cdd:COG5022 1259 EKLLSLLNSIDNLLSsyKLEEEVLPATINSLLQYInvglfNALRTKASSLRWKSATEVNYNSEELDDWCR-EFEISDVDE 1337
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261245016 1844 QAEEDKKNLSRMQALSDKLQLKVQSYKQQVEAAEAQANQYLSKYKKQQHELNEAKERAEAAESQVNKLRAKAKELEK 1920
Cdd:COG5022 1338 ELEELIQAVKVLQLLKDDLNKLDELLDACYSLNPAEIQNLKSRYDPADKENNLPKEILKKIEALLIKQELQLSLEGK 1414
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1506-1615 |
1.44e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1506 QVREGIKNL-AEVEKAKKLIEQEKTEVQVRLEETEGALERNESKILRFQLELSEAKAELERK---LSEKEEEAERLREKH 1581
Cdd:PRK12704 61 EAKEEIHKLrNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKqqeLEKKEEELEELIEEQ 140
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 261245016 1582 QQAMGSLqSNL-----------DLEASSRIEATRLRKKMEGDLKE 1615
Cdd:PRK12704 141 LQELERI-SGLtaeeakeilleKVEEEARHEAAVLIKEIEEEAKE 184
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1331-1654 |
1.75e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.49 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1331 YDLLREQYEEEQEVKAELHRALSKGNKETVQWRAKYEHDAMQRTEDLEEAKKKLAIRLQEAAEAMEvSNAKNASLERARh 1410
Cdd:COG5185 234 ALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIA-EYTKSIDIKKAT- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1411 rlqlelgDALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEVLT---FRQACEESTEAQE 1487
Cdd:COG5185 312 -------ESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGeveLSKSSEELDSFKD 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1488 TLKRQNQDLQEQicsLTNQVREGIKNLAEVEKAKKLIEQEktevqvrLEETEGALERNESKILRFQLELSEAKAELERKL 1567
Cdd:COG5185 385 TIESTKESLDEI---PQNQRGYAQEILATLEDTLKAADRQ-------IEELQRQIEQATSSNEEVSKLLNELISELNKVM 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1568 SE-KEEEAERLREKHQQAMGSLQSNLDLEASsriEATRLRKKMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQ 1646
Cdd:COG5185 455 REaDEESQSRLEEAYDEINRSVRSKKEDLNE---ELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMR 531
|
....*...
gi 261245016 1647 QLDDSIYQ 1654
Cdd:COG5185 532 ARGYAHIL 539
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1049-1894 |
2.60e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1049 ELKMNQEGAENLESSRQKLAEQLRKKEFEMGQMNSKVEneknqvsQLQKMVKELQTHILNLKEELESERTIRAKVEREKg 1128
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELA-------ELNEAESDLEQDYQAASDHLNLVQTALRQQEKIE- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1129 DLVQDLEDLNERLEEaggtslaQMEITkqQEARFQKlhhdmEETTRHFEATSASLKkrhaenlaELEGQVEHLQQvRLVL 1208
Cdd:PRK04863 352 RYQADLEELEERLEE-------QNEVV--EEADEQQ-----EENEARAEAAEEEVD--------ELKSQLADYQQ-ALDV 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1209 EQDKSdLQLQvddllnrvdQMARAKANAEKLCGL-------YERRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKR 1281
Cdd:PRK04863 409 QQTRA-IQYQ---------QAVQALERAKQLCGLpdltadnAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQA 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1282 LEEKEALISQLSREksnftrQVEELRAQLEEESRSQSALSHALQSAKHDYDLLREQYEEEQEVKAELHRALSKGNKEtvq 1361
Cdd:PRK04863 479 YQLVRKIAGEVSRS------EAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKN--- 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1362 wrakyehdaMQRTEDLEEAKKKLAIRLQEAAEAMEVSNAKNASLERARHRLQLELGDALSDLGKARSVAAALGQKQQHSD 1441
Cdd:PRK04863 550 ---------LDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSG 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1442 KALTSwKQKLDETQELLQASQKETRALSSEVLTFRQACEE--------STEAQETLKRQNQD--------------LQEQ 1499
Cdd:PRK04863 621 EEFED-SQDVTEYMQQLLERERELTVERDELAARKQALDEeierlsqpGGSEDPRLNALAERfggvllseiyddvsLEDA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1500 --ICSLTNQVREGI--KNLAEVekAKKLIEQEKTEVQVRL---------------EETEGAL-----ERnESKILRFQLE 1555
Cdd:PRK04863 700 pyFSALYGPARHAIvvPDLSDA--AEQLAGLEDCPEDLYLiegdpdsfddsvfsvEELEKAVvvkiaDR-QWRYSRFPEV 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1556 LSEAKAELERKLSEKEEEAERLREKHQQA---MGSLQSNLdlEASSRIEATRLRKKMEGDlKEMEIQlcAANRQVSQMTR 1632
Cdd:PRK04863 777 PLFGRAAREKRIEQLRAEREELAERYATLsfdVQKLQRLH--QAFSRFIGSHLAVAFEAD-PEAELR--QLNRRRVELER 851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1633 ALGQLQGQMKDLHQQLDdsiyqnkDLKEQVALAEQ---RTVLLQSEL--EELRTLQEQTERGRKlAEKELLEATERINLF 1707
Cdd:PRK04863 852 ALADHESQEQQQRSQLE-------QAKEGLSALNRllpRLNLLADETlaDRVEEIREQLDEAEE-AKRFVQQHGNALAQL 923
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1708 HTQNTSLLSQKKKLEADVAQVQkEAGEMLQACQKAEEKAKKTAAEAANMSEE-----LKKEQDTN-------AHLERMRK 1775
Cdd:PRK04863 924 EPIVSVLQSDPEQFEQLKQDYQ-QAQQTQRDAKQQAFALTEVVQRRAHFSYEdaaemLAKNSDLNeklrqrlEQAEQERT 1002
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1776 NMEQTIKDLQKRLDEAEQtaVLGS-KKQIQKLESRVRDLEGELES-EVRRSAEAQREARRlergikeltyQAEEDKKNLS 1853
Cdd:PRK04863 1003 RAREQLRQAQAQLAQYNQ--VLASlKSSYDAKRQMLQELKQELQDlGVPADSGAEERARA----------RRDELHARLS 1070
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 261245016 1854 RMQALSDKLQLKVQSYKQQVEAAEAQANQYLSKYKKQQHEL 1894
Cdd:PRK04863 1071 ANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1281-1878 |
2.88e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.89 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1281 RLEEKEALISQLSREKSNFTRQVEELRAQLEEESrSQSALSHALQSAKHDYDLLREQYEEEQEVKAElhralsKGNKETV 1360
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKA-SALKRQLDRESDRNQELQKRIRLLEKREAEAE------EALREQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1361 QwrakyehDAMQRTEDLEEAKKKLAIRLQEAAEAMEVSNAKNASLerarhrlqlelgdalsdlgkarsvaAALGQKQQHS 1440
Cdd:pfam05557 76 E-------LNRLKKKYLEALNKKLNEKESQLADAREVISCLKNEL-------------------------SELRRQIQRA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1441 DKALTSWKQKLDETQELLQASQKETRALSSEVLTFRQACEESTEAQETLKRQNQDLQEQ-------------------IC 1501
Cdd:pfam05557 124 ELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQeqdseivknskselaripeLE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1502 SLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALErnesKILRFQLELSeakaELERKLSEKEEEAerlrekh 1581
Cdd:pfam05557 204 KELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYRE----EAATLELEKE----KLEQELQSWVKLA------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1582 QQAMGSLQSNLDLeaSSRIEATRLRKKMEGDLK-EMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNKDLKE 1660
Cdd:pfam05557 269 QDTGLNLRSPEDL--SRRIEQLQQREIVLKEENsSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1661 QVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKeLLEATERINLFHTQNTSLLSQKKKLEADVAqVQKEAGEMLQACQ 1740
Cdd:pfam05557 347 RVLLLTKERDGYRAILESYDKELTMSNYSPQLLER-IEEAEDMTQKMQAHNEEMEAQLSVAEEELG-GYKQQAQTLEREL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1741 KAEEKAKKTAAEAANMSE--ELKKEQDtnaHLERMRKNMEQTIKDLQKRLDEAEQTAVLGSKKqiqkleSRVRDLEGELE 1818
Cdd:pfam05557 425 QALRQQESLADPSYSKEEvdSLRRKLE---TLELERQRLREQKNELEMELERRCLQGDYDPKK------TKVLHLSMNPA 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261245016 1819 SEVRRSAEAQREARRLE-RGIKELTYQAEEDKKNLSRMQALSDKLQLK-VQSYKQQVEAAEA 1878
Cdd:pfam05557 496 AEAYQQRKNQLEKLQAEiERLKRLLKKLEDDLEQVLRLPETTSTMNFKeVLDLRKELESAEL 557
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1369-1644 |
3.60e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.82 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1369 DAMQRTEDLEEAKKKLAIRLQEAAEAMEVS----NAKNASLERARH---------RLQLELGDALSDLG-KARSVAAALG 1434
Cdd:PRK10929 24 DEKQITQELEQAKAAKTPAQAEIVEALQSAlnwlEERKGSLERAKQyqqvidnfpKLSAELRQQLNNERdEPRSVPPNMS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1435 QKQQHSDKALTSwKQKLDETQELlQASQKETRALSSEVLTFRQaceESTEAqetlKRQNQDLQEQICSLTNqvregiKNL 1514
Cdd:PRK10929 104 TDALEQEILQVS-SQLLEKSRQA-QQEQDRAREISDSLSQLPQ---QQTEA----RRQLNEIERRLQTLGT------PNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1515 AEVEKAKKLIEQEKTEVQVRLEETEGA-LERNESKilrfqlELSEAKAELERKlsekeeEAERLREKHQQAMGSLQSNLD 1593
Cdd:PRK10929 169 PLAQAQLTALQAESAALKALVDELELAqLSANNRQ------ELARLRSELAKK------RSQQLDAYLQALRNQLNSQRQ 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 261245016 1594 LEASSRIEATRLRKKMEGDLKEMEIQLCAANRQVSQmtrALGQlQGQMKDL 1644
Cdd:PRK10929 237 REAERALESTELLAEQSGDLPKSIVAQFKINRELSQ---ALNQ-QAQRMDL 283
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1208-1414 |
3.76e-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: 45.14 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1208 LEQDKSDLQLQVDDLLNRVDQMARAKANAEKLCGLYERRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEA 1287
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1288 LIS-------------------------QLSREKSNFTRQVEELRAQLEEESRSQSALSHALQSAKHDYDLLREQYEEEQ 1342
Cdd:COG4942 105 ELAellralyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261245016 1343 EVKAELHRALSKGNKETVQWRAKYEHDAmQRTEDLEEAKKKL--AIRLQEAAEAMEVSNAKNASLERARHRLQL 1414
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELeaLIARLEAEAAAAAERTPAAGFAALKGKLPW 257
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1375-1924 |
3.83e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1375 EDLEEAKKKLAIRLQEAAEAMEVSNAKNASLERARHRLQLELGDALSDLgkarsvaaalgqkqQHSDKALTSWKQKLDET 1454
Cdd:PRK01156 186 DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDY--------------NNLKSALNELSSLEDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1455 QELLQASQKETRALSSEVltfrqacEESTEAQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQvR 1534
Cdd:PRK01156 252 NRYESEIKTAESDLSMEL-------EKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEIN-K 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1535 LEETEGALERNESKILRFqLELSEAKAELERKLSEKEEEaerlREKHQQAMGSLQSNLDLEASSRIEATRLRKKMEGDLK 1614
Cdd:PRK01156 324 YHAIIKKLSVLQKDYNDY-IKKKSRYDDLNNQILELEGY----EMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1615 EMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNKDLKEQVALAEQRTV--LLQSELEElrtlqEQTERGRKL 1692
Cdd:PRK01156 399 IQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpVCGTTLGE-----EKSNHIINH 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1693 AEKELLEATERINLFHTQNTSLLSQKKKLEADVAQVQKEAGEMLQACQKAEEKAKKTAAEAANMSEELK---------KE 1763
Cdd:PRK01156 474 YNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKdkhdkyeeiKN 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1764 QDTNAHLERMRKNMEQ-----------TIKDLQKRLDEAeqtavlgsKKQIQKLESRVRDLEGEL-------ESEVRRSA 1825
Cdd:PRK01156 554 RYKSLKLEDLDSKRTSwlnalavisliDIETNRSRSNEI--------KKQLNDLESRLQEIEIGFpddksyiDKSIREIE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1826 EaqrEARRLERGIKELtyqaeEDKKnlsrmqALSDKLQLKVQSYKQQVEAAE----------AQANQYLSKYKKQQHELN 1895
Cdd:PRK01156 626 N---EANNLNNKYNEI-----QENK------ILIEKLRGKIDNYKKQIAEIDsiipdlkeitSRINDIEDNLKKSRKALD 691
|
570 580
....*....|....*....|....*....
gi 261245016 1896 EAKERAEAAESQVNKLRAKAKELEKKVRE 1924
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRIND 720
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
905-1352 |
3.86e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 905 ELEVKIKELSRQVEEEEEINSELtargRKLEDECSELKKEIYDLEAILAKSEKgkcaaEHKVRNLTEEVHSLNEEVSKLS 984
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 985 RVVKDAQETQQQTQEQLHIEEEKLSNMSKANLKLAQQIDVL----EGDLERERKARMKCEREKRKLQDELKMNQEGAENL 1060
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1061 ESSRQKLAEQLRkkefemgqmnskVENEKNQVSQLQKMVKEL--QTHILNLKEELESERTIRAKVEREKGDLVQDLEDLN 1138
Cdd:COG4717 226 EEELEQLENELE------------AAALEERLKEARLLLLIAaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1139 ERLEEAGGTSLAQMEITKQQEARfqklhhDMEETTRHFEATSASlKKRHAENLAELEGQVEHLQQVRLVLEQDKSDLQLQ 1218
Cdd:COG4717 294 AREKASLGKEAEELQALPALEEL------EEEELEELLAALGLP-PDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1219 vdDLLNRVDQMArAKANAEKLCGLYER--RLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFfkrleEKEALISQLSREK 1296
Cdd:COG4717 367 --ELEQEIAALL-AEAGVEDEEELRAAleQAEEYQELKEELEELEEQLEELLGELEELLEAL-----DEEELEEELEELE 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 261245016 1297 snftRQVEELRAQLEEESRSQSALSHALQSAKHDyDLLREQYEEEQEVKAELHRAL 1352
Cdd:COG4717 439 ----EELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELRELA 489
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
885-1168 |
4.00e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.80 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 885 EQETLANSEEQCESLIKSKVELEVKIKELSRQVEEEEEInseltargRKLEDECSELKKEIYDLEAILAKSEKGKCAAEH 964
Cdd:pfam15905 44 SKDASTPATARKVKSLELKKKSQKNLKESKDQKELEKEI--------RALVQERGEQDKRLQALEEELEKVEAKLNAAVR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 965 KVRNLTEEVHSLNEEVSKLSRV-----VKDAQETQQQTQEQLHIEEEKLSNMSKANLK--LAQQIDvLEGDLERERKARM 1037
Cdd:pfam15905 116 EKTSLSASVASLEKQLLELTRVnellkAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKevMAKQEG-MEGKLQVTQKNLE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1038 KCEREKRKLQDELKMNQEGAENLESSRQKLAEQLRkkefEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESER 1117
Cdd:pfam15905 195 HSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYIT----ELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKE 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 261245016 1118 TIRAKVEREKGDLVQDLEDLNERL----EEAGGTSLAQMEITK----QQEARFQKLHHD 1168
Cdd:pfam15905 271 QELSKQIKDLNEKCKLLESEKEELlreyEEKEQTLNAELEELKekltLEEQEHQKLQQK 329
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1004-1313 |
4.98e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1004 EEEKLSNMSKANLKLAQQIDVLEGDLERERKARMKCEREKRKLQDELKmnqEGAENLESSRQKLAEQLRKKEFEmgQMNS 1083
Cdd:COG5185 234 ALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLN---ENANNLIKQFENTKEKIAEYTKS--IDIK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1084 KVENEKNQVSQ-------LQKMVKELQTHILNLKEELESERTI------RAKVEREKGDLVQDLEDLNERLEEAGgtslA 1150
Cdd:COG5185 309 KATESLEEQLAaaeaeqeLEESKRETETGIQNLTAEIEQGQESltenleAIKEEIENIVGEVELSKSSEELDSFK----D 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1151 QMEITKQqeaRFQKLHHDMEETTRHFEATSASLKKRHAENLAELEGQVEhlQQVRLVLEQDKSDLQLQVDdlLNRVDQMA 1230
Cdd:COG5185 385 TIESTKE---SLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIE--QATSSNEEVSKLLNELISE--LNKVMREA 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1231 RAKANA---EKLCGLYERRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLSREKSNFTRQVEELR 1307
Cdd:COG5185 458 DEESQSrleEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAH 537
|
....*.
gi 261245016 1308 AQLEEE 1313
Cdd:COG5185 538 ILALEN 543
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1040-1238 |
5.33e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1040 EREKRKLQDELKMNQEGAENLESSRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESerti 1119
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1120 RAKVEREKGDLV---------QDLEDLNERLEeaggtslAQMEITKQQEARFQKLHHDMEETTRHfEATSASLKKRHAEN 1190
Cdd:COG3883 91 RARALYRSGGSVsyldvllgsESFSDFLDRLS-------ALSKIADADADLLEELKADKAELEAK-KAELEAKLAELEAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 261245016 1191 LAELEGQVEHLQQVRLVLEQDKSDLQLQVDDLLNRVDQMARAKANAEK 1238
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1509-1620 |
5.75e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.48 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1509 EGIKNLAEV----EKAKKLIEQEkTEVQVRLEETEGALERNESKILRFQLELSEAKAELERKLSEKEEEAERLREKHQQA 1584
Cdd:COG2268 189 LGRRKIAEIirdaRIAEAEAERE-TEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAA 267
|
90 100 110
....*....|....*....|....*....|....*.
gi 261245016 1585 MGSLQSNLDLEASSRIEATRLRKKMEgdLKEMEIQL 1620
Cdd:COG2268 268 YEIAEANAEREVQRQLEIAEREREIE--LQEKEAER 301
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1284-1605 |
6.04e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.85 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1284 EKEALISQLSREKSNFTRQVEELRAQLEEESRSQSAL--SHALQSA--KHDYDLLREQYEEEQEVKAELHRALskgnKET 1359
Cdd:PLN03229 437 EVEKLKEQILKAKESSSKPSELALNEMIEKLKKEIDLeyTEAVIAMglQERLENLREEFSKANSQDQLMHPVL----MEK 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1360 VQwRAKYEHD-AMQRTEDLEEAKKKLAIrLQEAAEAMEVSNAKNASLErarhrLQLELGDALSDLGKARSVAAAL-GQKQ 1437
Cdd:PLN03229 513 IE-KLKDEFNkRLSRAPNYLSLKYKLDM-LNEFSRAKALSEKKSKAEK-----LKAEINKKFKEVMDRPEIKEKMeALKA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1438 QHSDKALTSWKQKLDETQELLQASQKETRALSSEVLT---FRQACEESTEAQETLKRQNQDLQEQICSLTNQVREGIKNL 1514
Cdd:PLN03229 586 EVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKsmgLEVIGVTKKNKDTAEQTPPPNLQEKIESLNEEINKKIERV 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1515 AEVEKAKKLIEQEKTEVqVRLEETEGALERNESKILRFQL--ELSEA--KAELERKLSEKEEEAERLREKHQQAMGSLQS 1590
Cdd:PLN03229 666 IRSSDLKSKIELLKLEV-AKASKTPDVTEKEKIEALEQQIkqKIAEAlnSSELKEKFEELEAELAAARETAAESNGSLKN 744
|
330
....*....|....*
gi 261245016 1591 NLDLEASSRIEATRL 1605
Cdd:PLN03229 745 DDDKEEDSKEDGSRV 759
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
575-666 |
6.39e-04 |
|
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: 42.33 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 575 GVVPY---NISGWIGKNKGLLNETVVALLQKSSNKVLanlftkdIIAGSASQFGE-KTHKKGTS--FHLITSL------- 641
Cdd:cd01363 71 GVIPYlasVAFNGINKGETEGWVYLTEITVTLEDQIL-------QANPILEAFGNaKTTRNENSsrFGKFIEIlldiagf 143
|
90 100
....*....|....*....|....*..
gi 261245016 642 --HKENINKLMTDLKSTAPHFVRCINP 666
Cdd:cd01363 144 eiINESLNTLMNVLRATRPHFVRCISP 170
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1017-1459 |
7.49e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1017 KLAQQIDVLEGDLERERKARMKCEREKRKLQDELKmnqegAENLESSRQKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQ 1096
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQ-----LLPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1097 KMVKELQthilNLKEELESE-RTIRAKVEREKGDLVQDLEDLNERLEEAggtslaqMEITKQQEARFQKLHHDMEETTRH 1175
Cdd:COG4717 167 ELEAELA----ELQEELEELlEQLSLATEEELQDLAEELEELQQRLAEL-------EEELEEAQEELEELEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1176 FEATSASLKKRHAENLAELEGQVEHLQQVRLVLEQDKSD----LQLQVDDLLNRVDQMARAKANAEKLCGLYERRLNEAN 1251
Cdd:COG4717 236 LEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1252 TKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLSREKsnftrqvEELRAQLEEESRsQSALSHALQSAKHDY 1331
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-------EELQLEELEQEI-AALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1332 DLLREQYEEEQEVKAELHRAlskgnKETVQwRAKYEHDAMQRTEDLEEAKKKLAIRLQEAAEAMEVSNAKNASLERARHR 1411
Cdd:COG4717 388 RAALEQAEEYQELKEELEEL-----EEQLE-ELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 261245016 1412 L-QLELGDALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQ 1459
Cdd:COG4717 462 LeQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1683-1922 |
8.12e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1683 QEQTERGRKLAEKELLEATERINLFHTQNTSLLSQKKKLEADVAQVQKEAGEMLQacqkaeekakKTAAEAANMSEELKK 1762
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ----------ELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1763 EQDTNAHLERMRKNMEQTIKDLQkRLDEAEQTAVLGSKKQIQKLESRVRDLEGELESEVRRSAEAQREARRLERGIKELT 1842
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALY-RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1843 YQAEEDKKNLSRMQALSDKLQLKVQSYKQQVEAAEAQanqylskYKKQQHELNEAKERAEAAESQVNKLRAKAKELEKKV 1922
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKE-------LAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
932-1338 |
8.63e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 932 RKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAqetqQQTQEQLHIEEEKLSNM 1011
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMK----NRYESEIKTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1012 SKANLKLAQQIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLRKKEfemgqmnsKVENEKNQ 1091
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS--------VLQKDYND 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1092 VSQLQKMVKELQTHILNLKEElesertirakvEREKGDLVQDLEDLNERLEEaggtslaqmeitkqQEARFQKLHHDMEE 1171
Cdd:PRK01156 341 YIKKKSRYDDLNNQILELEGY-----------EMDYNSYLKSIESLKKKIEE--------------YSKNIERMSAFISE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1172 TTRHFEATSASLKKRHAE---NLAELEGQVEHLQQVRLVLEQDKSDLQLQVDDLLNR----VDQMARAKANAEKLCGLYE 1244
Cdd:PRK01156 396 ILKIQEIDPDAIKKELNEinvKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpVCGTTLGEEKSNHIINHYN 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1245 RRLNEANTKLDEVTQLAHDLTTQKTKLQSesgeffkrleEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSALSHal 1324
Cdd:PRK01156 476 EKKSRLEEKIREIEIEVKDIDEKIVDLKK----------RKEYLESEEINKSINEYNKIESARADLEDIKIKINELKD-- 543
|
410
....*....|....*
gi 261245016 1325 qsaKHD-YDLLREQY 1338
Cdd:PRK01156 544 ---KHDkYEEIKNRY 555
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1375-1605 |
9.96e-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: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1375 EDLEEAKKKLAiRLQEAAEAMEVSNAKNASLERARhRLQLELGDALSDLGKARSVAAALGQKQQHSDKALTSWKQKlDET 1454
Cdd:COG3206 189 KELEEAEAALE-EFRQKNGLVDLSEEAKLLLQQLS-ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS-PVI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1455 QELLQASQKETRALSSEVLTFRqacEESTEAQEtLKRQNQDLQEQIcsltnqvregiknLAEVEKAKKLIEQEKTEVQVR 1534
Cdd:COG3206 266 QQLRAQLAELEAELAELSARYT---PNHPDVIA-LRAQIAALRAQL-------------QQEAQRILASLEAELEALQAR 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261245016 1535 LEETEGALERNESKILRFqlelseakAELERKLSEKEEEAERLREKHQQAMGSLQSnLDLEASSRIEATRL 1605
Cdd:COG3206 329 EASLQAQLAQLEARLAEL--------PELEAELRRLEREVEVARELYESLLQRLEE-ARLAEALTVGNVRV 390
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
844-984 |
1.15e-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: 43.90 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 844 KEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKSKVELEvkikelsRQVEEEEEI 923
Cdd:pfam05911 680 TEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAE-------TQLKCMAES 752
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261245016 924 NSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSL-NEEVSKLS 984
Cdd:pfam05911 753 YEDLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNeKKESSNCD 814
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1672-1925 |
1.25e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1672 LQSELEELRTLQEQTERGRKLAEKELLEATERINlfhtqntSLLSQKKKLEADVAQVQKEAGEMLQACQKAEEKAKKTAA 1751
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRD-------ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1752 EAANMSEELKKEQDTNAHLERMRKNmeqtIKDLQKRLDEAE---QTAVLGSKKQIQKLEsRVRDLEGELEsEVRRSAEAQ 1828
Cdd:COG1340 86 KLNELREELDELRKELAELNKAGGS----IDKLRKEIERLEwrqQTEVLSPEEEKELVE-KIKELEKELE-KAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1829 REARRLERGIKELTYQAEEDKKNLSRMQALSDKLQLKVQSYKQQVEAAEAQANQYLSKYKKQQHELNEAKERAEAAESQV 1908
Cdd:COG1340 160 EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
250
....*....|....*..
gi 261245016 1909 NKLRAKAKELEKKVREE 1925
Cdd:COG1340 240 RELRKELKKLRKKQRAL 256
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1568-1893 |
1.38e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.74 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1568 SEKEEEAERLREKHQQAMGSLQSNLDLEasSRIEATRLRKKMEGDLKEmEIQLCAANRQVSQMTRALG----QLQGQMKD 1643
Cdd:PLN02939 45 QQKKKRGKNIAPKQRSSNSKLQSNTDEN--GQLENTSLRTVMELPQKS-TSSDDDHNRASMQRDEAIAaidnEQQTNSKD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1644 LHQQLDdsiYQNKDLKEQVALAEQRTVLL-QSELEELRTLQeqtergRKLAEKELLEATERI---NLFHTQNTSLLSQKK 1719
Cdd:PLN02939 122 GEQLSD---FQLEDLVGMIQNAEKNILLLnQARLQALEDLE------KILTEKEALQGKINIlemRLSETDARIKLAAQE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1720 KLEADV--AQVQKEAGEMLQACQKAEEKAKKTAAE-----AANMS---------EELKKEQDTN---AHLERMRKNMEQT 1780
Cdd:PLN02939 193 KIHVEIleEQLEKLRNELLIRGATEGLCVHSLSKEldvlkEENMLlkddiqflkAELIEVAETEervFKLEKERSLLDAS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1781 IKDLQKRLDEAEQTAVLGSKKQIQKLESRVRDLEGELES---EVRRSAEAQREARRLERGIKELTYQAEEdkKNLSRMQA 1857
Cdd:PLN02939 273 LRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRatnQVEKAALVLDQNQDLRDKVDKLEASLKE--ANVSKFSS 350
|
330 340 350
....*....|....*....|....*....|....*..
gi 261245016 1858 -LSDKLQLKVQSYKQQVEAAEAQANQYLSKYKKQQHE 1893
Cdd:PLN02939 351 yKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKE 387
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1103-1348 |
1.44e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.99 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1103 QTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNERLEEaggtslaqmEITKQQ--EARFQKLHHDMEETTRH---FE 1177
Cdd:pfam00038 53 EKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED---------ELNLRTsaENDLVGLRKDLDEATLArvdLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1178 ATSASL-------KKRHAENLAELEGQVehlQQVRLVLEQDKSdLQLQVDDLLNRV-----DQMARAKANAEKlcgLYER 1245
Cdd:pfam00038 124 AKIESLkeelaflKKNHEEEVRELQAQV---SDTQVNVEMDAA-RKLDLTSALAEIraqyeEIAAKNREEAEE---WYQS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1246 RLNEANTkldEVTQLAHDLTTQKTKLQsesgEFFKRLEEKEALISQLSREKSNFTRQVEELRAQLEEE----SRSQSALS 1321
Cdd:pfam00038 197 KLEELQQ---AAARNGDALRSAKEEIT----ELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQladyQELISELE 269
|
250 260
....*....|....*....|....*..
gi 261245016 1322 HALQSAKHDYDLLREQYEEEQEVKAEL 1348
Cdd:pfam00038 270 AELQETRQEMARQLREYQELLNVKLAL 296
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1057-1238 |
1.45e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1057 AENLESSRQKLAEQLRKKefemgqmnsKVENEKNQVSQLQK-MVKELQTHILNLKEELESE-RTIRAKVEREKGDLVQDL 1134
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKR---------ILEEAKKEAEAIKKeALLEAKEEIHKLRNEFEKElRERRNELQKLEKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1135 EDLNERLEEAggtslaqmeitKQQEARFQKLHHDMEETTRHFEATSASLKKRHAENLAELEgQVEHLQQ---VRLVLEQD 1211
Cdd:PRK12704 96 ENLDRKLELL-----------EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE-RISGLTAeeaKEILLEKV 163
|
170 180
....*....|....*....|....*..
gi 261245016 1212 KSDLQLQVDDLLNRVdqMARAKANAEK 1238
Cdd:PRK12704 164 EEEARHEAAVLIKEI--EEEAKEEADK 188
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1280-1418 |
1.66e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 43.59 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1280 KRLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSALSHALQSAKHDYDLLREQYEE-----EQEVKAELHRALSK 1354
Cdd:COG1193 493 RRLGLPEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEkleelEEEKEEILEKAREE 572
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1355 GNKETVQWRAKYE------HDAMQRTEDLEEAKKKLAIRLQEAAEAMEVSNAKNASLERARhrlQLELGD 1418
Cdd:COG1193 573 AEEILREARKEAEelirelREAQAEEEELKEARKKLEELKQELEEKLEKPKKKAKPAKPPE---ELKVGD 639
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1019-1315 |
1.71e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1019 AQQIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAENLESSRQK---------LAEQLRKKEFEMgqmnSKVENEK 1089
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAEL----ERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1090 NQVSQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNERLEEAGGTS-------LAQM---------- 1152
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelralLEERfaaalgdave 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1153 -EITKQQEARFQKLHHDMEETTRHFEATSASLKKRHAENLAELEGQVEHLQQVRLVLEqdksdlQLQVDDLLNRVDQMAR 1231
Cdd:COG4913 765 rELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLD------RLEEDGLPEYEERFKE 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1232 AKANAEK-----LCGLYERRLNEANTKLDEVTQ-LAH---------DLTTQKTKLQsESGEFFKRLEEKEALISQLSREK 1296
Cdd:COG4913 839 LLNENSIefvadLLSKLRRAIREIKERIDPLNDsLKRipfgpgrylRLEARPRPDP-EVREFRQELRAVTSGASLFDEEL 917
|
330 340
....*....|....*....|
gi 261245016 1297 SN-FTRQVEELRAQLEEESR 1315
Cdd:COG4913 918 SEaRFAALKRLIERLRSEEE 937
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1551-1917 |
2.00e-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: 43.42 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1551 RFQLELSEAKAELErklsEKEEEAERLREKHQQAMGSLQSNLDLEassRIEATRLRKKMEGDLKEMEIQLCAANRQVSQM 1630
Cdd:pfam02463 153 ERRLEIEEEAAGSR----LKRKKKEALKKLIEETENLAELIIDLE---ELKLQELKLKEQAKKALEYYQLKEKLELEEEY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1631 TRALGQLqgqmKDLHQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATERINLFHTQ 1710
Cdd:pfam02463 226 LLYLDYL----KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1711 NTSLLSQKKKLEADVAQVQKEAgemlqacQKAEEKAKKTAAEAANMSEELKKEQDTNAHLERMRKNMEQtikdLQKRLDE 1790
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEK-------KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK----LQEKLEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1791 AEQTAVLGSKKQIQKLESRVRDLEGELESEVRRSAEAQREARRLERGIKELTYQAEEDKKNLSRMQALSDKLQLKVQSYK 1870
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEK 450
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 261245016 1871 QQVEAAEAQANQYLSKYKKQQHELNEAKERAEAAESQVNKLRAKAKE 1917
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1181-1313 |
2.14e-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: 41.83 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1181 ASLKKRHAENLAELEGQVEHLQQVRLVLEQDKSDLQLQVDDLLNRVDQmarAKANAEKlcglYERRLNEANTkLDEVTQL 1260
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE---VEARIKK----YEEQLGNVRN-NKEYEAL 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 261245016 1261 AHDLTTQKTKLQS---ESGEFFKRLEEKEALISQLSREKSNFTRQVEELRAQLEEE 1313
Cdd:COG1579 95 QKEIESLKRRISDledEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1499-1734 |
2.24e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1499 QICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALERNESKILRFQLELSEAKAELERKlseKEEEAERLR 1578
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER---REELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1579 ekHQQAMGSLQSNLD--LEASSrieatrlrkkmegdlkemeiqLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSIYQNK 1656
Cdd:COG3883 94 --ALYRSGGSVSYLDvlLGSES---------------------FSDFLDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261245016 1657 DLKEQVALAEQRTVLLQSELEELRTLQEQtergrklAEKELLEATERINLFHTQNTSLLSQKKKLEADVAQVQKEAGE 1734
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAE-------QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
836-1219 |
2.25e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 836 AGEEIAGLKEECAQLQKALESSESQREELKTkqvslvqEKNDLRLQLQAEQETLANSEEQCESLIKSKVEL---EVKIKE 912
Cdd:pfam05557 102 AREVISCLKNELSELRRQIQRAELELQSTNS-------ELEELQERLDLLKAKASEAEQLRQNLEKQQSSLaeaEQRIKE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 913 LSRQVEEEEEINSELTARGRKLEdECSELKKEIYDLEailaksEKGKCAAEHKVRN--LTEEVHSLNeevSKLSRVVKda 990
Cdd:pfam05557 175 LEFEIQSQEQDSEIVKNSKSELA-RIPELEKELERLR------EHNKHLNENIENKllLKEEVEDLK---RKLEREEK-- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 991 qetQQQTQEQLHIEEEKLSNMSKANLKLAQQIDVlegDLERERKARmkcEREKRKLQDELKMNQE------GAENLESSR 1064
Cdd:pfam05557 243 ---YREEAATLELEKEKLEQELQSWVKLAQDTGL---NLRSPEDLS---RRIEQLQQREIVLKEEnssltsSARQLEKAR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1065 QKLAEQLRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELES-------ERTIRAKVEREKG--DLVQDLE 1135
Cdd:pfam05557 314 RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESydkeltmSNYSPQLLERIEEaeDMTQKMQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1136 DLNERLEeaggtslAQMEITkQQEARFQKLHHDMEETTRHFEATSASLKKRH--AENLAELEGQVEHLQQVRLVLEQDKS 1213
Cdd:pfam05557 394 AHNEEME-------AQLSVA-EEELGGYKQQAQTLERELQALRQQESLADPSysKEEVDSLRRKLETLELERQRLREQKN 465
|
....*.
gi 261245016 1214 DLQLQV 1219
Cdd:pfam05557 466 ELEMEL 471
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
839-1217 |
2.37e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 839 EIAGLKEECAQLQKALESSESQREELKT------------KQVSLVQEK-----NDLRLQLQAEQETLANSEEQCESLIK 901
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKilaedeklldekKQFEKIAEElkgkeQELIFLLQAREKEIHDLEIQLTAIKT 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 902 SKVELEVKIKELSRQVEEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKsekgkcaaehkvrnlteevhslneevs 981
Cdd:pfam05483 465 SEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKK--------------------------- 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 982 klsrvvkdaqetqqqtqeqlhiEEEKLSNMSKANLKLAQQIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAEnlE 1061
Cdd:pfam05483 518 ----------------------HQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSE--E 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1062 SSRQKLAEQLrKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNERL 1141
Cdd:pfam05483 574 NARSIEYEVL-KKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKF 652
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261245016 1142 EEAGGTSLAQMEITKQQEARFQKLHHDMEETTRHFEATSASLKKRHAENLAELEGQVE-HLQQVRLVLEQDKSDLQL 1217
Cdd:pfam05483 653 EEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEkHKHQYDKIIEERDSELGL 729
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1506-1925 |
2.77e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1506 QVREGIKNLAEVEKAKKLIEQEKTEVQV--RLEETEGALERNESKILRFQLELSEAKAE-LERKLSEKEEEAERLREKHQ 1582
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWfAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1583 QAMGSLQSNLDLEASSRIEATRLRKKMEG----DLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDDSIyqnKDL 1658
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA---EEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1659 KEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATERINlfhtqntSLLSQKKKLEADVAQVQKE------- 1731
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA-------SLERRKSNIPARLLALRDAlaealgl 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1732 -------AGEMLQ-------------------------------------------------ACQKAEEKAKKTAAEAAN 1755
Cdd:COG4913 456 deaelpfVGELIEvrpeeerwrgaiervlggfaltllvppehyaaalrwvnrlhlrgrlvyeRVRTGLPDPERPRLDPDS 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1756 MSEELKKEQ--------------------DTNAHLERMRKNMEQT----------IKDLQKRLDEAeqtAVLGS--KKQI 1803
Cdd:COG4913 536 LAGKLDFKPhpfrawleaelgrrfdyvcvDSPEELRRHPRAITRAgqvkgngtrhEKDDRRRIRSR---YVLGFdnRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1804 QKLESRVRDLE---GELESEVRRSAEAQREARRLERGIKELTYQAEEDKKNLS---RMQALSDKLQL------KVQSYKQ 1871
Cdd:COG4913 613 AALEAELAELEeelAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaerEIAELEAELERldassdDLAALEE 692
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 261245016 1872 QVEAAEAQANQYLSKYKKQQHELNEAKERAEAAESQVNKLRAKAKELEKKVREE 1925
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1218-1470 |
2.83e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1218 QVDDLLNRVDQMARAKANAEKlcglyerRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLsreks 1297
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQA-------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1298 nfTRQVEELRAQLEEESRSQSALSHALQS----------------AKHDYDLLREQYEEEQEVKAElhralskgnketvq 1361
Cdd:COG3883 85 --REELGERARALYRSGGSVSYLDVLLGSesfsdfldrlsalskiADADADLLEELKADKAELEAK-------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1362 wrakyEHDAMQRTEDLEEAKKKLAIRLQEAAEAMEVSNAKNASLERARHRLQLELGDALSDLGKARSVAAALGQKQQHSD 1441
Cdd:COG3883 149 -----KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
250 260
....*....|....*....|....*....
gi 261245016 1442 KALTSWKQKLDETQELLQASQKETRALSS 1470
Cdd:COG3883 224 AAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1280-1394 |
2.96e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1280 KRLEEKEALISQLSREKSNFTRQVEELRAQLEEESRSQSALSHALQSAKHDYDLLREQYEEE-QEVKAELHRALSKGNKE 1358
Cdd:PRK00409 495 KRLGLPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKkEKLQEEEDKLLEEAEKE 574
|
90 100 110
....*....|....*....|....*....|....*...
gi 261245016 1359 TVQWR--AKYEHDAMQRTEDLEEAKKKLAIRLQEAAEA 1394
Cdd:PRK00409 575 AQQAIkeAKKEADEIIKELRQLQKGGYASVKAHELIEA 612
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
836-1415 |
3.08e-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: 42.43 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 836 AGEEIAGlKEECAQLQKALESSESQR---EELKTKQVSLVQ--EKNDLRLQLQAEQETLANSEEQCESLIKSKVELEVK- 909
Cdd:pfam07111 107 AVAEKAG-QAEAEGLRAALAGAEMVRknlEEGSQRELEEIQrlHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKr 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 910 ---IKELSRQVEEEEEINSELTARGRKLEDECS---ELKKeiYDLEAILakSEKGKCAAEHKVRNLTEEVHSLNEEVSKL 983
Cdd:pfam07111 186 ageAKQLAEAQKEAELLRKQLSKTQEELEAQVTlveSLRK--YVGEQVP--PEVHSQTWELERQELLDTMQHLQEDRADL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 984 SRVVKDAQETQQQTQEQLHIEEEKLSnmskanlKLAQQIDVLEGDLERERKARMKCEREKRKLqdelkmnqegaenless 1063
Cdd:pfam07111 262 QATVELLQVRVQSLTHMLALQEEELT-------RKIQPSDSLEPEFPKKCRSLLNRWREKVFA----------------- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1064 rqkLAEQLRKKEFEmgqmnskvenEKNQVSQLQKMVKELQTHILNLKEElesertirakvereKGDLVQDLEDLNERLE- 1142
Cdd:pfam07111 318 ---LMVQLKAQDLE----------HRDSVKQLRGQVAELQEQVTSQSQE--------------QAILQRALQDKAAEVEv 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1143 EAGGTSLAQMEITKQQEARfqklhhdmeettRHFEATSASLKKRHAENLAELEGQVEHLQQVRLVLEQDKSdlqlQVDDL 1222
Cdd:pfam07111 371 ERMSAKGLQMELSRAQEAR------------RRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVA----RIPSL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1223 LNRVDQMARakaNAEKLCGLYERRLNEANTKLDE------VTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQ---LS 1293
Cdd:pfam07111 435 SNRLSYAVR---KVHTIKGLMARKVALAQLRQEScpppppAPPVDADLSLELEQLREERNRLDAELQLSAHLIQQevgRA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1294 REKSNFTR-QVEELRAQLEEE-SRSQSALShalqSAKHDYDLLREQYEEEQEVKAELHRALSKgnKETVQWRAKYEHDAM 1371
Cdd:pfam07111 512 REQGEAERqQLSEVAQQLEQElQRAQESLA----SVGQQLEVARQGQQESTEEAASLRQELTQ--QQEIYGQALQEKVAE 585
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 261245016 1372 QRT---EDLEEAKKKLAIRLQEAAEAMevsnaknASLERARHRLQLE 1415
Cdd:pfam07111 586 VETrlrEQLSDTKRRLNEARREQAKAV-------VSLRQIQHRATQE 625
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
838-1170 |
3.26e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 838 EEIAGLKEECAQLQKALESSESQREELKTKQVSL--VQEKNDLRLQLQAEQETLANSEEQCESLIKSKVELEvkikelsr 915
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIAELEAELERLDASSDDLA-------- 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 916 qveeeeeinseltargrkledecsELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVkDAQETQQ 995
Cdd:COG4913 689 ------------------------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL-EAAEDLA 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 996 QTQEQLHIEEEKLSNMSKANLK-----LAQQIDVLEGDLERERKARMKCERE-KRKLQDELKMNQEGAENLESSRQKLAE 1069
Cdd:COG4913 744 RLELRALLEERFAAALGDAVERelrenLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLDR 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1070 QLR------KKEFEmGQMNSKVENEKNQ-VSQLQKMVKELQTHILNLKEELE-----SERTIRAKVEREKgdlVQDLEDL 1137
Cdd:COG4913 824 LEEdglpeyEERFK-ELLNENSIEFVADlLSKLRRAIREIKERIDPLNDSLKripfgPGRYLRLEARPRP---DPEVREF 899
|
330 340 350
....*....|....*....|....*....|...
gi 261245016 1138 NERLEEAggTSLAQMEITKQQEARFQKLHHDME 1170
Cdd:COG4913 900 RQELRAV--TSGASLFDEELSEARFAALKRLIE 930
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
824-1239 |
3.49e-03 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 42.14 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 824 FFKIKPLAKSvgAGEEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKS- 902
Cdd:COG4477 99 FKKAKKALDE--IEQLLDEIEEEIEEILEELEELLESEEKNREEIEELKEKYRELRKTLLAHRHSFGPAAEELEKQLEEl 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 903 ----------------------KVELEVKIKELSRQVEE----EEEINSELTARGRKLEDECSELKKEIYDLEAIlakse 956
Cdd:COG4477 177 epefeefeeltesgdyleareiLEQLEEELNALEELMEEipplLKELQTELPDQLEELKSGYREMKEQGYVLEHL----- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 957 kgkcaaehkvrNLTEEVHSLNEEVSKLSRvvkdaqetqqqtqeqlHIEEEKLSNMSKANLKLAQQIDVLEGDLERERKAR 1036
Cdd:COG4477 252 -----------NIEKEIEQLEEQLKEALE----------------LLEELDLDEAEEELEEIEEEIDELYDLLEKEVEAK 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1037 MKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLrkkefemgQMNskvENEKNQVSQLQKMVKELQTHILNLKEELESE 1116
Cdd:COG4477 305 KYVDKNQEELEEYLEHLKEQNRELKEEIDRVQQSY--------RLN---ENELEKVRNLEKQIEELEKRYDEIDERIEEE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1117 RTIRAKVEREKGDLVQDLEDLNERLEEAGGT--SLAQMEITKQQEArfQKLHHDMEETTRHfeatsasLKKRH-----AE 1189
Cdd:COG4477 374 KVAYSELQEELEEIEEQLEEIEEEQEEFSEKlkSLRKDELEAREKL--DELKKKLREIKRR-------LEKSNlpglpEE 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 261245016 1190 NLAELEGQVEHLQQVRLVLEQDKSDLQlQVDDLLNRV-DQMARAKANAEKL 1239
Cdd:COG4477 445 YLEMFEEASDEIEELSEELNEVPLNMD-EVNRLLEEAeEDIETLEEKTEEL 494
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
831-1070 |
3.62e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 831 AKSVGAGEEIAGLKEECAQLQKALESSESQREELKTKQVSLvqeknDLRLQLQAEQETLANSEEQCESLIKSKVELEVKI 910
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 911 KELSRQVEEEEEINSELTArgrklEDECSELKKEIYDLEAILAKsEKGKCAAEH-KVRNLTEEVHSLNEEVSKLSRVVKD 989
Cdd:COG3206 243 AALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAE-LSARYTPNHpDVIALRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 990 AqetqqqtqeqlhIEEEKLSNMSKANlKLAQQIDVLEGDLERERKArmkcEREKRKLQDELKMNQEGAENLESSRQKLAE 1069
Cdd:COG3206 317 S------------LEAELEALQAREA-SLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYESLLQRLEEARL 379
|
.
gi 261245016 1070 Q 1070
Cdd:COG3206 380 A 380
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1411-1695 |
3.71e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1411 RLQLELGDALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEVLTFRQACEESTEAQETLK 1490
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1491 RQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALERNESKILRFQLElsEAKAELERKLSEK 1570
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD--ELLKEANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1571 EEEAERLREKHQQAMGSLQSNLDLEASSRIEATRLRKKMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDLHQQLDD 1650
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 261245016 1651 SIYQNKDLKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEK 1695
Cdd:COG4372 280 IAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1243-1706 |
3.76e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.20 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1243 YERRLNEANTKLDEVTQLAHDLTTQKTKLQSesgeffkrleekealISQLSREKSNFTRQVEELRAQLEEESRSQSALSH 1322
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDE---------------LEALIDQWLAELEQVIALRRAGGLEAALALVRSG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1323 ALQSAKHDYDLLREQYEEEQEVKAELHRALSKGNKETVQWRAKYEHDAMQRTEDLEEAKKKLAIRlQEAAEAMEVSNAKN 1402
Cdd:COG5278 146 EGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLE-AELAAAAALLAAAA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1403 ASLERARHRLQLELGDALSDLGKARSVAAALGQKQQHSDKALTSWKQKLDETQELLQASQKETRALSSEVLTFRQACEES 1482
Cdd:COG5278 225 ALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELEL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1483 TEAQETLKRQNQDLQEQICSLTNQVREGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALERNESKILRFQLELSEAKAE 1562
Cdd:COG5278 305 ELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1563 LERKLSEKEEEAERLREKHQQAMGSLQSNLDLEASSRIEATRLRKKMEGDLKEMEIQLCAANRQVSQMTRALGQLQGQMK 1642
Cdd:COG5278 385 AEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEAL 464
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261245016 1643 DLHQQLDDSIYQNKDLKEQVALAEQRTVLLQSELEELRTLQEQTERGRKLAEKELLEATERINL 1706
Cdd:COG5278 465 AEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASA 528
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1431-1686 |
4.28e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1431 AALGQKQQHSDKALTSWKQKLDETQELLQASQKETRA----LSSEVLTFRQACEESTEAQETLKRQNQDLQEQICSLTNQ 1506
Cdd:pfam07888 44 AELLQAQEAANRQREKEKERYKRDREQWERQRRELESrvaeLKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1507 VREGIKNLAEVEKAKKLIEQEKTEVQVRLEEtegaLERNESKILRFQLELSEAKAELERKLSEKEEEAERLREKHQQAMG 1586
Cdd:pfam07888 124 RAAHEARIRELEEDIKTLTQRVLERETELER----MKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1587 SLqsnldleASSRIEATRLRKkmegDLKEMEIQLCAANRQVSQMTRALGQLQGqmkdlhqqlddsiyqnkdLKEQVALAE 1666
Cdd:pfam07888 200 SL-------AQRDTQVLQLQD----TITTLTQKLTTAHRKEAENEALLEELRS------------------LQERLNASE 250
|
250 260
....*....|....*....|
gi 261245016 1667 QRTVLLQSELEELRTLQEQT 1686
Cdd:pfam07888 251 RKVEGLGEELSSMAAQRDRT 270
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1508-1794 |
4.37e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1508 REGIKNLAEVEKAKKLIEQEKTEVQVRLEETEGALErnesKILRFQLELSEAKAELE---RKLSEKEEEAERLREKHQQA 1584
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLD----KIDRQKEETEQLKQQLAqapAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1585 MGSLQSNLDLEA-SSRIEATRlrkkmeGDLKEMEIQLCAANRQ-VSQMTR------ALGQLQGQMKDLHQQLDDSIYQNK 1656
Cdd:PRK11281 114 TRETLSTLSLRQlESRLAQTL------DQLQNAQNDLAEYNSQlVSLQTQperaqaALYANSQRLQQIRNLLKGGKVGGK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1657 DLK---------EQVALaEQRTVLLQSELEELRTLQEqtergrkLAEKELLEATERINLFHTQNTSL---LSQKKklead 1724
Cdd:PRK11281 188 ALRpsqrvllqaEQALL-NAQNDLQRKSLEGNTQLQD-------LLQKQRDYLTARIQRLEHQLQLLqeaINSKR----- 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261245016 1725 VAQVQKEAGEMLQAcqkaeekakkTAAEAANMSEELKKEQDTNAHL--------ERMRKNMEQTIKdLQKRLDEAEQT 1794
Cdd:PRK11281 255 LTLSEKTVQEAQSQ----------DEAARIQANPLVAQELEINLQLsqrllkatEKLNTLTQQNLR-VKNWLDRLTQS 321
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
838-1703 |
4.38e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 838 EEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKND----LRLQLQA--EQETLANSEEQCEslikskvELEVKIK 911
Cdd:COG3096 292 RELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAasdhLNLVQTAlrQQEKIERYQEDLE-------ELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 912 ELSRQVEEEEEINSELTARGRKLEDECSELKKEIYDL---------------EAILAKSE-KGKCAAEH-KVRNLTEEVH 974
Cdd:COG3096 365 EQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYqqaldvqqtraiqyqQAVQALEKaRALCGLPDlTPENAEDYLA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 975 SLNEEVSKLSRVVKDAqetqqqtqeqlhieEEKLSNMSKANLKLAQQIDVLE---GDLERER---KAR--MKCEREKRKL 1046
Cdd:COG3096 445 AFRAKEQQATEEVLEL--------------EQKLSVADAARRQFEKAYELVCkiaGEVERSQawqTARelLRRYRSQQAL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1047 qdelkmnqegAENLESSRQKLAEqLRKKEFEMgqmnskvENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVERE 1126
Cdd:COG3096 511 ----------AQRLQQLRAQLAE-LEQRLRQQ-------QNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQ 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1127 KGDLVQDLEDLNERLEEAGgtslAQMEITKQQE----ARFQKLHHDMEETTRHFEATSA--SLKKRHAENLAELEGQVEH 1200
Cdd:COG3096 573 AAEAVEQRSELRQQLEQLR----ARIKELAARApawlAAQDALERLREQSGEALADSQEvtAAMQQLLEREREATVERDE 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1201 LQQVRLVLEQDKSDLQLQVDDLLNRVDQMARaKANAEKLCGLYE-----------------------RRLNEANTKLDEV 1257
Cdd:COG3096 649 LAARKQALESQIERLSQPGGAEDPRLLALAE-RLGGVLLSEIYDdvtledapyfsalygparhaivvPDLSAVKEQLAGL 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1258 TQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLSREKSNFTR--------------QVEELRAQLEEESRsqsalsha 1323
Cdd:COG3096 728 EDCPEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSDRQWRYSRfpevplfgraarekRLEELRAERDELAE-------- 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1324 lQSAKHDYDLLREQyeeeqevkaELHRALSkgnketvQWRAKYEHDAMQrtEDLEEAKKKLAIRLQEAAEAMEVSNAKNa 1403
Cdd:COG3096 800 -QYAKASFDVQKLQ---------RLHQAFS-------QFVGGHLAVAFA--PDPEAELAALRQRRSELERELAQHRAQE- 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1404 slerARHRLQLE-LGDALSDLGKARSVAAALgQKQQHSDKaLTSWKQKLDETQELLQASQKETRALsSEVLTFRQACEES 1482
Cdd:COG3096 860 ----QQLRQQLDqLKEQLQLLNKLLPQANLL-ADETLADR-LEELREELDAAQEAQAFIQQHGKAL-AQLEPLVAVLQSD 932
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1483 TEAQETLKRQNQDLQEQIcsltNQVREGIKNLAEVekakklieqekteVQVRL----EETEGALERNEskilrfqlELSE 1558
Cdd:COG3096 933 PEQFEQLQADYLQAKEQQ----RRLKQQIFALSEV-------------VQRRPhfsyEDAVGLLGENS--------DLNE 987
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1559 AkaeLERKLSEKEEEAERLREKHQQAMGSLQSNLDLEA---SSRIEATRLRKKMEGDLKEMEIQLCAAnrqvsqmtrALG 1635
Cdd:COG3096 988 K---LRARLEQAEEARREAREQLRQAQAQYSQYNQVLAslkSSRDAKQQTLQELEQELEELGVQADAE---------AEE 1055
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261245016 1636 QLQGQMKDLHQQLDdsiyQNKDLKEQvaLAEQRTVlLQSELEELRTLQEQTERGRKLAEKELLEATER 1703
Cdd:COG3096 1056 RARIRRDELHEELS----QNRSRRSQ--LEKQLTR-CEAEMDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1017-1164 |
4.65e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1017 KLAQQIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLrkkefeMGQMNSK-VENEKNQVSQL 1095
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL------GNVRNNKeYEALQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261245016 1096 QKMVKELQTHILNLKEELESERTIRAKVEREKGDLVQDLEDLNERLEEAGGTSLAQMEITKQQEARFQK 1164
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1251-1576 |
4.80e-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: 41.92 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1251 NTKLDEV-TQLAHDLTTQKTKlqSESGEFFKRLEEKEALISQLSREKSNFTRQVEELRAQLEEesrsqsalshALQSAKH 1329
Cdd:NF033838 90 NKKLSDIkTEYLYELNVLKEK--SEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEE----------AEKKAKD 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1330 DYDLLREQYEEEQEVKAELHRALS-----KGNKETVQWRAKYEHDamqrTEDLEEAKKKLAIRLQEAAEAMEVSNAKNAS 1404
Cdd:NF033838 158 QKEEDRRNYPTNTYKTLELEIAESdvevkKAELELVKEEAKEPRD----EEKIKQAKAKVESKKAEATRLEKIKTDREKA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1405 LERARHRLQLELGDALSDLG--------KARSVAAALGQkQQHSDKALTSWKQkldetqellQASQKETRALSSEVLTFR 1476
Cdd:NF033838 234 EEEAKRRADAKLKEAVEKNVatseqdkpKRRAKRGVLGE-PATPDKKENDAKS---------SDSSVGEETLPSPSLKPE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1477 QACEESTEAQETLKRQNQDLQEQicSLTNQVREGIKNLaEVEKAKKLIEQEKTEVQVRLEETEGAleRNESKILRFQLEL 1556
Cdd:NF033838 304 KKVAEAEKKVEEAKKKAKDQKEE--DRRNYPTNTYKTL-ELEIAESDVKVKEAELELVKEEAKEP--RNEEKIKQAKAKV 378
|
330 340
....*....|....*....|....*.
gi 261245016 1557 SEAKAELER------KLSEKEEEAER 1576
Cdd:NF033838 379 ESKKAEATRlekiktDRKKAEEEAKR 404
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1161-1589 |
5.19e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1161 RFQKLHHDMEE-TTRHF--------EATSASLKKRHAENLAELEGQVEHLQQVRLVLEQDKSDLQlqvddLLNRVdqmar 1231
Cdd:COG3096 810 KLQRLHQAFSQfVGGHLavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQ-----LLNKL----- 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1232 akanaeklcglyerrLNEANTKLDEVTQlahdlttqktklqsesgeffKRLEEKEALISQLSrEKSNFTRQVEELRAQLE 1311
Cdd:COG3096 880 ---------------LPQANLLADETLA--------------------DRLEELREELDAAQ-EAQAFIQQHGKALAQLE 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1312 EesrsqsaLSHALQSAKHDYDLLREQYEEEQEVKAELHR---ALSkgnkETVQWRakyEHDAMQRTEDLEEAKKKLAIRL 1388
Cdd:COG3096 924 P-------LVAVLQSDPEQFEQLQADYLQAKEQQRRLKQqifALS----EVVQRR---PHFSYEDAVGLLGENSDLNEKL 989
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1389 QEAAEAMEvsnaknasLERARHRLQLElgdalsdlgkarsvaaalGQKQQHSD--KALTSWKQKLDETQELLQASQKETR 1466
Cdd:COG3096 990 RARLEQAE--------EARREAREQLR------------------QAQAQYSQynQVLASLKSSRDAKQQTLQELEQELE 1043
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1467 ALSSEVltfrqaceeSTEAQETLKRQNQDLQEQICSLTNQvregiknLAEVEKAKKLIEQEKTEVQVRLEETEgalerNE 1546
Cdd:COG3096 1044 ELGVQA---------DAEAEERARIRRDELHEELSQNRSR-------RSQLEKQLTRCEAEMDSLQKRLRKAE-----RD 1102
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 261245016 1547 SKILRFQLElsEAKAE------------LERKLSEKE---EEAERLREKHQQAMGSLQ 1589
Cdd:COG3096 1103 YKQEREQVV--QAKAGwcavlrlardndVERRLHRRElayLSADELRSMSDKALGALR 1158
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1478-1610 |
5.26e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 41.93 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1478 ACEESTEAQETLKRQNQDLQEQICS--LTNQVregIKNLAEVEKAK-KLIEQE--KTEVQVRLEETEGALERNESKILRF 1552
Cdd:PTZ00491 656 AIEITTKSQEAAARHQAELLEQEARgrLERQK---MHDKAKAEEQRtKLLELQaeSAAVESSGQSRAEALAEAEARLIEA 732
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261245016 1553 QLELSEAKAELERKLSEKEEEAERLREKHQQAMGSLQSNLDLE-----ASSRIEATRLRKKME 1610
Cdd:PTZ00491 733 EAEVEQAELRAKALRIEAEAELEKLRKRQELELEYEQAQNELEiakakELADIEATKFERIVE 795
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1191-1363 |
5.41e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1191 LAELEGQVEHLQQVrLVLEQD-KSDLQLQVDDLLNRVDQmarAKANAEKLCGLYerrlneantklDEVTQLAHDLTTQKT 1269
Cdd:PRK09039 55 LDRLNSQIAELADL-LSLERQgNQDLQDSVANLRASLSA---AEAERSRLQALL-----------AELAGAGAAAEGRAG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1270 KLQSEsgeffkrLEEKEALISQLSREKSNFTRQVEELRAQLeeesrsqSALSHALQSAkhdydllrEQYEEEQEVKAE-- 1347
Cdd:PRK09039 120 ELAQE-------LDSEKQVSARALAQVELLNQQIAALRRQL-------AALEAALDAS--------EKRDRESQAKIAdl 177
|
170
....*....|....*....
gi 261245016 1348 ---LHRALSKGNKETVQWR 1363
Cdd:PRK09039 178 grrLNVALAQRVQELNRYR 196
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1001-1812 |
6.02e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1001 LHIEEEKLSNMSKanlKLAQQIDvLEGDLERERKA---RMKCEREKRKLQDELKMNQEGAENLE-------SSRQKLAEQ 1070
Cdd:PRK04863 302 LAAEQYRLVEMAR---ELAELNE-AESDLEQDYQAasdHLNLVQTALRQQEKIERYQADLEELEerleeqnEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1071 LRKKEFEMGQMNSKVENEKNQVSQLQKMVKELQTHIL---NLKEELESERTIRAKVEREKGDLVQDLEDLNERLEEAGGT 1147
Cdd:PRK04863 378 QEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIqyqQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1148 SLA---QMEITKQQEARFQKLhhdMEETTRHFEATSASLKKRHA-ENLAELEGQVEHLQQVrlvleqdkSDLQLQVDDLL 1223
Cdd:PRK04863 458 LLSleqKLSVAQAAHSQFEQA---YQLVRKIAGEVSRSEAWDVArELLRRLREQRHLAEQL--------QQLRMRLSELE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1224 NRVDQMARAKANAEKLCGLYERRLNEAntklDEVTQLAhdlttqktklqsesgeffkrlEEKEALISQLSREKSNFTRQV 1303
Cdd:PRK04863 527 QRLRQQQRAERLLAEFCKRLGKNLDDE----DELEQLQ---------------------EELEARLESLSESVSEARERR 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1304 EELRAQLEE------ESRSQSALSHALQSAkhdYDLLREQYEEEQEVKAELhralskgnKETVQWRAKYEHDAMQRTEDL 1377
Cdd:PRK04863 582 MALRQQLEQlqariqRLAARAPAWLAAQDA---LARLREQSGEEFEDSQDV--------TEYMQQLLERERELTVERDEL 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1378 EEAKKKLairlqeAAEAMEVSNAKNASLERARH---RL----------QLELGDA---------------LSDLGKARSV 1429
Cdd:PRK04863 651 AARKQAL------DEEIERLSQPGGSEDPRLNAlaeRFggvllseiydDVSLEDApyfsalygparhaivVPDLSDAAEQ 724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1430 AAAL-----------GQKQQHSDKALTSWKQKLDETQELLQASQKETRaLSSEVLTFRQACEESTEAqetLKRQNQDLQE 1498
Cdd:PRK04863 725 LAGLedcpedlylieGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSR-FPEVPLFGRAAREKRIEQ---LRAEREELAE 800
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1499 QICSLTnqvregiknlAEVEKAKKLIEQEKTEVQVRLEEtegALERNESKILRfqlELSEAKAELERKLSEKEEEAERLR 1578
Cdd:PRK04863 801 RYATLS----------FDVQKLQRLHQAFSRFIGSHLAV---AFEADPEAELR---QLNRRRVELERALADHESQEQQQR 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1579 EKHQQAMGSLQSNLDLEASSRI-EATRLRKKMEgDLKEMEIQLCAANRQVSQMTRALGQLQGQMKDL------HQQLDDS 1651
Cdd:PRK04863 865 SQLEQAKEGLSALNRLLPRLNLlADETLADRVE-EIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLqsdpeqFEQLKQD 943
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1652 IYQNKDLKEQV-----ALAE-------------QRTVLLQSEL-EELRTLQEQTERGRKLAEKELLEATERINLFHTQNT 1712
Cdd:PRK04863 944 YQQAQQTQRDAkqqafALTEvvqrrahfsyedaAEMLAKNSDLnEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLA 1023
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1713 SLLSQKKKLEADVAQVQKEAGEM-LQACQKAEEKAKKTAAEaanMSEELKKEQDTNAHLERMRKNMEQTIKDLQKRLDEA 1791
Cdd:PRK04863 1024 SLKSSYDAKRQMLQELKQELQDLgVPADSGAEERARARRDE---LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKL 1100
|
890 900
....*....|....*....|....*..
gi 261245016 1792 E------QTAVLGSKKQIQKLESRVRD 1812
Cdd:PRK04863 1101 ErdyhemREQVVNAKAGWCAVLRLVKD 1127
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1700-1891 |
6.65e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1700 ATERINLFHTQNTSLLSQKKKLEADVAQVQKEAGEMLQACQKAEEKAKKTAAEAANMSEELKKeqdTNAHLERMRKNMEQ 1779
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE---AEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1780 TIKDLQKRLDEAEQ-TAVLGSK---------KQIQKLESRVRDLEGELESEVRRSAEAQREARRLERGIKELTYQAEEDK 1849
Cdd:COG3883 91 RARALYRSGGSVSYlDVLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 261245016 1850 KNL----SRMQALSDKLQLKVQSYKQQVEAAEAQANQYLSKYKKQQ 1891
Cdd:COG3883 171 AELeaqqAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1245-1588 |
6.83e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1245 RRLNEANTKL----DEVTQLAHDLTTQKTKLQSesgeffkrLEEKEALISQLSREksNFTRQVEELRAQLEEES------ 1314
Cdd:PRK04863 844 RRRVELERALadheSQEQQQRSQLEQAKEGLSA--------LNRLLPRLNLLADE--TLADRVEEIREQLDEAEeakrfv 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1315 -RSQSALSH------ALQSAKHDYDLLREQYEEEQEVKAELH---RALSkgnkETVQWRA--KYEhDAMQRTEDLEEAKK 1382
Cdd:PRK04863 914 qQHGNALAQlepivsVLQSDPEQFEQLKQDYQQAQQTQRDAKqqaFALT----EVVQRRAhfSYE-DAAEMLAKNSDLNE 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1383 KLAIRLqEAAEAMevsnaknasLERARHRLQlelgdalsdlgkarsvaaalGQKQQHSD--KALTSWKQKLDETQELLQA 1460
Cdd:PRK04863 989 KLRQRL-EQAEQE---------RTRAREQLR--------------------QAQAQLAQynQVLASLKSSYDAKRQMLQE 1038
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1461 SQKETRALSSevltfrQACEestEAQETLKRQNQDLQEQICslTNQVREgiknlAEVEKAKKLIEQEKTEVQVRLEETEg 1540
Cdd:PRK04863 1039 LKQELQDLGV------PADS---GAEERARARRDELHARLS--ANRSRR-----NQLEKQLTFCEAEMDNLTKKLRKLE- 1101
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261245016 1541 alerNESKILRFQLElsEAKA------------ELERKLsEKEE----EAERLREKHQQAMGSL 1588
Cdd:PRK04863 1102 ----RDYHEMREQVV--NAKAgwcavlrlvkdnGVERRL-HRRElaylSADELRSMSDKALGAL 1158
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1061-1582 |
7.16e-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: 41.35 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1061 ESSRQKLAEQLRKKEFEMgQMNSKVENEKNQVSQLQKMVKELQTHIlnlkeelESERTIRAKVEREKGDLVQDLEDLN-- 1138
Cdd:pfam10174 191 EMQLGHLEVLLDQKEKEN-IHLREELHRRNQLQPDPAKTKALQTVI-------EMKDTKISSLERNIRDLEDEVQMLKtn 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1139 ------ERLEEaggtsLAQMEITKQQeARFQK-----LHHDMEETTRHFEATSASLKKRHAENlAELEGQVEHLQQVRLV 1207
Cdd:pfam10174 263 gllhteDREEE-----IKQMEVYKSH-SKFMKnkidqLKQELSKKESELLALQTKLETLTNQN-SDCKQHIEVLKESLTA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1208 LEQDKSDLQLQVDDLLNRvdqmarakanaeklcglyerrLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEA 1287
Cdd:pfam10174 336 KEQRAAILQTEVDALRLR---------------------LEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKER 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1288 LISQLSreksnftRQVEELRAQLEEESRSQSALSHALQSakhdydlLREQYEEEQEVKAELHRALSKGNKETVQWRAKYE 1367
Cdd:pfam10174 395 KINVLQ-------KKIENLQEQLRDKDKQLAGLKERVKS-------LQTDSSNTDTALTTLEEALSEKERIIERLKEQRE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1368 HDAMQRTEDLEEAKKKLAIrLQEAAEAMEVSNA-KNASLERARHRLQLELGDALSDLGKARSVAAALGQKQQHSDKALTS 1446
Cdd:pfam10174 461 REDRERLEELESLKKENKD-LKEKVSALQPELTeKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQ 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1447 WK--QKLDETQELLQASQKETRALSSEVLTFRqacEESTEAQETLKR----------QNQDLQEQICSLTNQVREGIKNL 1514
Cdd:pfam10174 540 LKkaHNAEEAVRTNPEINDRIRLLEQEVARYK---EESGKAQAEVERllgilrevenEKNDKDKKIAELESLTLRQMKEQ 616
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261245016 1515 AEVEKAKKLIEQEKTEVQVRLEEtEGALERNESKILRFQLELSEAKAELERKLSEKEEEAERLREKHQ 1582
Cdd:pfam10174 617 NKKVANIKHGQQEMKKKGAQLLE-EARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1156-1393 |
7.83e-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: 41.26 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1156 KQQEARFQKLhhDMEETTRHFEATSASLKKRHAENLAELEGQVEHLQQVRLVLEQDKsdLQLQVDDLLNRVDQMARAKAN 1235
Cdd:pfam17380 287 RQQQEKFEKM--EQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQER--MAMERERELERIRQEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1236 AEklcgLYERRLNEANTKLDEVT--QLAHDLTTQKTKLQSESGEFFKRLE-EKEALISQLSREKSNFTRQVEELRAQ--- 1309
Cdd:pfam17380 363 ER----IRQEEIAMEISRMRELErlQMERQQKNERVRQELEAARKVKILEeERQRKIQQQKVEMEQIRAEQEEARQRevr 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1310 -LEEE-SRSQSALSHALQSAKHDYDLLREQYEEEQEVKAELHRALSKGNKETVQWRAKYEHDAMQRTEDLEEAKKKLAIR 1387
Cdd:pfam17380 439 rLEEErAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLL 518
|
....*.
gi 261245016 1388 LQEAAE 1393
Cdd:pfam17380 519 EKEMEE 524
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
876-1412 |
7.98e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 876 NDLRLQLQAEQETLANSEEQCESLIKSKVELEVKIKELSRQVEEEEEINSELTARGRKLedecSELKKEIYDLEAILAKS 955
Cdd:PRK01156 186 DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNEL----SSLEDMKNRYESEIKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 956 EKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQQTQEQLHIEEEKLSNMSKANLKLAQQIDVLEgDLERERKA 1035
Cdd:PRK01156 262 ESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDYND 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1036 RMKCEREKRKLQDEL------KMNQEGAENLESSRQKLAEQLRKKEFEMGQMNSKVENEKN-QVSQLQKMVKELQTHILN 1108
Cdd:PRK01156 341 YIKKKSRYDDLNNQIlelegyEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEiDPDAIKKELNEINVKLQD 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1109 LKEELESertirakVEREKGDLVQDLEDLNERLEEAGGTSLAQMEITKQQEARFQKLHHD-------MEETTRHFEATSA 1181
Cdd:PRK01156 421 ISSKVSS-------LNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHynekksrLEEKIREIEIEVK 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1182 SL--KKRHaenLAELEGQVEHLQQVRLVLEQDK-SDLQLQVDDLLNRVDQMARAKANAEKLCGLY--------------- 1243
Cdd:PRK01156 494 DIdeKIVD---LKKRKEYLESEEINKSINEYNKiESARADLEDIKIKINELKDKHDKYEEIKNRYkslkledldskrtsw 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1244 ---------------ERRLNEANTKLDEVTQLAHDLTTQKTKLQSESGEFFKRLEEKEALISQLSREKSNFTRQVEELRA 1308
Cdd:PRK01156 571 lnalavislidietnRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRG 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1309 QLeEESRSQSALSHALQSAKHDydlLREQYEEEQEVKAELHRALSKGNKETVQWRAKYEHDaMQRTEDLEEAKKKLAIRL 1388
Cdd:PRK01156 651 KI-DNYKKQIAEIDSIIPDLKE---ITSRINDIEDNLKKSRKALDDAKANRARLESTIEIL-RTRINELSDRINDINETL 725
|
570 580
....*....|....*....|....
gi 261245016 1389 qeaaEAMEVSNAKNASLERARHRL 1412
Cdd:PRK01156 726 ----ESMKKIKKAIGDLKRLREAF 745
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
836-1181 |
9.35e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 836 AGEEIAGLKEECAQLQKALESSESQREELKTKQVSLVQEKNDLRLQLQAEQETLANSEEQCESLIKSKVELEVKIKELSR 915
Cdd:COG4372 22 TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 916 QVEEEEEINSELTARGRKLEDECSELKKEIYDLEAILAKSEKGKCAAEHKVRNLTEEVHSLNEEVSKLSRVVKDAQETQQ 995
Cdd:COG4372 102 ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 996 QTQEQLHIEEEKLSNMSKANLKLAQQIDVLEGDLERERKARMKCEREKRKLQDELKMNQEGAENLESSRQKLAEQLRKKE 1075
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245016 1076 FEMGQMNSKVENEKNQVSQLQKMVKELQTHILNLKEELESERTIRAKVERE-KGDLVQDLEDLNERLEEAGGTSLAQMEI 1154
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGAlEDALLAALLELAKKLELALAILLAELAD 341
|
330 340
....*....|....*....|....*..
gi 261245016 1155 TKQQEARFQKLHHDMEETTRHFEATSA 1181
Cdd:COG4372 342 LLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| |
