|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
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: 1461.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 658
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 1335178301 739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-771 |
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: 1336.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP-GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKkGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYR-FLSNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 337 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 416
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 417 ADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 497 EEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK-FQKPRQLKDKADF 575
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRivgldqvtgmtETAFGSAYKTKKGMFRTVGQ 655
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 656 LYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 1335178301 736 IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01377 627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-771 |
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: 1245.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP----GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD 574
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGsAYKTKKGMFRTVG 654
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHG-AFKTRKGMFRTVG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14932 560 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 1335178301 735 AIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14932 640 AIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
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: 1218.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14919 318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 658
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14919 558 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 1335178301 739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14919 638 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-771 |
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: 1214.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 658
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 1335178301 739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-771 |
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: 1195.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHN----IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD 574
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTEtaFGSAYKTKKGMFRTVG 654
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*..
gi 1335178301 735 AIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd15896 639 AIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-771 |
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: 1174.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVASS---------HKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 249
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 250 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 329
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 330 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 409
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 410 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 490 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKpRQL 569
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 570 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrIVGLDQVTgMTETAFGSayKTKKGM 649
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA--RTRKGM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 650 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14911 553 FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1335178301 730 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14911 633 LLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 1160.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQdKDNFQETMEAMHIMGF 338
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSayKTKKGMFRTVGQLYK 658
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG--RPRRGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14930 558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 1335178301 739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14930 638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-771 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1120.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 87 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFI 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSA----GNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 247 RINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSN-GYIPIPGQQDKDN 325
Cdd:pfam00063 157 EIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTIDGIDDSEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 326 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 405
Cdd:pfam00063 237 FKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:pfam00063 317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQK 565
Cdd:pfam00063 397 FFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 566 PRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETafgsAYKT 645
Cdd:pfam00063 474 PRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKST----PKRT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 646 KKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1335178301 726 QRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:pfam00063 629 QRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
840-1674 |
0e+00 |
|
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: 1107.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 840 KVKPLLQVTRQEEELQAKDEELLKVKEKQ--------TKVEGELEEM------------ERKHQQAR-----ATAEAGGD 894
Cdd:pfam01576 174 KAKSLSKLKNKHEAMISDLEERLKKEEKGrqelekakRKLEGESTDLqeqiaelqaqiaELRAQLAKkeeelQAALARLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 895 DETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQEL------------ 962
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELrskreqevtelk 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 963 ------------------------------------RFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQ 1006
Cdd:pfam01576 334 kaleeetrsheaqlqemrqkhtqaleelteqleqakRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQ 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1007 VQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNLSSRIRQ 1086
Cdd:pfam01576 414 LQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1087 LEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEK 1166
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1167 TKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKE 1246
Cdd:pfam01576 574 TKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKE 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1247 EFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDL 1326
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDL 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1327 QTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRE 1406
Cdd:pfam01576 734 QARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRE 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1407 LEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1486
Cdd:pfam01576 814 LEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQ 893
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1487 LEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALE 1566
Cdd:pfam01576 894 LEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALE 973
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1567 AKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASR 1646
Cdd:pfam01576 974 AKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAAR 1053
|
890 900
....*....|....*....|....*...
gi 1335178301 1647 RKLQRELDDATEANEGLSREVSTLKNRL 1674
Cdd:pfam01576 1054 RKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-783 |
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: 1025.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 80 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 160 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRkdhnipGELERQLLQANPILESFGNAKTVKNDNS 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 240 SRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIP 318
Cdd:smart00242 155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGgCLTVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 319 GQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENT-VAQKLCHLLGMNVMEFTRAIL 397
Cdd:smart00242 235 GIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 398 TPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCIN 477
Cdd:smart00242 315 KRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFEVNSFEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 478 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQ 557
Cdd:smart00242 394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 558 GSHSKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivgldqvtgmtet 637
Cdd:smart00242 471 KKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS---------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 638 afGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 717
Cdd:smart00242 534 --GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPY 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1335178301 718 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERD 783
Cdd:smart00242 612 RLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1477 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 941.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 36 VWIPSERHGFEAASIKEERGDEVMVELA---ENGKKAMVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKDRYY 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 111 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 191 VIQYLAHVASSHkgrkdHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSR 270
Cdd:COG5022 172 IMQYLASVTSSS-----TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 271 AVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP-IPGQQDKDNFQETMEAMHIMGFSHEEILSMLKV 349
Cdd:COG5022 247 VVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 350 VSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATY 429
Cdd:COG5022 327 LAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 430 ERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI 509
Cdd:COG5022 406 SNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 510 DFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVEKLVQ--EQGSHSKFQKPRQLKDKadFCIIHYAGKVDYK 587
Cdd:COG5022 485 DY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHYAGDVEYD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 588 ADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVgldqvtgmtetafgsayktKKGMFRTVGQLYKESLTKLMAT 667
Cdd:COG5022 561 VEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPTLGSRFKESLNSLMST 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 668 LRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA----IPKGFMDG 743
Cdd:COG5022 622 LNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDT 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 744 KQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIIFFQAVCRGYLARKAFAKKQQQLSALKVLQRNC 823
Cdd:COG5022 702 KNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGF 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 824 AAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEEL--LKVKEKQTKVEGELEEMERKHQQARATAEAGGDDETLHKN 901
Cdd:COG5022 782 RLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIikLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRF 861
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 902 NALK--VVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTaAQQELRFK----ANLEKNKQGL 975
Cdd:COG5022 862 SLLKkeTIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSD-LIENLEFKteliARLKKLLNNI 940
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 976 ETDNkELACEVkVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELaekaNKLQNELDNVSSLLEEAEKKGIKFSKD 1055
Cdd:COG5022 941 DLEE-GPSIEY-VKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREG----NKANSELKNFKKELAELSKQYGALQES 1014
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1056 AASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnslqeQQEEEEEARKNLEKQVLALQSQlTDTKKKVDDDLGTIES 1135
Cdd:COG5022 1015 TKQLKELPVEVAELQSASKIISSESTELSILKPLQK-----LKGLLLLENNQLQARYKALKLR-RENSLLDDKQLYQLES 1088
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1136 LE-EAKKKLLKDGEALSQRL--EEKALAYDKLEKTKNRLQQELDDLM-VDLDHQRQIVSNLEKKQKKFDqLLAEEKNISA 1211
Cdd:COG5022 1089 TEnLLKTINVKDLEVTNRNLvkPANVLQFIVAQMIKLNLLQEISKFLsQLVNTLEPVFQKLSVLQLELD-GLFWEANLEA 1167
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1212 RYA--------EERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDV--------GKNVHE 1275
Cdd:COG5022 1168 LPSpppfaalsEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEGWVPteystslkGFNNLN 1247
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1276 LEKSKRAlEQQVEEMRTQLEELEDELQAT--EDAKLRLEVN--MQAMKAQFERDLQTR---------DEQNEEKKRLLIK 1342
Cdd:COG5022 1248 KKFDTPA-SMSNEKLLSLLNSIDNLLSSYklEEEVLPATINslLQYINVGLFNALRTKasslrwksaTEVNYNSEELDDW 1326
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1343 QVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLrKLQAQMKDYQRELEEARASRdeIFAQSK 1422
Cdd:COG5022 1327 CREFEISDVDEELEELIQAVKVLQLLKDDLNKLDELLDACYSLNPAEIQNL-KSRYDPADKENNLPKEILKK--IEALLI 1403
|
1450 1460 1470 1480 1490 1500
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1423 ESEKKLKSLEAEILQ-LQEELASSE----RARRHAEQERDELADEIANSASGKSALLDEK 1477
Cdd:COG5022 1404 KQELQLSLEGKDETEvHLSEIFSEEksliSLDRNSIYKEEVLSSLSALLTKEKIALLDRK 1463
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-771 |
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: 870.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNIpGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA-SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL-----SNGYIPIPGQQDKDNFQETMEA 332
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 333 MHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNT--DQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 490 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 569
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 570 KDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDrfvaelwkdvdrivgldqvtgmtetafgsayktkkgm 649
Cdd:cd00124 477 AKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 650 frtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd00124 519 -------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYR 591
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1335178301 730 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd00124 592 ILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-771 |
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: 787.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVA------SSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalgdgpGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 253 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKsDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETM 330
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 331 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 490
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 491 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPR-- 567
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPRpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 568 -QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdriVGLDQVtgmTETAFGSAYKTK 646
Cdd:cd14927 476 kKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDST---EDPKSGVKEKRK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 647 KGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:cd14927 550 KAAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1335178301 726 QRYEILTPNAIPK-GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14927 630 QRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-771 |
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: 781.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 180 SGAGKTENTKKVIQYLAHVASSH--KGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNpyDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 336 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 416 QADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 496 QEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKDKAD 574
Cdd:cd14913 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 575 --FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvTGMTETAFGSAYKTKKGMFRT 652
Cdd:cd14913 477 ahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFA--------TADADSGKKKVAKKKGSSFQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14913 549 VSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLN 628
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1335178301 733 PNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14913 629 ASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-771 |
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: 760.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 418 DFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 498 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLK---DKA 573
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivgLDQVTGMTETAFGSAYKtKKGMFRTV 653
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD------HAGQSGGGEQAKGGRGK-KGGGFATV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 654 GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14909 550 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP 629
|
650 660 670
....*....|....*....|....*....|....*...
gi 1335178301 734 NAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14909 630 AGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-771 |
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: 749.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGK--GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHL-KSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELiESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 418 DFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 498 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK---A 573
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGKgpeA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivgldqvtgmtETAFGSAYKTKKGM-FRT 652
Cdd:cd14934 475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKE--------------EEAPAGSKKQKRGSsFMT 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14934 541 VSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLN 620
|
650 660 670
....*....|....*....|....*....|....*....
gi 1335178301 733 PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14934 621 PNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-771 |
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: 728.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVASSHKGrkDHNIpgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--ETQV----EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGgSPVIDGVDDAAEFEETRKALTLLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 417
Cdd:cd01380 236 ISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 418 DFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 497 EEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK--FQKPRQLKDKad 574
Cdd:cd01380 396 EEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTA-- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRfvaelwkdvdrivgldqvtgmtetafgsayktKKgmfrTVG 654
Cdd:cd01380 470 FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR--------------------------------KK----TVG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd01380 514 SQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPS 593
|
650 660 670
....*....|....*....|....*....|....*..
gi 1335178301 735 AIPKGfMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01380 594 KEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-771 |
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: 723.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL---GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEhlKSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEELLATEQAMDIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 337 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 416
Cdd:cd14929 236 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 417 ADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd14929 316 VTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 497 EEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK--A 573
Cdd:cd14929 395 EEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKKfeA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivglDQVTGmTETAFGSAYKTKKGMFRTV 653
Cdd:cd14929 472 HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTD-SAIQFGEKKRKKGASFQTV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 654 GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14929 544 ASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNP 623
|
650 660 670
....*....|....*....|....*....|....*....
gi 1335178301 734 NAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14929 624 RTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-771 |
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: 714.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE--LERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 336 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 416 QADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 496 QEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK-- 572
Cdd:cd14917 400 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGKpe 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 573 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdriVGLDqvtGMTETAFGsayKTKKG-MFR 651
Cdd:cd14917 477 AHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY---AGAD---APIEKGKG---KAKKGsSFQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 652 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14917 548 TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 627
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1335178301 732 TPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14917 628 NPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-771 |
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: 700.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 181 GAGKTENTKKVIQYLAHVASSHKGRKDHN--IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 418 DFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14918 323 YNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 498 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKDKAD-- 574
Cdd:cd14918 402 EYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAEah 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgldqVTGMTETAFGSAYKTKKGMFRTVG 654
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAKKGAKKKGSSFQTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14918 551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 1335178301 735 AIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14918 631 AIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-771 |
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: 698.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 180 SGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 415 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14912 322 EQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKDKA 573
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVVKGKA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 574 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvTGMTETAFGSAYK--TKKG- 648
Cdd:cd14912 478 EahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQ--------TAEGASAGGGAKKggKKKGs 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 649 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14912 550 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1335178301 729 EILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14912 630 KVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-771 |
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: 695.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKD--HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 256
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 257 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEgfNN---YRFLSNGYIPIPGQQDKDNFQETMEAM 333
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVT--NNpydYAFVSQGEVSVASIDDSEELLATDSAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 334 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 413
Cdd:cd14916 240 DVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 414 KEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 494 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK 572
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 573 --ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdriVGLDqvTGmtETAFGSAYKTKKGMF 650
Cdd:cd14916 476 qeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY---ASAD--TG--DSGKGKGGKKKGSSF 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 651 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14916 549 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 628
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1335178301 731 LTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14916 629 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-771 |
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: 693.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 180 SGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEatsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 415 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14910 322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK- 572
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGKv 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 573 -ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgldqVTGMTETAFGSAYKTKKG-MF 650
Cdd:cd14910 478 eAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA--------AAAEAEEGGGKKGGKKKGsSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 651 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14910 550 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1335178301 731 LTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14910 630 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-771 |
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: 692.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHN---IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 256
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQpgkMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 257 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNpfDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 415 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKDKA 573
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPAKGKA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 574 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdriVGLDQVTGMTETAFGsayKTKKGMFR 651
Cdd:cd14923 477 EahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSKKGG---KKKGSSFQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 652 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14923 551 TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1335178301 732 TPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14923 631 NASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-771 |
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: 682.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 180 SGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEaasgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFNNYRF--LSNGYIPIPGQQDKDNFQETMEAM 333
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 334 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 413
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 414 KEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 494 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK 572
Cdd:cd14915 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 573 AD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvTGMTETAFGSAYKTKKG-M 649
Cdd:cd14915 477 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQ--------TAEAEGGGGKKGGKKKGsS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 650 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14915 549 FQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1335178301 730 ILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14915 629 VLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-771 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 654.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS---------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGE--HLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 337 GFSHEEILSMLKVVSSVLQFGNISFKK-ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd14883 233 GIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 416 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 496 QEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADF 575
Cdd:cd14883 392 QEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrIVGLDQVTGMTETAfGSAYKTKKGMfRTVGQ 655
Cdd:cd14883 469 GVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGD-TTSRGTSKGK-PTVGD 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 656 LYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd14883 546 TFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRA 625
|
650 660 670
....*....|....*....|....*....|....*.
gi 1335178301 736 IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14883 626 RSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-771 |
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: 653.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRgkKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 180 SGAGKTENTKKVIQYLAHVASSHKGrkdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd01383 151 KIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd01383 231 SKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd01383 311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 499 YQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRqlkDKAdFCII 578
Cdd:cd01383 391 YELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER---GGA-FTIR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSayktkkgMFRTVGQLYK 658
Cdd:cd01383 464 HYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQLFASKMLDASRKALPLTKASGSDS-------QKQSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIpK 738
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-S 614
|
650 660 670
....*....|....*....|....*....|...
gi 1335178301 739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01383 615 ASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-771 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 651.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVER-----VKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGY-IPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDAADFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 339 SHEEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVG---RDYVQKAQTKE 415
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 416 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 496 QEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFVEKLVQEQGSHSKFQKPRQLKD--K 572
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 573 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRivgldqvtgmtetafgsayKTKKGMFRT 652
Cdd:cd01378 473 GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD-------------------LDSKKRPPT 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd01378 534 AGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 1335178301 733 PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01378 614 PKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-771 |
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: 615.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS---------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRDDAAEFADIRSAMKVLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 338 FSHEEILSMLKVVSSVLQFGNISFKK--ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd01381 232 FTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 416 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd01381 312 QALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 494 LEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDK 572
Cdd:cd01381 392 LEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 573 AdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkDVDRIVGLDqvtgmtetafgSAYKTKkgmfrT 652
Cdd:cd01381 468 S-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF-NEDISMGSE-----------TRKKSP-----T 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd01381 530 LSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLV 609
|
650 660 670
....*....|....*....|....*....|....*....
gi 1335178301 733 PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01381 610 PGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-771 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 611.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 178 GESGAGKTENTKKVIQYLAHVA--SSHKGRKdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGgrAVTEGRS-------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGYiPIPGQQDKDNFQETMEAM 333
Cdd:cd01384 154 ISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLnqSKCF-ELDGVDDAEEYRATRRAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 334 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAiLTPRIKVGRD-YVQ 409
Cdd:cd01384 233 DVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDA-LCKRVIVTPDgIIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 410 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd01384 312 KPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 490 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRql 569
Cdd:cd01384 391 HVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK-- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 570 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRivgldqvtgmteTAFGSAYKtkkgm 649
Cdd:cd01384 466 LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR------------EGTSSSSK----- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 650 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd01384 529 FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFG 608
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1335178301 730 ILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd01384 609 LLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-771 |
0e+00 |
|
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: 579.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 178 GESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG--------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNyrflsngyipipgqqDKDNFQETMEAMHIMG 337
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLD---------------DVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 338 FSHEEILSMLKVVSSVLQFGNISFKKERNT-------DQASMPENTVAQKlchLLGMNVMEF-----TRAILTPRIKVGR 405
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRVMQTTRGGAKG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd01382 295 TVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 486 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQK 565
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 566 PRQ--------LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdvdrivgldqvTGMTET 637
Cdd:cd01382 450 PRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF------------ESSTNN 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 638 AFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 717
Cdd:cd01382 518 NKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPS 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1335178301 718 RIVFQEFRQRYEILTPNAIPKgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01382 598 RTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-771 |
0e+00 |
|
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: 578.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG---------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAgeHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14872 152 ASTENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSlSGCIEVEGVDDVADFEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQAS---MPENTVAQKLCHLLGMNVMEFTRAILTPRIKV-GRDYVQKAQT 413
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 414 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14872 310 PAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 494 LEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKA 573
Cdd:cd14872 390 LEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgLDQVTGMTetafgsayktkkgmfrTV 653
Cdd:cd14872 467 EFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE----GDQKTSKV----------------TL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 654 GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtP 733
Cdd:cd14872 527 GGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-V 605
|
650 660 670
....*....|....*....|....*....|....*....
gi 1335178301 734 NAIPKGFM-DGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14872 606 KTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-771 |
1.80e-179 |
|
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: 555.54 E-value: 1.80e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 174 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNI----------PGELERQLLQANPILESFGNAKTVKNDNSSRFG 243
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGeaaseaieqtLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 244 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 323
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 324 DNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTD--QASMPENTVAqKLCHLLGMNVMEFTRAILTPRI 401
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTvlEDATTLQSLK-LAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 402 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNE 481
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 482 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPKAT--DKTFVEKLVQ--- 555
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHAsfg 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 556 ----------EQGSHSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDRFVAELwkdvdri 625
Cdd:cd14890 477 rksgsggtrrGSSQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELI-KQSRRSIREV------- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 626 vgldqvtgmtetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVL 705
Cdd:cd14890 548 --------------------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMM 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1335178301 706 EGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14890 602 EAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-771 |
2.50e-178 |
|
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: 552.05 E-value: 2.50e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVASSHkgrkdhniPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRR--------NNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQ---ASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd01387 232 FSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 415 EQADFAVEALAKATYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 495 EQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQlkDKAD 574
Cdd:cd01387 391 EQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM--PLPE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgLDQVTGMTETAFGSAYKTKKGMFRTVG 654
Cdd:cd01387 466 FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH-----RAQTDKAPPRLGKGRFVTMKPRTPTVA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd01387 541 ARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVAL 620
|
650 660 670
....*....|....*....|....*....|....*...
gi 1335178301 735 AIPKGfMDGKQACERMIRALELDP-NLYRIGQSKIFFR 771
Cdd:cd01387 621 KLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-771 |
4.92e-174 |
|
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: 540.90 E-value: 4.92e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIpgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI-----KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLsgAGEHLKSDLLLEGFNNYRFL-SNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14903 153 GAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGMSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 337 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASM--PENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 495 EQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVqeqGSHSKFQK----PRqlK 570
Cdd:cd14903 390 VQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefPR--T 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 571 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrIVGLDQVTGMTETAFGSAYKTKKGMF 650
Cdd:cd14903 461 SRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGARRRRGGALTT 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 651 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14903 538 TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1335178301 731 LTPNAiPKGFMDGKQACERMIRALELD-PNLYRIGQSKIFFR 771
Cdd:cd14903 618 FLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-771 |
8.44e-172 |
|
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: 536.19 E-value: 8.44e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLahVASSHKGrkdHNipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG---YG--SGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFERLKQAMEMVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 338 FSHEEILSMLKVVSSVLQFGNISFKKER-NTDQASMPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd01385 234 FLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPeVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 416 QADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd01385 314 EAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 492 FILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPrQLKD 571
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVME 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 572 KAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELwkdvdriVGLDQV-------------------- 631
Cdd:cd01385 469 PA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVavfrwavlrafframaafre 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 632 TGM----------------TETAFGSAYKTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLV 695
Cdd:cd01385 541 AGRrraqrtaghsltlhdrTTKSLLHLHKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELV 618
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1335178301 696 LDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01385 619 LRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-769 |
9.29e-171 |
|
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: 532.06 E-value: 9.29e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY------RGKKRHEMPPHIYAISESAYRCMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 171 --DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 249 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGYIPIPGQQDKDNF 326
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 327 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF-KKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 405
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFELNSFEQLCINYTNEKLQ 484
Cdd:cd14901 321 EYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEKLQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 485 QLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSH 560
Cdd:cd14901 401 QLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 561 SKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAElwkdvdrivgldqvtgmtetafg 640
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 641 sayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIV 720
Cdd:cd14901 531 -----------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1335178301 721 FQEFRQRYEILTPNAIPKGFMDGKQACERMIRA------LELDPNLYrIGQSKIF 769
Cdd:cd14901 600 HDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-733 |
6.20e-168 |
|
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: 524.64 E-value: 6.20e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRgKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVT---- 253
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS-----LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLkskr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 254 -----GYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP------------ 316
Cdd:cd14888 155 msgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPisidmssfephl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 317 ------------IPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL--- 381
Cdd:cd14888 235 kfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLekv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 382 CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIA 461
Cdd:cd14888 315 ASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 462 GFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWF 541
Cdd:cd14888 395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 542 PKATDKTFVEKLVQEQGSHSKFQKPRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKD 621
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 622 -VDRIVGLdqvtgmtetafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLR 700
Cdd:cd14888 550 yLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLK 614
|
650 660 670
....*....|....*....|....*....|...
gi 1335178301 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14888 615 YGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-771 |
8.94e-168 |
|
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: 523.97 E-value: 8.94e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 337 GFSHEEILSMLKVVSSVLQFGNISFKkerNTDQASMPENTVAQKLCHLLGMNVMEFTRAiLTPRIKVGR-DYVQKAQTKE 415
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQRSMFLRgEEILTPLNVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 416 QADFAVEALAKATYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14873 317 QAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 495 EQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDkaD 574
Cdd:cd14873 394 EQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVN--N 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVtgmtetafGSAYKTKKgmfRTVG 654
Cdd:cd14873 468 FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTL--------KCGSKHRR---PTVS 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14873 537 SQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRN 616
|
650 660 670
....*....|....*....|....*....|....*..
gi 1335178301 735 AIPKGFMDGKqaCERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14873 617 LALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-771 |
5.21e-166 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 518.37 E-value: 5.21e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 180 SGAGKTENTKKVIQYLAHVAsshkgrKDHNipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG------KANN--RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGagehLKSDLLLEGFN-------NYRFLSNGYIPIPGQQD--KDNFQETM 330
Cdd:cd01379 154 RISEYLLEKSRVVHQAIGERNFHIFYYIYAG----LAEDKKLAKYKlpenkppRYLQNDGLTVQDIVNNSgnREKFEEIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 331 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFK---KERNTDQASMPENTVA-QKLCHLLGMNVMEFTRAiLTPRIKVGR- 405
Cdd:cd01379 230 QCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRISNPEAlNNVAKLLGIEADELQEA-LTSHSVVTRg 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 483
Cdd:cd01379 309 ETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 484 QQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPKATDKTFVEKLvqEQGSHSK 562
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKF--HNNIKSK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 563 FQKpRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAElwkdvdrivgldqvtgmtetafgsa 642
Cdd:cd01379 463 YYW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 643 yktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 722
Cdd:cd01379 517 ---------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFA 587
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1335178301 723 EFRQRYEILTPNAIPKGFMDgKQACERMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd01379 588 DFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-771 |
3.65e-162 |
|
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: 508.08 E-value: 3.65e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKK-RHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 178 GESGAGKTENTKKVIQYLAHVASShkgrkdhnIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS--------DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQD-------KDNFQETM 330
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseeleyyRQMFHDLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 331 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:cd14897 233 NIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 486
Cdd:cd14897 313 WKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 487 FNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKP 566
Cdd:cd14897 393 FNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVAS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 567 rqLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdvdrivgldqvtgmtetafgsayktk 646
Cdd:cd14897 470 --PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT-------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 647 kgmfrtvgQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd14897 522 --------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVK 593
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1335178301 727 RYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd14897 594 RYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-771 |
1.67e-161 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 506.99 E-value: 1.67e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEM---PPHIYAISESAYRCMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 172 QSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 248 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNF 326
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 327 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFkkERNTDQ----ASMPENTVAQKLCHLLGMNVMEFTRAILTPRIK 402
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 403 VGRDYV-QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ---------GASFIGILDIAGFEIFELNSFE 472
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 473 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFP-KATDKTFVE 551
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 552 KLVQEQ-GSHSKFQKPRQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDrfvaelwkdvdrivgldq 630
Cdd:cd14892 476 IYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 631 vtgmtetafgsayktkkgmFRTvgqlykeSLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRI 710
Cdd:cd14892 536 -------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRI 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1335178301 711 CRQGFPNRIVFQEFRQRYEILTPN-AIPKGFMDGKQACERM-----IRALELDPNLYRIGQSKIFFR 771
Cdd:cd14892 590 RREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-731 |
7.63e-150 |
|
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: 474.79 E-value: 7.63e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY-----------RGKKRHEMPPHIYAISESAYRCM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHV------ASSHKGRKDHNIPGelerQLLQANPILESFGNAKTVKND 237
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlaASVSMGKSTSGIAA----KVLQTNILLESFGNARTLRND 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 238 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEhlksdlllegfnnyrflsngyipi 317
Cdd:cd14900 158 NSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE------------------------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 318 pGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQK-------LCHLLGMNVM 390
Cdd:cd14900 214 -AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLAPSsiwsrdaAATLLSVDAT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 391 EFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGAS-FIGILDIAGFEIF 466
Cdd:cd14900 293 KLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 467 ELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATD 546
Cdd:cd14900 373 PKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 547 KTFVEKLVQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDplndnvatLLHQSSdrfvaelwkdVDriv 626
Cdd:cd14900 450 TTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------VD--- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 627 gldqvtgmtetafgsayktkkgMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLE 706
Cdd:cd14900 509 ----------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVME 565
|
650 660
....*....|....*....|....*
gi 1335178301 707 GIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14900 566 AVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-771 |
9.06e-149 |
|
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: 472.85 E-value: 9.06e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 177 TGESGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYI 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS---------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 257 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG--AGEHLKSDLLLEGFnnYRFLSNGYipipGQQD-----KDNFQET 329
Cdd:cd14889 153 KGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNGA----GCKRevqywKKKYDEV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 330 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFkkERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAiLTPRIKVGR- 405
Cdd:cd14889 227 CNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKT-LTCTVTFTRg 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFELNSFEQLCINYTNEKL 483
Cdd:cd14889 304 EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 484 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKF 563
Cdd:cd14889 384 QYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 564 QKPRQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQS-----SDRFVAELWKdVDRIVGLDQVTGMTETA 638
Cdd:cd14889 461 GKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSatpllSVLFTATRSR-TGTLMPRAKLPQAGSDN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 639 FGSAYKtkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNR 718
Cdd:cd14889 538 FNSTRK------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWR 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1335178301 719 IVFQEFRQRYEIL--TPNaIPKgfmdGKQACERMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd14889 612 PSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-734 |
2.94e-147 |
|
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: 469.13 E-value: 2.94e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH--------EMPPHIYAISESAYRCMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 170 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE-----------LERQLLQANPILESFGNAKTVKNDN 238
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSsiratskstksIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 239 SSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLE----GFNNYRFLSNG 313
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlsGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 314 YIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFK-KERNTDQASMPENT-VAQKLCHLLGMNVME 391
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKeTLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 392 FTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL-------DRTKRQGASFIGILDIAGFE 464
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 465 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFP 542
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 543 KATDKTFVEKLVQEQGSHSKFQKPRQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdv 622
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF--- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 623 driVGLDQVTGMTETAFGSAYKTKKgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 702
Cdd:cd14907 554 ---SGEDGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
650 660 670
....*....|....*....|....*....|..
gi 1335178301 703 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-771 |
1.80e-143 |
|
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: 457.97 E-value: 1.80e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiysENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 172 QSILCTGESGAGKTENTKKVIQYLAH--VASSHKGRKDHNI--------PGELERQLLQANPILESFGNAKTVKNDNSSR 241
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTraVGGKKASGQDIEQsskkrklsVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 242 FGKFIRINFDVTGY-IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPG 319
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 320 QQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKErNTDQASMPENTVAQK-----LCHLLGMNVMEFTR 394
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEE-DTSEGEAEIASESDKealatAAELLGVDEEALEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 395 AILTPRIkVGRDYVQKAQ-TKEQADFAVEALAKATYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFEL-NSFE 472
Cdd:cd14891 315 VITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 473 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEK 552
Cdd:cd14891 393 QLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNET 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 553 LVQEQGSHSKFQKPRQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHqSSDRFvaelwkdvdrivgLDQV 631
Cdd:cd14891 470 LHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLA-SSAKF-------------SDQM 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 632 TGMTEtafgsayktkkgmfrtvgqlykesltklmaTLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIC 711
Cdd:cd14891 535 QELVD------------------------------TLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVL 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1335178301 712 RQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14891 585 KVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-771 |
6.23e-140 |
|
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: 448.62 E-value: 6.23e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIPgelerQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:cd14904 153 GAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 336 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQkLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQ-VAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 416 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14904 312 EAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 496 QEEYQREGIEWNFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKL---VQEQGSHSKFQKPRQlkDK 572
Cdd:cd14904 392 EEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKV--KR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 573 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvtGMTETAFGSAYKTKKGMfRT 652
Cdd:cd14904 466 TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APSETKEGKSGKGTKAP-KS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14904 536 LGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMF 615
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1335178301 733 PNAIPKGfmDGKQACERMIRAL-ELDPNLYRIGQSKIFFR 771
Cdd:cd14904 616 PPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-771 |
2.57e-139 |
|
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: 446.53 E-value: 2.57e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLahvASSHKGRKDHNIpgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL---SSLYQDQTEDRL-----RQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14896 152 ASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQ--ASMPENTVAQKLCHLLGMNVmEFTRAILTPRIKV-GRDYVQKAQTK 414
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPP-ERLEGAVTHRVTEtPYGRVSRPLPV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14896 311 EGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 494 LEQEEYQREGIEWNFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQlkDKA 573
Cdd:cd14896 391 QEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PLP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvtgmtetafgSAYKTKKGMfRTV 653
Cdd:cd14896 466 VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAE-----------------PQYGLGQGK-PTL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 654 GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTp 733
Cdd:cd14896 528 ASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG- 606
|
650 660 670
....*....|....*....|....*....|....*...
gi 1335178301 734 NAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14896 607 SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-771 |
8.33e-138 |
|
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: 443.97 E-value: 8.33e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR--GKKRHE-------MPPHIYAISESAYRCMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE---LERQLLQANPILESFGNAKTVKNDNSSRFGKF 245
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGklsIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 246 IRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGE--------HLKSDLLLEGFNNYRFLSNGYIPI 317
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 318 PGQ-QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPE---NTVAQKLCHLLGMNVMEFT 393
Cdd:cd14908 241 LREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 394 RAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASfIGILDIAGFEIFELNSF 471
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 472 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFV 550
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 551 EKLV--------QEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLM-KNMDPLNdnvatllhqssdrfvaelwkd 621
Cdd:cd14908 477 SRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP--------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 622 vdrivgldqvtgmtetafgsayKTKKGMFRTvGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 701
Cdd:cd14908 536 ----------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRY 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 702 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPK-----------------GFMDGKQACERMIRALELDPNL---- 760
Cdd:cd14908 593 GGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlswsmerldpqklcvKKMCKDLVKGVLSPAMVSMKNIpedt 671
|
730
....*....|.
gi 1335178301 761 YRIGQSKIFFR 771
Cdd:cd14908 672 MQLGKSKVFMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-733 |
1.45e-135 |
|
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: 438.94 E-value: 1.45e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEMPPHIYAISESAYRCMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 169 REDQSILCTGESGAGKTENTKKVIQYLAHV-ASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgRDQSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 248 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLsNGYIP----IPGQQDK 323
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELL-NSYGPsfarKRAVADK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 324 DN--FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAILT 398
Cdd:cd14902 240 YAqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLakcAELMGVDVDKLETLLSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 399 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD--------RTKRQGASFIGILDIAGFEIFELNS 470
Cdd:cd14902 320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 471 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFV 550
Cdd:cd14902 400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKGSNQALS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 551 EKLVQEQGSHSKfqkprqlkdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDrfvaelwkDVDRIVGLDQ 630
Cdd:cd14902 477 TKFYRYHGGLGQ------------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN--------EVVVAIGADE 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 631 VTGMTETAFGSAYKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGI 708
Cdd:cd14902 537 NRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAV 616
|
650 660
....*....|....*....|....*
gi 1335178301 709 RICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14902 617 RIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-732 |
4.18e-135 |
|
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: 437.08 E-value: 4.18e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyseniiEMYRGKKRHE-------MPPHIYAISESAYRCMLQ----- 167
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 168 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKDHNIPGElerQLLQANPILESFGNAKTVKNDNSSR 241
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGS---ELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 242 FGKFIRINF-----DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFN--NYRFLSNG- 313
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 314 -YIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTD---------------QASMPENTV 377
Cdd:cd14895 232 cYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 378 AQKL---CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTK------ 448
Cdd:cd14895 312 QQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpn 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 449 ----RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIEr 524
Cdd:cd14895 392 kaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 525 pANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRqlKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDN 602
Cdd:cd14895 470 -QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 603 VATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGmfrtVGQLYKESLTKLMATLRNTNPNFVRCIIPN 682
Cdd:cd14895 547 LFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVG----IGSQFKQQLASLLDVVQQTQTHYIRCIKPN 622
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1335178301 683 HEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14895 623 DESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
97-824 |
1.86e-134 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 439.47 E-value: 1.86e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 97 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHE-MPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 176 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIpgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI----QNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:PTZ00014 261 IRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 336 MGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASM--PEN-TVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:PTZ00014 341 MGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESlEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEG 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 490
Cdd:PTZ00014 421 PWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDI 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 491 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLK 570
Cdd:PTZ00014 500 VFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDS 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 571 DKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGldqvtgmtetafgsayKTKKGMF 650
Cdd:PTZ00014 577 NK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG----------------KLAKGQL 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 651 rtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:PTZ00014 640 --IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 731 LTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR---AGVLAHLEEERDLKITDIIIFFQAVCRGYLARKAFA 807
Cdd:PTZ00014 718 LDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVR 797
|
730
....*....|....*..
gi 1335178301 808 KKqqqlsaLKVLQRNCA 824
Cdd:PTZ00014 798 KN------IKSLVRIQA 808
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-769 |
8.14e-130 |
|
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: 420.55 E-value: 8.14e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 178 GESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIpgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI----QTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKSMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 338 FSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMPEN---TVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQ 412
Cdd:cd14876 234 LTEEQIDTVFSIVSGVLLLGNVKItgKTEQGVDDAAAISNeslEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 413 TKEQADFAVEALAKATYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd14876 314 TKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 492 FILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFqKPRQLKD 571
Cdd:cd14876 392 FERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF-KPAKVDS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 572 KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGldqvtgmtetafgsayKTKKGMFr 651
Cdd:cd14876 468 NINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG----------------KIAKGSL- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 652 tVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14876 531 -IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL 609
|
650 660 670
....*....|....*....|....*....|....*...
gi 1335178301 732 TPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIF 769
Cdd:cd14876 610 DLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-771 |
1.14e-125 |
|
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: 410.55 E-value: 1.14e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVASSHKGRkdhnipgeLERQLLQA-NPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV--------LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLE--GFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNqlAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 336 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAI------------LTPRIKV 403
Cdd:cd01386 233 LGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSGQE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 404 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFEIFELN------SFEQLCIN 477
Cdd:cd01386 313 SPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPGFQNPAHSgsqrgaTFEDLCHN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 478 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERP---ANPP---------GVLALLDEECWFPKAT 545
Cdd:cd01386 392 YAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLLDEEALYPGSS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 546 DKTFVEKLVQEQG--SHSKFQKPRQLKDKA-DFCIIHYAGK--VDYKADEWLMK-NMDPLNDNVATLLHQSSDRFVAelw 619
Cdd:cd01386 472 DDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKETAA--- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 620 kdvdrivgldqvtgmtetafgsayKTKKGMFRTVgqlyKESLTKLMATLRNTNPNFVRCIIPNH--EKRAGK-------- 689
Cdd:cd01386 549 ------------------------VKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHnaGKDERStsspaagd 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 690 --LDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGF-----MDGKQACERMIRALELDPNLYR 762
Cdd:cd01386 601 elLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLEKSSYR 680
|
....*....
gi 1335178301 763 IGQSKIFFR 771
Cdd:cd01386 681 IGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-733 |
1.56e-122 |
|
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: 400.77 E-value: 1.56e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 175 LCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGyipiPGQQDKDNFQETMEAMH 334
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP----ERNLEEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTV---AQKLCHLLGMNVMEFTRAILTPRIKVGRDYV--Q 409
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRAGKQQQvfK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 410 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 490 TMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 569
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 570 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAfgsayktkkgm 649
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAP----------- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 650 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14880 543 VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
....
gi 1335178301 730 ILTP 733
Cdd:cd14880 623 LLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-734 |
1.52e-119 |
|
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: 394.35 E-value: 1.52e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 177 TGESGAGKTENTKKVIQYLAHVASS--HKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSnqQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 255 YIV-GANIETYLLEKSR-AVRQAKDERTFHIFYQLLSGAGehlKSDLLLEGFNN----YRFL--------------SNGY 314
Cdd:cd14906 161 GKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGAS---KDERSKWGLNNdpskYRYLdarddvissfksqsSNKN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 315 IPIPGQQDKD-NFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNVM 390
Cdd:cd14906 238 SNHNNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLesvSKLLGYIES 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 391 EFTRAILTPRIKV-GRDYVQ-KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR----------TKRQGASFIGIL 458
Cdd:cd14906 318 VFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 459 DIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEE 538
Cdd:cd14906 398 DIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 539 CWFPKATDKTFVEKLVQEQgsHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAEL 618
Cdd:cd14906 475 CIMPKGSEQSLLEKYNKQY--HNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 619 WKdvdrivglDQVTGMTETafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQ 698
Cdd:cd14906 553 FQ--------QQITSTTNT------TKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQ 618
|
650 660 670
....*....|....*....|....*....|....*.
gi 1335178301 699 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14906 619 LRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-771 |
1.90e-115 |
|
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: 380.77 E-value: 1.90e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH-----EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 173 SILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSST--------DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 253 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQDKDNFQETME 331
Cdd:cd14886 153 DGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGIDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 332 AMHIMgFSHEEILSMLKVVSSVLQFGNISFKKERN--TDQASMPENTVA-QKLCHLLGMNVMEFTRAILTPRIKVGRDYV 408
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 409 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERNTYEQLLINYANERLQQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECwfpkatdktfvekLVQeQGSHSKFQK 565
Cdd:cd14886 388 YFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQC-------------LIQ-TGSSEKFTS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 566 PRQLKDKAD-----------FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLdqvtgm 634
Cdd:cd14886 451 SCKSKIKNNsfipgkgsqcnFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 635 tetafgsayktKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQG 714
Cdd:cd14886 525 -----------MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRG 591
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1335178301 715 FPNRIVFQEFRQRYEILT--PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14886 592 FAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-771 |
9.27e-114 |
|
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: 376.46 E-value: 9.27e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRG-KKRHEMPPHIYAISESAYRCM-LQDREDQSIL 175
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 176 CTGESGAGKTENTKKVIQYLAHVASSHKGR-KDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFD-VT 253
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNtSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 254 GYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDL-LLEGFNNYRFLSNGYI----PIPGQ--QDKDNF 326
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDGKtlDDAHEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 327 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILtprIKVGRD 406
Cdd:cd14875 241 QNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 407 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd14875 317 LVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK-FQ 564
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPyFV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 565 KPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELwkdvdrivgldqvtgmtetafgsaYK 644
Cdd:cd14875 474 LPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL------------------------LS 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 645 TKKGMFR---TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 721
Cdd:cd14875 529 TEKGLARrkqTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPI 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1335178301 722 QEFRQRYEILTPNAIPKGFMDGK--QACERMIRALE-----LDPNlYRIGQSKIFFR 771
Cdd:cd14875 609 EQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-728 |
2.41e-107 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 359.79 E-value: 2.41e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY----------RGKKRHEMPPHIYAISESAYRCMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 168 DREDQSILCTGESGAGKTENTKKVIQYLA-------HVASSHKGRKDHNIPGE--LERQLLQANPILESFGNAKTVKNDN 238
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnNNLTNSESISPPASPSRttIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 239 SSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG-----AGEHLKSDLLLEGFNNYRFLSN 312
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 313 GYIPI--PGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKK--ERNTDQASMPENTVAQ--------- 379
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMSsttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 380 -KLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRT----------- 447
Cdd:cd14899 321 tKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 448 ---KRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIER 524
Cdd:cd14899 401 vddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 525 paNPPGVLALLDEECWFPKATDKTFVEKL---VQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLND 601
Cdd:cd14899 480 --RPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 602 NVATLLHQSSDRFVAEL-----WKDVDRIVGLDQVTGMTETAFGSAYKTKkgmfrTVGQLYKESLTKLMATLRNTNPNFV 676
Cdd:cd14899 558 SAAQLLAGSSNPLIQALaagsnDEDANGDSELDGFGGRTRRRAKSAIAAV-----SVGTQFKIQLNELLSTVRATTPRYV 632
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1335178301 677 RCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14899 633 RCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-771 |
4.44e-99 |
|
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: 336.62 E-value: 4.44e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 171 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 251 DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFlsngyipipgqqDKDNFQETM 330
Cdd:cd14887 157 TGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST------------DLRRITAAM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 331 EAMHIMGFSHEEIlsmLKVVSSVLQFGNISFKKERNTDQASMPENT--------VAQKLCHLL-------GMNVMEFTRA 395
Cdd:cd14887 225 KTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTsvsvgceeTAADRSHSSevkclssGLKVTEASRK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 396 ILT--------PRIKVGRDYV------------QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR------ 449
Cdd:cd14887 302 HLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesds 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 450 -------QGASFIGILDIAGFEIFE---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI--DFGLDLQP 517
Cdd:cd14887 382 dedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSFPL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 518 CIDLIERPAN---------------------PPGVLALLDE------ECWFPKATDKTFVEKLVQEQGSHSKFQK--PRQ 568
Cdd:cd14887 462 ASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSAKYKNitPAL 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 569 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDRFVaelwkdvdRIVGLDQVTGMtetafgSAYKTKKg 648
Cdd:cd14887 542 SRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT--------RLVGSKKNSGV------RAISSRR- 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 649 mfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14887 606 --STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRY 683
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1335178301 729 EILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14887 684 ETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-770 |
6.13e-98 |
|
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: 330.67 E-value: 6.13e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 96 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYSENIIEMYR-------GKKRHEMPPHIYAISESAYRCM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 166 LQDREDQSILCTGESGAGKTENTKKVIQYLAHV-ASSHKGRKdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGK 244
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTK-------LSSQISAAEFVLDSFGNAKTLTNPNASRFGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 245 FIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGY--IPIPGQ 320
Cdd:cd14879 152 YTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHplPLGPGS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 321 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMpENT-VAQKLCHLLGMNVMEFtRAIL 397
Cdd:cd14879 232 DDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTdVLDIVAAFLGVSPEDL-ETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 398 TPRIK-VGRD----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIF---ELN 469
Cdd:cd14879 310 TYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRsstGGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 470 SFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIERPanPPGVLALLDEEC-WFPK 543
Cdd:cd14879 386 SLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGK--PGGLLGILDDQTrRMPK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 544 ATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD---FCIIHYAGKVDYKADEWLMKNMDPLndnvatllhqSSDrFVAelwk 620
Cdd:cd14879 458 KTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPD-FVN---- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 621 dvdrivgldqvtgmtetafgsayktkkgMFRTVGQLyKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLR 700
Cdd:cd14879 523 ----------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIR 573
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQACERMIRALELDPNLYRIGQSKIFF 770
Cdd:cd14879 574 SLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-735 |
6.62e-98 |
|
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: 328.40 E-value: 6.62e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYSENIIEMYRGKKRHeMPPHIYAISESAYRCMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvtGYIVGA 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT---------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDlllegFNNYRFLSNGYIPIPgqQDKDNFQETMEAMHIMGFS 339
Cdd:cd14898 147 KFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSSTAGNKESIV--QLSEKYKMTCSAMKSLGIA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 340 HeeILSMLKVVSSVLQFGNISFKKERNTDQASmpeNTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADF 419
Cdd:cd14898 220 N--FKSIEDCLLGILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQART 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 420 AVEALAKATYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 499
Cdd:cd14898 295 IRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 500 QREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLvqeqgshSKFQKPRqLKDKADFCII- 578
Cdd:cd14898 372 KEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI-------KKYLNGF-INTKARDKIKv 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 579 -HYAGKVDYKADEWLMKNMDplndnvatllhqssdrfvaelwkdvdrivgldqvtGMTETAFGSAYKTKKGMFRTVGQLY 657
Cdd:cd14898 440 sHYAGDVEYDLRDFLDKNRE-----------------------------------KGQLLIFKNLLINDEGSKEDLVKYF 484
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1335178301 658 KESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd14898 485 KDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-771 |
4.17e-94 |
|
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: 319.84 E-value: 4.17e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR---GKKRHEMPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 176 CTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF-DVTG 254
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT--------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGY----IPIPGQQDKDNFQETM 330
Cdd:cd14878 153 HLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredvSTAERSLNREKLAVLK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 331 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:cd14878 233 QALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 487
Cdd:cd14878 313 RHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 488 NHTMFILEQEEYQREGIewnfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECWFPKATDKTFVEKL--V 554
Cdd:cd14878 393 NEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVEPNLPKKLqsL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 555 QEQGSHSKFQKPRQ-------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELwkdvdriv 626
Cdd:cd14878 460 LESSNTNAVYSPMKdgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL-------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 627 gldqvtgmtetafgsaYKTKkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLE 706
Cdd:cd14878 532 ----------------FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLE 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1335178301 707 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfmDGKQACERMIRALELDPNL--YRIGQSKIFFR 771
Cdd:cd14878 593 MVKIFRYGYPVRLSFSDFLSRYKPLADTLLGE---KKKQSAEERCRLVLQQCKLqgWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-771 |
3.73e-92 |
|
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: 313.49 E-value: 3.73e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYseniIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAhvasshKGRKDHNipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN---EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 339 sHEEILSMLKVVSSVLQFGNISFK---KERNTDQASMPENT--VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 413
Cdd:cd14937 228 -HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 414 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14937 307 VEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 494 LEQEEYQREGIEWNFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKa 573
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINK- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTetafgsaYKtkkgmfrtv 653
Cdd:cd14937 461 NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRKNLIT-------FK--------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 654 gqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIcRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14937 525 ---YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDY 600
|
650 660 670
....*....|....*....|....*....|....*...
gi 1335178301 734 NAIPKGFMDGKQACERMIRAlELDPNLYRIGQSKIFFR 771
Cdd:cd14937 601 STSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-723 |
3.47e-83 |
|
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: 289.11 E-value: 3.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHE-------MPPHIYAISESAYRCMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 171 DQSILCTGESGAGKTENTKKVIQYLAHVasshKGRKDHNipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMT---ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 251 D---------VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG-AGEHLKSDLLLEGFNNYRFL---------- 310
Cdd:cd14884 154 EeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnpdeshqkrs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 311 ----------SNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKkerntdqasmpentvaqK 380
Cdd:cd14884 234 vkgtlrlgsdSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-----------------A 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 381 LCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-------- 452
Cdd:cd14884 297 AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediys 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 453 ---SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpanpp 529
Cdd:cd14884 377 ineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK----- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 530 gVLALLDE-----ECWFPKATDKTFV-----EKLVQEQGSHSK-FQKPR--------QLKDKADFCIIHYAGKVDYKADE 590
Cdd:cd14884 451 -IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVSYgFVLNHdadgtakkQNIKKNIFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 591 WLMKNMDPLNDNVATLLHQSSDRFVAElwkdvdrivgldqvtgmtetafgSAYKTKKGMFRTVGQLYKESLTKLMATLRN 670
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQS 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1335178301 671 TNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 723
Cdd:cd14884 587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-758 |
2.25e-78 |
|
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: 273.14 E-value: 2.25e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyseniieMYRGKKRH-------EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 173 SILCTGESGAGKTENTKKVIQYLAHVASshkgrkdhnipGELE----RQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 248
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG-----------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 249 NFdVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNF 326
Cdd:cd14881 139 QV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 327 QETMEAMHIMGFsheEILSMLKVVSSVLQFGNISF--KKERNTDQASMPE-NTVAQklchLLGMNVMEFTRAiLTPRIK- 402
Cdd:cd14881 218 QAWKACLGILGI---PFLDVVRVLAAVLLLGNVQFidGGGLEVDVKGETElKSVAA----LLGVSGAALFRG-LTTRTHn 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 403 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIFELNSFEQL 474
Cdd:cd14881 290 ARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 475 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPKATDKTFVEKL 553
Cdd:cd14881 366 CINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKI 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 554 VQEQGSHSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSdrfvaelwkdvdrivgldqvtg 633
Cdd:cd14881 442 KVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN---------------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 634 mteTAFGsayktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQ 713
Cdd:cd14881 499 ---CNFG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAG 566
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1335178301 714 GFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIR--ALELDP 758
Cdd:cd14881 567 GYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPP 613
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-736 |
1.38e-72 |
|
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: 256.34 E-value: 1.38e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgkkrhemppHIYAISESAYRCMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNipgelerqllQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYIV 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSS----------AIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 258 GANIE-TYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14874 140 GLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 337 GFSHEEILSMLKVVSSVLQFGNISFKKERNTD-QASMPE--NTVAQKLCHLLGMNVMEFTRAILTPRIKVGrdyvqKAQT 413
Cdd:cd14874 220 GFSDDHCISIYKIISTILHIGNIYFRTKRNPNvEQDVVEigNMSEVKWVAFLLEVDFDQLVNFLLPKSEDG-----TTID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 414 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14874 295 LNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 494 LEQEEYQREGIEWNF-IDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQlKDK 572
Cdd:cd14874 373 DQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KER 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 573 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELwkdvdrivgldqvtgmtetaFGSAYKTKKGMFRT 652
Cdd:cd14874 450 LEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLL--------------------FESYSSNTSDMIVS 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14874 510 QAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLL 589
|
....
gi 1335178301 733 PNAI 736
Cdd:cd14874 590 PGDI 593
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
100-771 |
6.48e-71 |
|
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: 252.71 E-value: 6.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYrgKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHV-ASSHKGRKDHnipgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTdLSRSKYLRDY---------ILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSN-GYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14905 151 GAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 337 GFSHEEILSMLKVVSSVLQFGNISFKKERNtdQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAqtkeq 416
Cdd:cd14905 231 DFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR----- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 417 adfavEALAKATYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd14905 304 -----DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 497 EEYQREGIEW-NFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPKATDKTFVEKLVQEQGSHSKF-QKPRQlkdkad 574
Cdd:cd14905 377 REYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK------ 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRF-------------VAELWKDVD----------RIVGL--- 628
Cdd:cd14905 444 FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYlfsrdgvfninatVAELNQMFDakntakksplSIVKVlls 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 629 ------DQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPN--FVRCIIPNHEKRAGKLDPHLVLDQLR 700
Cdd:cd14905 524 cgsnnpNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTFDVKSVNEQIK 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1335178301 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipKGFMD-GKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14905 604 SLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVGNTKIFLR 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-770 |
3.96e-68 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 246.04 E-value: 3.96e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 102 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKR----------HEMPPHIYAISESAYRCMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 172 QSILCTGESGAGKTENTKKVIQYLAHVASS----HKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 248 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAgEH---LKSDLLL-EGFNNYRFLSNGyIPIPGQ--Q 321
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQA-DPLATNfaL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 322 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMPENTVAQ-KLCHL-------LGMNVME 391
Cdd:cd14893 242 DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpDPEGGKSVGGANSTTVSDaQSCALkdpaqilLAAKLLE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 392 FTRAILTPRIKVGRDYVQ---------KAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQG----ASF 454
Cdd:cd14893 322 VEPVVLDNYFRTRQFFSKdgnktvsslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNivinSQG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 455 IGILDIAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQPCIDLIERP 525
Cdd:cd14893 402 VHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFEDK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 526 anPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD------------FCIIHYAGKVDYKADEWLM 593
Cdd:cd14893 482 --PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNGKGLSS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 594 KNMDPLNDNVATLLHQSSDrfvaelwkDVDRIVGLDQVT--------------GMTETAFG----SAYKTKKGMFRTVGQ 655
Cdd:cd14893 560 KNMLSISSTCAAIMQSSKN--------AVLHAVGAAQMAaassekaakqteerGSTSSKFRksasSARESKNITDSAATD 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 656 LYKESlTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYeiltpna 735
Cdd:cd14893 632 VYNQA-DALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY------- 703
|
730 740 750
....*....|....*....|....*....|....*....
gi 1335178301 736 ipKGFMDGKQACERMIRALE----LDPNLYRIGQSKIFF 770
Cdd:cd14893 704 --KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-731 |
2.50e-66 |
|
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: 238.10 E-value: 2.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 180 SGAGKTENTKKVIQYLAHVasshkGRKDHNIPGELERqllqANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYL-----GDGNRGATGRVES----SIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSG--AGEHLKsDLLLEGFNNYRFLSngyIP--IPG----------QQDKDN 325
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLR---IPpeVPPsklkyrrddpEGNVER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 326 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKerNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 405
Cdd:cd14882 229 YKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFELNSFEQLCINYTN 480
Cdd:cd14882 307 SAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMVNTLN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 481 EKLQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQPCIdlierpANPPGVLALLDEECwfPKATDKTFVEKLVQEQ 557
Cdd:cd14882 384 EQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVDQLM------TKPDGLFYIIDDAS--RSCQDQNYIMDRIKEK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 558 gsHSKFQKPrqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivglDQVTGMtet 637
Cdd:cd14882 456 --HSQFVKK---HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM--- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 638 afgsayKTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQG 714
Cdd:cd14882 521 ------RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKG 588
|
650
....*....|....*..
gi 1335178301 715 FPNRIVFQEFRQRYEIL 731
Cdd:cd14882 589 FSYRIPFQEFLRRYQFL 605
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-769 |
6.41e-60 |
|
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: 220.86 E-value: 6.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR-GKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 179 ESGAGKTENTKKVIQYLAHVA----------SSHKGRKDHNIP-----GELERQLLQANPILESFGNAKTVKNDNSSRFG 243
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVkgsrrlptnlNDQEEDNIHNEEntdyqFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 244 KFIRINFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 323
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 324 DNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNI----SFKKE----------------------RNTDQASMPENTV 377
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkAFRKKsllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 378 AQKL-CHLLGMNVMEFTRAILTPRIkVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR--QGASF 454
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 455 IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANppGVLAL 534
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 535 LDEECWFPKATDKTFVEKLVQEQGSHSKF--QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSD 612
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSIIRKFSRNSKyiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 613 RFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQ----LYKESLTKLMATLRNTNPNFVRCIIPNHEKRA- 687
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 688 GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACERMIRALELDPNLYRIGQSK 767
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 1335178301 768 IF 769
Cdd:cd14938 710 IF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-255 |
8.77e-59 |
|
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: 200.26 E-value: 8.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 121 FCVVINPYKNLPIYSEN-IIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1335178301 200 SSHKGRKDHN-------IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd01363 81 FNGINKGETEgwvylteITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
849-1621 |
2.13e-33 |
|
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: 141.35 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 849 RQEEELQakdeeLLKVKEKQTKVEGELEEMERK----HQQARATAEAggddetlhknnalkvvRELQAQIAELQ-----E 919
Cdd:TIGR02168 174 RKETERK-----LERTRENLDRLEDILNELERQlkslERQAEKAERY----------------KELKAELRELElallvL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 920 DFESEKASRNKAEKQKRDLSEELEALKTELeDTLDTTAAQQELRFkANLEKNKQGLETDNKELACEVKVLQQVKAESEHK 999
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAEL-QELEEKLEELRLEV-SELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1000 RKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQE------E 1073
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETlrskvaQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1074 TRQKLN-LSSRIRQLEEEKNSLQE-----QQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKkkllkdg 1147
Cdd:TIGR02168 391 LELQIAsLNNEIERLEARLERLEDrrerlQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL------- 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1148 EALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRQI---VSNLEKKQKKF--------DQLLAEEKNISARYAEE 1216
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFsegVKALLKNQSGLsgilgvlsELISVDEGYEAAIEAAL 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1217 RDRAEAEAREKETKAL----SLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRT 1292
Cdd:TIGR02168 544 GGRLQAVVVENLNAAKkaiaFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLG 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1293 QLEELEDELQATEDAKL------------------------RLEVNMQAMKAQFE-RDLQTRDEQNEEKKRLLIKQVREL 1347
Cdd:TIGR02168 624 GVLVVDDLDNALELAKKlrpgyrivtldgdlvrpggvitggSAKTNSSILERRREiEELEEKIEELEEKIAELEKALAEL 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1348 EAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK 1427
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1428 LKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRK 1507
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1508 TTLQVDTLNAEL--------------AAERSAAQKSDNARQQLERQNKELKAKLQELEGAVkSKFKATISALEAKIGQLE 1573
Cdd:TIGR02168 864 LEELIEELESELeallnerasleealALLRSELEELSEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQ 942
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1335178301 1574 EQLEQEAK---------------ERAAANKLVRRTEKKLKEI----------FMQVEDERRHADQYKEQMEKA 1621
Cdd:TIGR02168 943 ERLSEEYSltleeaealenkiedDEEEARRRLKRLENKIKELgpvnlaaieeYEELKERYDFLTAQKEDLTEA 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
925-1680 |
5.57e-32 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 136.72 E-value: 5.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 925 KASRNKAEKQKRDLSEELEALK---TELEDTLDTTAAQ----QELRFKANLEKNKQG--LETDNKELACEVKVLQQVKAE 995
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEdilNELERQLKSLERQaekaERYKELKAELRELELalLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 996 SEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETR 1075
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1076 QKLNLSSRIRQLEEEK-------NSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLG--------------TIE 1134
Cdd:TIGR02168 331 KLDELAEELAELEEKLeelkeelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELqiaslnneierleaRLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1135 SLEEAKKKLLKDGEALSQRLEEKALA-----YDKLEKTKNRLQQELDDLMVDLDHQRQivsNLEKKQKKFDQLLAEEKNI 1209
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKelqaeLEELEEELEELQEELERLEEALEELRE---ELEEAEQALDAAERELAQL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1210 SAR-YAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQ---------NKQLRADMEDL-MSSKDDVGKNVHELEK 1278
Cdd:TIGR02168 488 QARlDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISvdegyeaaiEAALGGRLQAVvVENLNAAKKAIAFLKQ 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1279 S---KRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTR----------DEQNEEKKRLlikQVR 1345
Cdd:TIGR02168 568 NelgRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddlDNALELAKKL---RPG 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1346 ELEAELEDER--------KQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEI 1417
Cdd:TIGR02168 645 YRIVTLDGDLvrpggvitGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1418 FAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQleeeleeEQSN 1497
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ-------LKEE 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1498 MELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSkFKATISALEAKIGQLEEQLE 1577
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1578 QEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANAS-RRKLQRELDDA 1656
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEA 956
|
810 820 830
....*....|....*....|....*....|.
gi 1335178301 1657 -------TEANEGLSREVSTLKNRLRRGGPI 1680
Cdd:TIGR02168 957 ealenkiEDDEEEARRRLKRLENKIKELGPV 987
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
829-1607 |
5.66e-32 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 136.72 E-value: 5.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 829 LRHWQWWRVftkvkpLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATaeaggddetlhknnalkvVR 908
Cdd:TIGR02168 222 LRELELALL------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE------------------VS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 909 ELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKT---ELEDTLDTTAAQ-QELRFKAN-LEKNKQGLETDNKELA 983
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERqleELEAQLEELESKlDELAEELAeLEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 984 CEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEgdrlrveLAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASL---- 1059
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQ-------LELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkl 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1060 -ESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKkkvdDDLGTIESLEE 1138
Cdd:TIGR02168 431 eEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE----RLQENLEGFSE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1139 AKKKLLKDGEALSQ---RLEEKALAYDKLEKTKNR-LQQELDDLMV-DLDHQRQIVSNLEKKQKKFDQLLaEEKNISARY 1213
Cdd:TIGR02168 507 GVKALLKNQSGLSGilgVLSELISVDEGYEAAIEAaLGGRLQAVVVeNLNAAKKAIAFLKQNELGRVTFL-PLDSIKGTE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1214 AEERDRaeaEAREKETKALSLARALEEALEAKEEF-----------------ERQNKQLRADME------DLMSSK---- 1266
Cdd:TIGR02168 586 IQGNDR---EILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvddldnaLELAKKLRPGYRivtldgDLVRPGgvit 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1267 -----------------DDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERdLQTR 1329
Cdd:TIGR02168 663 ggsaktnssilerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAE 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1330 DEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQ---------- 1399
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltllneeaan 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1400 ----MKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLD 1475
Cdd:TIGR02168 822 lrerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1476 EKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSA--------AQKSDNARQQLERQNKELKAKL 1547
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtleeaealENKIEDDEEEARRRLKRLENKI 981
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1335178301 1548 QELeGAVKSKFKATISALEAKIGQLEEQLE--QEAKE--RAAANKLVRRTEKKLKEIFMQVEDE 1607
Cdd:TIGR02168 982 KEL-GPVNLAAIEEYEELKERYDFLTAQKEdlTEAKEtlEEAIEEIDREARERFKDTFDQVNEN 1044
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
846-1604 |
2.21e-28 |
|
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: 124.80 E-value: 2.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 846 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAGGDDETLHKNnalKVVRELQAQIAELQEDFESEK 925
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK---EKIGELEAEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 926 ASRNKAEKQKRDLSEELEALKTELEDtLDTTAAQQELR---FKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKK 1002
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEE-LEREIEEERKRrdkLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1003 LDAQVQELHAKVSEGDRL-------RVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDaaslESQLQDTQELLQEETR 1075
Cdd:TIGR02169 394 LEKLKREINELKRELDRLqeelqrlSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ----EWKLEQLAADLSKYEQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1076 QKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGE-ALSQRL 1154
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvAAGNRL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1155 E----------EKALAYDKLEKTK-------NRLQQELDDL--------------MVDLDHQRQ-----------IVSNL 1192
Cdd:TIGR02169 550 NnvvveddavaKEAIELLKRRKAGratflplNKMRDERRDLsilsedgvigfavdLVEFDPKYEpafkyvfgdtlVVEDI 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1193 EKKQKKFDQL--------LAE-----------EKNISARYAEERDRAEAEAREKEtkalSLARALEEALEAKEEFERQNK 1253
Cdd:TIGR02169 630 EAARRLMGKYrmvtlegeLFEksgamtggsraPRGGILFSRSEPAELQRLRERLE----GLKRELSSLQSELRRIENRLD 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1254 QLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErdlQTRDEQN 1333
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH---KLEEALN 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1334 EEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARAS 1413
Cdd:TIGR02169 783 DLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1414 RDEIfaqskesEKKLKSLEAEILQLQEELAsserarrHAEQERDELADEIansasgkSALLDEKRRLEARIAQLEEELEE 1493
Cdd:TIGR02169 863 KEEL-------EEELEELEAALRDLESRLG-------DLKKERDELEAQL-------RELERKIEELEAQIEKKRKRLSE 921
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1494 EQSNMELLNDRfrkttlqvdtlNAELAAERSAAQKSDNARQQLERQNKELKAKLQELE--GAVKSKFKATISALEAKIGQ 1571
Cdd:TIGR02169 922 LKAKLEALEEE-----------LSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRalEPVNMLAIQEYEEVLKRLDE 990
|
810 820 830
....*....|....*....|....*....|...
gi 1335178301 1572 LEEQLEQEAKERAAANKLVRRTEKKLKEIFMQV 1604
Cdd:TIGR02169 991 LKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
925-1604 |
2.45e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 124.28 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 925 KASRNKAEKQKRDLSEELEALK---TELEDTLDTTAAQQE--LRFKanlEKNKQGLETDNKELACEVKVLQQVKAESEHK 999
Cdd:COG1196 171 KERKEEAERKLEATEENLERLEdilGELERQLEPLERQAEkaERYR---ELKEELKELEAELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1000 RKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLN 1079
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1080 LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKAL 1159
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1160 AYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARale 1239
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE--- 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1240 ealeaKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRaLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMK 1319
Cdd:COG1196 485 -----ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1320 AQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQ 1399
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1400 MKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRR 1479
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1480 LEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKsdnARQQLERQNKEL-----KAkLQELEgav 1554
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER---ELERLEREIEALgpvnlLA-IEEYE--- 791
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1335178301 1555 kskfkatisALEAKIGQLEEQLE--QEAKE--RAAANKLVRRTEKKLKEIFMQV 1604
Cdd:COG1196 792 ---------ELEERYDFLSEQREdlEEAREtlEEAIEEIDRETRERFLETFDAV 836
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
218-712 |
3.80e-26 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 117.15 E-value: 3.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 218 LLQANPILESFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAVRQA------KDERTFHIFYQ 286
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 287 LLSGAGEH-----LKSDLLLEGFN--NYRFLSNGYIPIPG--------QQDKDNFQETMEAMHIMGFSHEEILSMLKVVS 351
Cdd:cd14894 329 MVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 352 SVLQFGNISFKKERNTDQASMPEN---TVAQKLCHLLGMNVME-FTRAILTPRIKV--GRDYVQKAQTKEQADFAVEALA 425
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEkLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 426 KATYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFELNSFEQLCINYTNEKLqqlfnh 489
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL------ 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 490 tmfileqeeYQREGiewNFIDFGLDLQPciDLIERPA---------NPPGVLALLDEECWFPKATD----------KTFV 550
Cdd:cd14894 563 ---------YAREE---QVIAVAYSSRP--HLTARDSekdvlfiyeHPLGVFASLEELTILHQSENmnaqqeekrnKLFV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 551 EKLVQEQGSHSKfQKPRQLKDKA----------DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWK 620
Cdd:cd14894 629 RNIYDRNSSRLP-EPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLN 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 621 DVDRivgLDQVTGMTETAFGSAYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLR 700
Cdd:cd14894 708 ESSQ---LGWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCR 783
|
570
....*....|..
gi 1335178301 701 CNGVLEGIRICR 712
Cdd:cd14894 784 SQRLIRQMEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1067-1632 |
9.07e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 116.19 E-value: 9.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1067 QELLQEETRQKLNLSS-RIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLK 1145
Cdd:COG1196 216 RELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1146 DGEALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAR 1225
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1226 EKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDdvgknvhELEKSKRALEQQVEEMRTQLEELEDELQATE 1305
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE-------RLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1306 DAKLRLEvnmqamkaQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKA 1385
Cdd:COG1196 449 EEEAELE--------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1386 RdeVIKQLRKLQAQMKDYQRELEEARASR--------DEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERD 1457
Cdd:COG1196 521 G--LAGAVAVLIGVEAAYEAALEAALAAAlqnivvedDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1458 ELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLE 1537
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1538 RQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQ 1617
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570
....*....|....*...
gi 1335178301 1618 M---EKANARMKQLKRQL 1632
Cdd:COG1196 759 PpdlEELERELERLEREI 776
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
907-1627 |
1.00e-24 |
|
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: 112.90 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 907 VRELQAQIAELQEDFESEKASRNKAEKQKRDLS-------EELEALKTELEDTLDTTAAQQELRFKANLekNKQGLETD- 978
Cdd:pfam15921 112 VIDLQTKLQEMQMERDAMADIRRRESQSQEDLRnqlqntvHELEAAKCLKEDMLEDSNTQIEQLRKMML--SHEGVLQEi 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 979 -----NKELACEVKVLQQVKAESEHKR----------KKLDAQVQELHAKV-SEGDRLRVELAEKANK----LQNELDNV 1038
Cdd:pfam15921 190 rsilvDFEEASGKKIYEHDSMSTMHFRslgsaiskilRELDTEISYLKGRIfPVEDQLEALKSESQNKiellLQQHQDRI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1039 SSLLEEAEKKGIKFSKDAASLESQ---LQDTQELLQEETRQKLnlSSRIRQLEEeknslqeqqeeeeearknLEKQVLAL 1115
Cdd:pfam15921 270 EQLISEHEVEITGLTEKASSARSQansIQSQLEIIQEQARNQN--SMYMRQLSD------------------LESTVSQL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1116 QSQLTDTKKKVDDdlgTIESLEeaKKKLLKDGEALSQRLEEkalayDKLEKTKNRLQQELDDLMVDLdHQRQIVSNLEKK 1195
Cdd:pfam15921 330 RSELREAKRMYED---KIEELE--KQLVLANSELTEARTER-----DQFSQESGNLDDQLQKLLADL-HKREKELSLEKE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1196 QKK--FDQLLAEEKNISARYAEERDR-AEAEAREKETKALSlARALEEALEAKEEFERQNKQLR---ADMEDLMSSKDDV 1269
Cdd:pfam15921 399 QNKrlWDRDTGNSITIDHLRRELDDRnMEVQRLEALLKAMK-SECQGQMERQMAAIQGKNESLEkvsSLTAQLESTKEML 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1270 GKNVHELEKSKRALE---QQVEEMRTQLEELEDELQAT--EDAKLRLEVNMQAMKAQFERdlqtrdeqNEEKkrllikQV 1344
Cdd:pfam15921 478 RKVVEELTAKKMTLEsseRTVSDLTASLQEKERAIEATnaEITKLRSRVDLKLQELQHLK--------NEGD------HL 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1345 RELEAELEDERKQRAlavASKKKMEIDLKDLESQIE-AANKARDEVIKQLRK--LQAQMKDYQRELEEARASRDEIFAQS 1421
Cdd:pfam15921 544 RNVQTECEALKLQMA---EKDKVIEILRQQIENMTQlVGQHGRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKI 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1422 KESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEkrrleariaqleeeleeeqsnMELL 1501
Cdd:pfam15921 621 RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSED---------------------YEVL 679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1502 NDRFRKTTLQVDT----LNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLE 1577
Cdd:pfam15921 680 KRNFRNKSEEMETttnkLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMT 758
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1578 QEAKERaaanKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQ 1627
Cdd:pfam15921 759 NANKEK----HFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
908-1663 |
2.00e-22 |
|
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: 105.54 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 908 RELQAQIAELQE-DFESEKASRNKAEKQKRdlSEELEALKTELEDTLDTTAAQQE--LRFKAnLEKNKQglETDNKELAC 984
Cdd:TIGR02169 156 RKIIDEIAGVAEfDRKKEKALEELEEVEEN--IERLDLIIDEKRQQLERLRREREkaERYQA-LLKEKR--EYEGYELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 985 EVKVLqqvkaesEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEE-AEKKGIKFSKDAASLESQL 1063
Cdd:TIGR02169 231 EKEAL-------ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1064 QDTQELLQEETRQKLNLSSRIRQLEEEknslqeqqeeeeeaRKNLEKQVLALQSQLTDTKKKVDddlgtieSLEEAKKKL 1143
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAE--------------IDKLLAEIEELEREIEEERKRRD-------KLTEEYAEL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1144 LKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLD-HQRQIVSNLEKKQKKFDQLL---AEEKNISARYAE---E 1216
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINeLKRELDRLQEELQRLSEELAdlnAAIAGIEAKINEleeE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1217 RDRAEAEAREKETKALSLAraleealEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEE 1296
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLA-------ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEV 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1297 L--------------------------------------EDELQATEDAKLRLEVN-----------MQAMKAQFER--- 1324
Cdd:TIGR02169 516 LkasiqgvhgtvaqlgsvgeryataievaagnrlnnvvvEDDAVAKEAIELLKRRKagratflplnkMRDERRDLSIlse 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1325 --------DLQTRDEQN-----------------EEKKRLLIK-QVRELEAELEDE--------RKQRALAVASKKKMEi 1370
Cdd:TIGR02169 596 dgvigfavDLVEFDPKYepafkyvfgdtlvvediEAARRLMGKyRMVTLEGELFEKsgamtggsRAPRGGILFSRSEPA- 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1371 DLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARR 1450
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1451 HAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQsnMELLNDRFRKTTLQVDTLNAELAAERSAAQKSD 1530
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1531 NARQQLERQNKELKAKLQELEGAV------KSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQV 1604
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIenlngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 1335178301 1605 EDERRHADQYKEQMEKANARMKQLKRqLEEAEEEATRANASRRKLQRELDDATEANEGL 1663
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEIED-PKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1342-1632 |
2.13e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.94 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1342 KQVRELEAELEdeRKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAqmkdyqrELEEARASRDEIFAQS 1421
Cdd:COG1196 213 ERYRELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1422 KESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELL 1501
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1502 NDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAvKSKFKATISALEAKIGQLEEQLEQEAK 1581
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1335178301 1582 ERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQL 1632
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
876-1680 |
3.09e-21 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 101.68 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 876 EEMERKHQQARATAEAGGddETLHKNNAlkVVRELQAQIAELQEdfESEKASRNKA---EKQKRDLSE---ELEALKTEL 949
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVE--ENIERLDL--IIDEKRQQLERLRR--EREKAERYQAllkEKREYEGYEllkEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 950 EDTLDTTAAQQElrfkaNLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVsEGDRLRVELAEKAN 1029
Cdd:TIGR02169 240 EAIERQLASLEE-----ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGEL-EAEIASLERSIAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1030 KLQneldnvsslLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLE 1109
Cdd:TIGR02169 314 ERE---------LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1110 KQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEekalaydKLEKTKNRLQQELDDLMVDLDHQRQIV 1189
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA-------GIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1190 SNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSK--- 1266
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGery 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1267 -------------------DDVGKNVHELEKSK---RALEQQVEEMRTQLEELEdelQATEDAKLRLEVNMQAMKAQFER 1324
Cdd:TIGR02169 538 ataievaagnrlnnvvvedDAVAKEAIELLKRRkagRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDLVEFDPKYEP 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1325 DLQ--TRD----EQNEEKKRLLIK-QVRELEAELEDE--------RKQRALAVASKKKMEiDLKDLESQIEAANKARDEV 1389
Cdd:TIGR02169 615 AFKyvFGDtlvvEDIEAARRLMGKyRMVTLEGELFEKsgamtggsRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSL 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1390 IKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASG 1469
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1470 KSALLDEKRRLEARIAQLEEELEEEQsnMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKlqe 1549
Cdd:TIGR02169 774 LHKLEEALNDLEARLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ--- 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1550 legavKSKFKATISALEAKIGQLEEQLEQEAKEraaanklVRRTEKKLKEIfmqvederrhadqyKEQMEKANARMKQLK 1629
Cdd:TIGR02169 849 -----IKSIEKEIENLNGKKEELEEELEELEAA-------LRDLESRLGDL--------------KKERDELEAQLRELE 902
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1335178301 1630 RQLEEaeeeatrANASRRKLQRELDDATEANEGLSREVSTLKNRLRRGGPI 1680
Cdd:TIGR02169 903 RKIEE-------LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
904-1444 |
1.05e-20 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 99.37 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 904 LKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRF-KANLEKNKQGLETDNKEL 982
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKeLESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 983 ACEVKVLQQVKAESEHKRKKLDaQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQ 1062
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1063 LQDTQELLQ--EETRQKLNLSSRIRQLEEEKNSLQEQQ------------EEEEEARKNLEKQVLALQSQLTDTKKKVDD 1128
Cdd:PRK03918 344 KKKLKELEKrlEELEERHELYEEAKAKKEELERLKKRLtgltpeklekelEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1129 DLGTIESLEEAKKKLLKDGEALSQR-----LEEKALAYDKLEKTKNRLQQELDDL---MVDLDHQRQIVSNLEKKQKKFD 1200
Cdd:PRK03918 424 LKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLrkeLRELEKVLKKESELIKLKELAE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1201 QLLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK 1280
Cdd:PRK03918 504 QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1281 RALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRL--LIKQVRELEAELEDERKQR 1358
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLeeLRKELEELEKKYSEEEYEE 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1359 ALAVASKKKMEidLKDLESQIEAANKARDEVIKQLRKLQAQ---MKDYQRELEEARASRDEIfAQSKESEKKLKSLEAE- 1434
Cdd:PRK03918 664 LREEYLELSRE--LAGLRAELEELEKRREEIKKTLEKLKEEleeREKAKKELEKLEKALERV-EELREKVKKYKALLKEr 740
|
570
....*....|
gi 1335178301 1435 ILQLQEELAS 1444
Cdd:PRK03918 741 ALSKVGEIAS 750
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
807-1413 |
2.04e-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: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 807 AKKQQQLSA-LKVLQrncaAYLKLRHWQWWRvftkvkplLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQA 885
Cdd:COG1196 212 AERYRELKEeLKELE----AELLLLKLRELE--------AELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 886 RATAEAGGDDETLH-----------------KNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTE 948
Cdd:COG1196 280 ELELEEAQAEEYELlaelarleqdiarleerRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 949 LEDtldttAAQQELRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKA 1028
Cdd:COG1196 360 LAE-----AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1029 NKLQNELDNVSSLLEEAEKKgikfskdAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnslqeqqeeeeeARKNL 1108
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAEL-------EEEEEALLELLAELLEEAALLEAALAELLEELAEAA------------ARLLL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1109 EKQVLALQSQLTDTKKKVDDDLGtIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQ-QELDDLMVDLDHQRQ 1187
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAG-LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVaAAAIEYLKAAKAGRA 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1188 IVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKD 1267
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1268 DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATED---AKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQV 1344
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELeleEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1345 RELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKAR--------------DEVIKQLRKLQAQMKDyqreLEEA 1410
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIealgpvnllaieeyEELEERYDFLSEQRED----LEEA 810
|
...
gi 1335178301 1411 RAS 1413
Cdd:COG1196 811 RET 813
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1287-1607 |
3.96e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.70 E-value: 3.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1287 VEEMRTQLEELEDelQAtEDAKLRLEVNMQAMKAQFERDLQtRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKK 1366
Cdd:COG1196 195 LGELERQLEPLER--QA-EKAERYRELKEELKELEAELLLL-KLRELEAELEELEAELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1367 KMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIfaqskesEKKLKSLEAEILQLQEELASSE 1446
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL-------EEELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1447 RARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAA 1526
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1527 QKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVED 1606
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
.
gi 1335178301 1607 E 1607
Cdd:COG1196 504 E 504
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
844-1456 |
5.36e-20 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 97.03 E-value: 5.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 844 LLQVTRQEEELQAKD--EELLKVKEKQTKVEGELEEMERKHQQARATAEAGGDDETLHKNNaLKVVRELQAQIAELQEDF 921
Cdd:PRK02224 189 LDQLKAQIEEKEEKDlhERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER-REELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 922 ESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTA---AQQElrfkaNLEKNKQGLETDNKELacevkvlqqvkaeseh 998
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddADAE-----AVEARREELEDRDEEL---------------- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 999 kRKKLDAQVQELHAKVSEGDRLR---VELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETR 1075
Cdd:PRK02224 327 -RDRLEECRVAAQAHNEEAESLRedaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1076 QKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTK-----KKVDDDlGTIESLEEAKKKLlkdgEAL 1150
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEGS-PHVETIEEDRERV----EEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1151 SQRLEEKALAYDKLEKTKNRLQqelddlmvDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETK 1230
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1231 AlslaraleealeakeeferqnKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEemrtQLEELEDELQATEDAKLR 1310
Cdd:PRK02224 553 A---------------------EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE----SLERIRTLLAAIADAEDE 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1311 LEVNMQAMKAQFERDLQTRDEQNEEKKRllikqVRELEAELEDERKQRALavASKKKMEIDLKDLESQIEAANKARDEVI 1390
Cdd:PRK02224 608 IERLREKREALAELNDERRERLAEKRER-----KRELEAEFDEARIEEAR--EDKERAEEYLEQVEEKLDELREERDDLQ 680
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1335178301 1391 KQLRKLQAQMKdyqrELEEARASRDEIfaqsKESEKKLKSLEAEILQLQE---ELASSERARRHAEQER 1456
Cdd:PRK02224 681 AEIGAVENELE----ELEELRERREAL----ENRVEALEALYDEAEELESmygDLRAELRQRNVETLER 741
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1040-1676 |
1.42e-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: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1040 SLLEEAekKGI-KFSKDAASLESQLQDTQELLQeetRQKLNLSSRIRQLE--EEKNSLQEQQEEEEEARKNLEKQVLALQ 1116
Cdd:TIGR02168 159 AIFEEA--AGIsKYKERRKETERKLERTRENLD---RLEDILNELERQLKslERQAEKAERYKELKAELRELELALLVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1117 sqLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLmvdldhqRQIVSNLEKKQ 1196
Cdd:TIGR02168 234 --LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL-------ANEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1197 KKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHEL 1276
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1277 EKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLevnmqamkaqferdlqtRDEQNEEKKRLLIKQVRELEAELEDERK 1356
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERL-----------------QQEIEELLKKLEEAELKELQAELEELEE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1357 QRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK--LKSLEAE 1434
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgILGVLSE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1435 ILQLQE--ELASSERARRHAEQ---ERDELADEI----ANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRF 1505
Cdd:TIGR02168 528 LISVDEgyEAAIEAALGGRLQAvvvENLNAAKKAiaflKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1506 RKTTLQVD---------------------------------TLNAELAAERSAAQKSDNARQQ--LERQN--KELKAKLQ 1548
Cdd:TIGR02168 608 VKFDPKLRkalsyllggvlvvddldnalelakklrpgyrivTLDGDLVRPGGVITGGSAKTNSsiLERRReiEELEEKIE 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1549 ELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQL 1628
Cdd:TIGR02168 688 ELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1335178301 1629 KRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1676
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1037-1632 |
1.70e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 92.43 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1037 NVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNLS---SRIRQLEEEKNSLQEQQEEEEEARKNLEKQVL 1113
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1114 ALQSQLTDTKKKVDDdlgtIESLEEAKKKLLKDGEALSQRLEEKAlaydKLEKTKNRLQQELDDLmvdldhQRQIvSNLE 1193
Cdd:PRK03918 270 ELKKEIEELEEKVKE----LKELKEKAEEYIKLSEFYEEYLDELR----EIEKRLSRLEEEINGI------EERI-KELE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1194 KKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKAlslaraleealeakeeferQNKQLRADMEDLmsSKDDVGKNV 1273
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-------------------ELERLKKRLTGL--TPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1274 HELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamKAQFERDLQTRDEQNEEKKRLLikqvRELEAELED 1353
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELL----EEYTAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1354 ERKQRALAVASKKKMEIDLKDLESQIEAANKAR--DEVIKQLRKLQAQMKDYQRE-LEEARASRDEIFAQSKESEKKLKS 1430
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1431 LEAEILQLQE---ELASSERARRHAEQERDELADEIANSASGKSALLDEKrrleariaqleeeleeeQSNMELLNDRFRK 1507
Cdd:PRK03918 544 LKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEER-----------------LKELEPFYNEYLE 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1508 TTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAAN 1587
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELE 686
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1335178301 1588 KLVRRTEKKLKEIFMQVEdERRHADQYKEQMEKANARMKQLKRQL 1632
Cdd:PRK03918 687 KRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEELREKV 730
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
986-1668 |
6.11e-18 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 90.74 E-value: 6.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 986 VKVLQQVKAESEhKRKKLDAQVQELHAkvsEGDRLRVELAE-KANKLQNELDNVSSLLEEAEKKgikfskdAASLESQLQ 1064
Cdd:COG4913 251 IELLEPIRELAE-RYAAARERLAELEY---LRAALRLWFAQrRLELLEAELEELRAELARLEAE-------LERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1065 DTQELLQEETRQKLNLS-SRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKkkvdddlgtiESLEEAKKKL 1143
Cdd:COG4913 320 ALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA----------EEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1144 LKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISA---RYA------ 1214
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEaelPFVgeliev 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1215 EERDRAEAEAREKE--TKALSLARALEEALEAKEEFERQNKQLRADMEdlmsskdDVGKNVHELEKSKRALEQQVEEMRT 1292
Cdd:COG4913 470 RPEEERWRGAIERVlgGFALTLLVPPEHYAAALRWVNRLHLRGRLVYE-------RVRTGLPDPERPRLDPDSLAGKLDF 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1293 QLEELEDELQAtedaklRLEVNMQAMKAQFERDLQTrdeqneEKKRL----LIKQVRELeAELEDERKQRALAV----AS 1364
Cdd:COG4913 543 KPHPFRAWLEA------ELGRRFDYVCVDSPEELRR------HPRAItragQVKGNGTR-HEKDDRRRIRSRYVlgfdNR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1365 KKkmeidLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARAsrdeiFAQSKESEKKLKSLEAEILQLQEELAS 1444
Cdd:COG4913 610 AK-----LAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-----LAEYSWDEIDVASAEREIAELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1445 SERAR---RHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRK-TTLQVDTLNAELA 1520
Cdd:COG4913 680 LDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFAAAL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1521 AERSAAQKSDNARQQLERQNKELKAKLQELEGAV---KSKFKATISALEAKIGQLEE------QLEQE---AKERAAANK 1588
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMrafNREWPAETADLDADLESLPEylalldRLEEDglpEYEERFKEL 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1589 LVRRTEKKLKEIFMQVEDERRHAdqyKEQMEKANARMKQLK----RQLeeAEEEATRANASRRKLQRELDDATEANEGLS 1664
Cdd:COG4913 840 LNENSIEFVADLLSKLRRAIREI---KERIDPLNDSLKRIPfgpgRYL--RLEARPRPDPEVREFRQELRAVTSGASLFD 914
|
....
gi 1335178301 1665 REVS 1668
Cdd:COG4913 915 EELS 918
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
853-1612 |
9.17e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.59 E-value: 9.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 853 ELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAGGDDETLHKNNALKVvrelqaqiaelQEDFESEKASRNKAE 932
Cdd:PTZ00121 1089 ADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKA-----------EEARKAEDAKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 933 KQKRDLSEELEALKTELEDTLDTTAAQQELRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHA 1012
Cdd:PTZ00121 1158 RKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1013 KvsegdrlrvelAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQK---LNLSSRIRQLEE 1089
Cdd:PTZ00121 1238 D-----------AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKadeAKKAEEKKKADE 1306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1090 EKNSLQEQQEEEEEARKNLE--KQVLALQSQLTDTKKKvdddlgtieslEEAKKKLLKDGEALSQRLEEKALAYDKLEKT 1167
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEakKKADAAKKKAEEAKKA-----------AEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1168 KNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQL--LAEEKNIS---ARYAEERDRAEaEAREKETKALSLARALEEAL 1242
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELkkAAAAKKKAdeaKKKAEEKKKAD-EAKKKAEEAKKADEAKKKAE 1454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1243 EAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELE--DELQATEDAKLRLEvnmqAMKA 1320
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAKKADE----AKKA 1530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1321 QFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEaanKARDEVIKQLRKLQAQM 1400
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE---EARIEEVMKLYEEEKKM 1607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1401 KDYQ-RELEEARASRDEIfaqsKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEiansasGKSALLDEKRR 1479
Cdd:PTZ00121 1608 KAEEaKKAEEAKIKAEEL----KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE------AKKAEEDKKKA 1677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1480 LEARIAQLEEELEEEQSNMELLNDRfrkttlQVDTLNAELAAERSAAQKSDNARQqlERQNKELKAKLQELEGAVKSKFK 1559
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAK------KAEELKKKEAEEKKKAEELKKAEE--ENKIKAEEAKKEAEEDKKKAEEA 1749
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1335178301 1560 ATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHAD 1612
Cdd:PTZ00121 1750 KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1109-1676 |
1.09e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 89.71 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1109 EKQVLALQSQLTDTKKKVDDDLGTIESLEEAKkkllkdgEALSQRLEEKALAYDKLEKTknrlQQELDDLMVDLDHQRQI 1188
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQR-------EQARETRDEADEVLEEHEER----REELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1189 VSNLEKKQKKFDQLLAEEKNISARYAEERD--RAEAEAREKETKALSLARALEEaleakeefeRQNKQLRADMEDLMSSK 1266
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDdlLAEAGLDDADAEAVEARREELE---------DRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1267 DDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAklrlevnmqamkaqferdLQTRDEQNEEkkrllikqvre 1346
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREA------------------VEDRREEIEE----------- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1347 LEAELEDERKQRALAvaskkkmEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDE---------- 1416
Cdd:PRK02224 389 LEEEIEELRERFGDA-------PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpv 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1417 ----IFAQSKESEKKLKSLEAEILQLQEELASSErarrhaeqERDELADEIANSASGKSALLDEKRRLEARIAQLEEELE 1492
Cdd:PRK02224 462 egspHVETIEEDRERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1493 EEQSNMELLNDRfrkttlqVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKfkATISALEAKIGQL 1572
Cdd:PRK02224 534 EKRERAEELRER-------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIADA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1573 EEQLEqeakeraaanklvRRTEKKlkEIFMQVEDERRhadqykEQMEKANARMKQLKRQ-----LEEAEEEATRANASRR 1647
Cdd:PRK02224 605 EDEIE-------------RLREKR--EALAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLE 663
|
570 580
....*....|....*....|....*....
gi 1335178301 1648 KLQRELDDATEANEGLSREVSTLKNRLRR 1676
Cdd:PRK02224 664 QVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
849-1466 |
2.98e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 88.66 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 849 RQEEELQaKDEELLKVKEKQTKVE--GELEEMERKHQQARATAEAGGDDETLHKNNALKVVRELQAQIAELQEDFESEKA 926
Cdd:PTZ00121 1290 KKADEAK-KAEEKKKADEAKKKAEeaKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 927 SRNKAEKQKRDlSEELEALKTELEDTLDTTAAQQELRFKANLEKNKQGLETDNKEL---ACEVKVLQQVKAESEHKRKKL 1003
Cdd:PTZ00121 1369 AEKKKEEAKKK-ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAkkkAEEKKKADEAKKKAEEAKKAD 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1004 DAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSlLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNLSSR 1083
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK-ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1084 IRQLEEEKNSLQEQQEEEEEARKNLEKqvlALQSQLTDTKKKVDDDlgtiESLEEAKKKLLKDGEALSQ----RLEEKAL 1159
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKK---AEELKKAEEKKKAEEA----KKAEEDKNMALRKAEEAKKaeeaRIEEVMK 1599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1160 AYDKLEKTKNRLQQELDDLMVDLDHQR----------QIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKET 1229
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKkaeeekkkveQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1230 kalslARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTqlEELEDELQATEdakL 1309
Cdd:PTZ00121 1680 -----AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK--EAEEDKKKAEE---A 1749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1310 RLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQvreleaELEDERKQRALAVASKKKmeiDLKDLESQIEAANKARDEV 1389
Cdd:PTZ00121 1750 KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE------ELDEEDEKRRMEVDKKIK---DIFDNFANIIEGGKEGNLV 1820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1390 IKQLRKLQ-AQMKDY----QRELEEARASRDEIFAQSKESEK---KLKSLEAEILQLQEELASSERARRHAEQERDELAD 1461
Cdd:PTZ00121 1821 INDSKEMEdSAIKEVadskNMQLEEADAFEKHKFNKNNENGEdgnKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIER 1900
|
....*
gi 1335178301 1462 EIANS 1466
Cdd:PTZ00121 1901 EIPNN 1905
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
890-1621 |
3.64e-17 |
|
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: 88.10 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 890 EAGGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAA----------- 958
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLdylklneerid 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 959 --QQELRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELD 1036
Cdd:pfam02463 241 llQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1037 NVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQ 1116
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1117 SQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKnrlQQELDDLMVDLDHQRQIVSNLEKKQ 1196
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE---LEKQELKLLKDELELKKSEDLLKET 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1197 KKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSS------KDDVG 1270
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIStaviveVSATA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1271 KNVHELEKSKRALEQQVEEMRTQLEELEDELQ-----ATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQVR 1345
Cdd:pfam02463 558 DEVEERQKLVRALTELPLGARKLRLLIPKLKLplksiAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1346 ELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESE 1425
Cdd:pfam02463 638 KESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1426 KKLKSLEAEIlqlQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRf 1505
Cdd:pfam02463 718 EAEELLADRV---QEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKE- 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1506 RKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAA 1585
Cdd:pfam02463 794 EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELL 873
|
730 740 750
....*....|....*....|....*....|....*.
gi 1335178301 1586 AnKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKA 1621
Cdd:pfam02463 874 L-KEEELEEQKLKDELESKEEKEKEEKKELEEESQK 908
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
853-1541 |
7.10e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.50 E-value: 7.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 853 ELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAGGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRnKAE 932
Cdd:PTZ00121 1155 EIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK-KAE 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 933 KQKRDlseELEALKTELEDTLDTTAAQQELRFkANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHA 1012
Cdd:PTZ00121 1234 EAKKD---AEEAKKAEEERNNEEIRKFEEARM-AHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1013 KVSEGDRLRvELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKlnlssrirqlEEEKN 1092
Cdd:PTZ00121 1310 KAEEAKKAD-EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK----------EEAKK 1378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1093 SLQEQQEEEEEARKNLEkqvlaLQSQLTDTKKKVDDdlgtIESLEEAKKKllkdGEALSQRLEEKALAyDKLEKtKNRLQ 1172
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADE-----AKKKAEEDKKKADE----LKKAAAAKKK----ADEAKKKAEEKKKA-DEAKK-KAEEA 1443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1173 QELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKE-EFERQ 1251
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaEEAKK 1523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1252 NKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDE 1331
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1332 QNEEKKRLLIK--QVRELEAELEDERKQRALAVASKKKMEIDLKDLES--QIEAANKARDEVIKQLRKLQAQMKDYQREL 1407
Cdd:PTZ00121 1604 EKKMKAEEAKKaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1408 EEARASRDEIFAQSKESEKK---LKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRrleaRI 1484
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKaeeLKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK----KI 1759
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1335178301 1485 AQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNK 1541
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
957-1605 |
8.93e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 86.61 E-value: 8.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 957 AAQQELRFKaNLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELD 1036
Cdd:TIGR04523 28 ANKQDTEEK-QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1037 NVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQ 1116
Cdd:TIGR04523 107 KINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1117 SQLTDTKKKvdddlgtieslEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ 1196
Cdd:TIGR04523 187 KNIDKIKNK-----------LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1197 KKFDQLLAEEKNISARYAEERDRAEAEAREKEtkalslaraleealeakeefeRQNKQLRADMEDLMSSKD-DVGKNVHE 1275
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEKQKELEQNNKKIKELE---------------------KQLNQLKSEISDLNNQKEqDWNKELKS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1276 ----LEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFE---RDLQTRDEQNEEKK---RLLIKQVR 1345
Cdd:TIGR04523 315 elknQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEekqNEIEKLKKENQSYKqeiKNLESQIN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1346 ELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESE 1425
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1426 KKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRF 1505
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1506 RKTTL--QVDTLNAELaaersaaQKSDNARQQLERQNKELKAKLQELEgAVKSKFKATISALEAKIGQLEEQLEQEAKER 1583
Cdd:TIGR04523 555 KKENLekEIDEKNKEI-------EELKQTQKSLKKKQEEKQELIDQKE-KEKKDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
650 660
....*....|....*....|..
gi 1335178301 1584 AAANKLVRRTEKKLKEIFMQVE 1605
Cdd:TIGR04523 627 EKLSSIIKNIKSKKNKLKQEVK 648
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1003-1574 |
1.04e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 86.25 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1003 LDAQVQELHAKvsegdrlrvELAEKANKLQNELDNVSSLLEEAEKKgikfsKDAAslESQLQDTQELLQ--EETRQKLN- 1079
Cdd:PRK02224 192 LKAQIEEKEEK---------DLHERLNGLESELAELDEEIERYEEQ-----REQA--RETRDEADEVLEehEERREELEt 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1080 LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKAL 1159
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1160 AYDKLEKTKNRLQQELDDLmvdldhqrqivsnlekkqkkfDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALE 1239
Cdd:PRK02224 336 AAQAHNEEAESLREDADDL---------------------EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1240 EALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLE-----ELEDELQATEDAklrlevn 1314
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHV------- 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1315 mqamkaqferdlQTRDEQNEekkrllikQVRELEAELEDERKQRAlAVASKKKMEIDLKDLESQIEAANKARDEVIKQLR 1394
Cdd:PRK02224 468 ------------ETIEEDRE--------RVEELEAELEDLEEEVE-EVEERLERAEDLVEAEDRIERLEERREDLEELIA 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1395 KLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADeIANSASGKSALL 1474
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1475 DEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttlqVDTLNAELAAERSAAQKSDnaRQQLERQNKELKAKLQELEgAV 1554
Cdd:PRK02224 606 DEIERLREKREALAELNDERRERLAEKRER-------KRELEAEFDEARIEEARED--KERAEEYLEQVEEKLDELR-EE 675
|
570 580
....*....|....*....|
gi 1335178301 1555 KSKFKATISALEAKIGQLEE 1574
Cdd:PRK02224 676 RDDLQAEIGAVENELEELEE 695
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
967-1608 |
1.09e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.27 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 967 NLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELaEKANKLQNELDNVSSLLEEAE 1046
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1047 KKGIKFSKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEeearknlekqvlALQSQLTDTKKKV 1126
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLS------------EFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1127 DDDLGTIESLEEAKKKLLKDGEALSQRLEEkalaydkLEKTKNRLQQELddlmvdldhqrqivSNLEKKQKKFD---QLL 1203
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEE-------LKKKLKELEKRL--------------EELEERHELYEeakAKK 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1204 AEEKNISARYA-EERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRa 1282
Cdd:PRK03918 372 EELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR- 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1283 lEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQ------AMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERK 1356
Cdd:PRK03918 451 -KELLEEYTAELKRIEKELKEIEEKERKLRKELRelekvlKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1357 QRALAVASKKKMEIDLKDLESqIEAANKARDEVIKQLRKLQAQMKDYQRELEEarasrdEIFAQSKESEKKLKSLEaEIL 1436
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEK-LEELKKKLAELEKKLDELEEELAELLKELEE------LGFESVEELEERLKELE-PFY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1437 QLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEeqsnmellnDRFRKTTLQVDTLN 1516
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE---------EEYEELREEYLELS 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1517 AELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVK--SKFKATISALEAKIGQLEEqLEQEAKERAaanklVRRTE 1594
Cdd:PRK03918 673 RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKelEKLEKALERVEELREKVKK-YKALLKERA-----LSKVG 746
|
650
....*....|....
gi 1335178301 1595 KKLKEIFMQVEDER 1608
Cdd:PRK03918 747 EIASEIFEELTEGK 760
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
849-1587 |
6.73e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.42 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 849 RQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQARaTAEAGGDDETLHKNNALKVVRELQAQIAELQEDFESEKASR 928
Cdd:PTZ00121 1206 RKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK-KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 929 NKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQ 1008
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1009 ELHA--KVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAAslESQLQDTQELLQEETRQklnlSSRIRQ 1086
Cdd:PTZ00121 1365 KAEAaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA--AKKKADEAKKKAEEKKK----ADEAKK 1438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1087 LEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKALAyDKLEK 1166
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA-DEAKK 1517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1167 TKNRlqQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKnisARYAEERDRAEAEAREKETKALSLARaleealeakE 1246
Cdd:PTZ00121 1518 AEEA--KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE---LKKAEEKKKAEEAKKAEEDKNMALRK---------A 1583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1247 EFERQNKQLRAdmedlmsskDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDElqatEDAKLRLEVNMQAMKAQFERDL 1326
Cdd:PTZ00121 1584 EEAKKAEEARI---------EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA----EEEKKKVEQLKKKEAEEKKKAE 1650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1327 QTRDEQNEEKkrllIKQVRELEAELEDERKqralAVASKKKMEIDLKDLESQIEAANKARDevIKQLRKLQAQMKdyqRE 1406
Cdd:PTZ00121 1651 ELKKAEEENK----IKAAEEAKKAEEDKKK----AEEAKKAEEDEKKAAEALKKEAEEAKK--AEELKKKEAEEK---KK 1717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1407 LEEARASRDEIFAQSKESEKKlkslEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDE--KRRLEARI 1484
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEelDEEDEKRR 1793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1485 AQLEEELEEEQSNMELLNDRFRKTTLQV-DTLNAELAAERSAAQKSDNARQQLE--RQNKELKAKLQELEGAVKSKFKAT 1561
Cdd:PTZ00121 1794 MEVDKKIKDIFDNFANIIEGGKEGNLVInDSKEMEDSAIKEVADSKNMQLEEADafEKHKFNKNNENGEDGNKEADFNKE 1873
|
730 740 750
....*....|....*....|....*....|.
gi 1335178301 1562 ISALEAKIGQLEE-----QLEQEAKERAAAN 1587
Cdd:PTZ00121 1874 KDLKEDDEEEIEEadeieKIDKDDIEREIPN 1904
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
943-1482 |
1.47e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.78 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 943 EALKTELEDTLDTTAAQQELRFKANLEKNKQGLETDNKELACEVK--------------VLQQVKAESEHKRKKLD---A 1005
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIEryeeqreqaretrdEADEVLEEHEERREELEtleA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1006 QVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQlQDTQELLQEETRQKL-NLSSRI 1084
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEAR-REELEDRDEELRDRLeECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1085 RQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEakkkllkDGEALSQRLEEKALAYDKL 1164
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE-------EIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1165 EKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEK-----------NISARYAEERDRAEAEAREKETkals 1233
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsPHVETIEEDRERVEELEAELED---- 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1234 lARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEV 1313
Cdd:PRK02224 487 -LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1314 NMQAMK---AQFERDLQTRDEQNE--EKKRLLIKQVRELEAELEDERKQRAlavaskkkmeidlkdlesQIEAANKARDE 1388
Cdd:PRK02224 566 EAEEAReevAELNSKLAELKERIEslERIRTLLAAIADAEDEIERLREKRE------------------ALAELNDERRE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1389 VIKQLRKLQAQMKDYQRE--LEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELaDEIANS 1466
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEarIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERR-EALENR 706
|
570
....*....|....*.
gi 1335178301 1467 ASGKSALLDEKRRLEA 1482
Cdd:PRK02224 707 VEALEALYDEAEELES 722
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
901-1549 |
3.99e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 81.22 E-value: 3.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 901 NNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTEledtldttaaQQELRFKANLEKNK-QGLETDN 979
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQ----------IKDLNDKLKKNKDKiNKLNSDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 980 KELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASL 1059
Cdd:TIGR04523 106 SKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1060 ESQLQDTQellQEETRQKLNLSSrIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEA 1139
Cdd:TIGR04523 186 QKNIDKIK---NKLLKLELLLSN-LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1140 KKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDL--MVDLDHQRQIVSNLEKKQKKFDQL---LAEEKNISARYA 1214
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQEKKLEEIqnqISQNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1215 EERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQL 1294
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1295 EELEDELQATEDAKL-------RLEVNMQAMKAQFERDLQTRDEQNEEKKRLLiKQVRELEAELEDERKQRALAVASKKK 1367
Cdd:TIGR04523 422 ELLEKEIERLKETIIknnseikDLTNQDSVKELIIKNLDNTRESLETQLKVLS-RSINKIKQNLEQKQKELKSKEKELKK 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1368 MEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARasrDEIfaQSKESEKKLKSLEAEILQLQEELASSER 1447
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE---DEL--NKDDFELKKENLEKEIDEKNKEIEELKQ 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1448 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQ 1527
Cdd:TIGR04523 576 TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
650 660
....*....|....*....|..
gi 1335178301 1528 KSDNARQQLERQNKELKAKLQE 1549
Cdd:TIGR04523 656 EIRNKWPEIIKKIKESKTKIDD 677
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
851-1312 |
1.10e-14 |
|
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: 79.68 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 851 EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATaeaggddeTLHKNNALKVVRELQAQIAELQEDFESEKASRNK 930
Cdd:TIGR04523 179 EKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSL--------ESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 931 AEKQKRDLSEELEALKTELEDTldttaaQQELrfKANLEKNKQgLETDNKELACEVKVLQQVKAESEHKR-----KKLDA 1005
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSEK------QKEL--EQNNKKIKE-LEKQLNQLKSEISDLNNQKEQDWNKElkselKNQEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1006 QVQELHAKVSEGDRLRVELAEKANKLQNELDNVSS-------LLEEAEKKGIKFSKDAAS-------LESQLQDTQELLQ 1071
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESensekqrELEEKQNEIEKLKKENQSykqeiknLESQINDLESKIQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1072 EETRQKLNLSSRIRQLEEEKNSlqeqqeeeeearknLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALS 1151
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKEL--------------LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1152 QRLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKA 1231
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1232 LSLARALEEALEAKEEFERQNK--QLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKL 1309
Cdd:TIGR04523 548 NKDDFELKKENLEKEIDEKNKEieELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
|
...
gi 1335178301 1310 RLE 1312
Cdd:TIGR04523 628 KLS 630
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
844-1619 |
1.58e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 79.63 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 844 LLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQqarataeaggddetlhknnalKVVRELQAQIAELQEDFES 923
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE---------------------KELKKEKEEIEELEKELKE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 924 EKASRNKAEKQKRDLSEELEALKTELEDTLDTtaaqqelrFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKL 1003
Cdd:pfam02463 347 LEIKREAEEEEEEELEKLQEKLEQLEEELLAK--------KKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1004 DaqvqELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNLSSR 1083
Cdd:pfam02463 419 D----LLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1084 IRQ----LEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKAL 1159
Cdd:pfam02463 495 LEErsqkESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELP 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1160 AYDKLEKTKNRLQQELDDLMVDLDHQRQIvsNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALE 1239
Cdd:pfam02463 575 LGARKLRLLIPKLKLPLKSIAVLEIDPIL--NLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGV 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1240 EALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK---RALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQ 1316
Cdd:pfam02463 653 SLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEilrRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQD 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1317 AMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVA-----SKKKMEIDLKDLESQIEAANKARDEVIK 1391
Cdd:pfam02463 733 KINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEErekteKLKVEEEKEEKLKAQEEELRALEEELKE 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1392 QLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKS 1471
Cdd:pfam02463 813 EAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKE 892
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1472 ALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELE 1551
Cdd:pfam02463 893 EKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL 972
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1335178301 1552 GAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQME 1619
Cdd:pfam02463 973 GKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYL 1040
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
898-1626 |
1.61e-14 |
|
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: 79.50 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 898 LHKNNALKVVRELQAQIAELQEDFESEKASRNK----------AEKQKRDLSEELEALKTELEDTLDTTAAQ-QELRFKA 966
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRlshlhfgyksDETLIASRQEERQETSAELNQLLRTLDDQwKEKRDEL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 967 NLEKNKQGLETDNKElacevkvlQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAE 1046
Cdd:pfam12128 307 NGELSAADAAVAKDR--------SELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1047 KKGIKFSKDAASLESQLQDTQELLQEEtrqklnlssRIRQLEEEKNslqeqqeeeeearkNLEKQVLALQSQLTDTKKKV 1126
Cdd:pfam12128 379 RRRSKIKEQNNRDIAGIKDKLAKIREA---------RDRQLAVAED--------------DLQALESELREQLEAGKLEF 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1127 DDDLGTIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDlmvdldhQRQIVSNLEKKQKKFDQLLaEE 1206
Cdd:pfam12128 436 NEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAE-------VERLQSELRQARKRRDQAS-EA 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1207 KNISARYAEERDRAEAEARE----KETKALSLARALEEALEAKEEFERQNKQL-RADME-DLMSSKDDVGKNVHELEKSK 1280
Cdd:pfam12128 508 LRQASRRLEERQSALDELELqlfpQAGTLLHFLRKEAPDWEQSIGKVISPELLhRTDLDpEVWDGSVGGELNLYGVKLDL 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1281 RALE-----QQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFER------DLQTRDEQNEEKKRLLIKQVRELEA 1349
Cdd:pfam12128 588 KRIDvpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKasreetFARTALKNARLDLRRLFDEKQSEKD 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1350 ELEDERKQR-ALAVASKKKMEIDLKDLESQIEAANKARDEvikQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKkl 1428
Cdd:pfam12128 668 KKNKALAERkDSANERLNSLEAQLKQLDKKHQAWLEEQKE---QKREARTEKQAYWQVVEGALDAQLALLKAAIAARR-- 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1429 KSLEAEILQLQEELASSERARRHAEQERDELADEIANsasgksalldekrrLEARIAQLEEELEEEQSNMELLNDRFrkt 1508
Cdd:pfam12128 743 SGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRT--------------LERKIERIAVRRQEVLRYFDWYQETW--- 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1509 TLQVDTLNAELAAERSAAQKsdnARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGqLEEQLEQEAKERAAANk 1588
Cdd:pfam12128 806 LQRRPRLATQLSNIERAISE---LQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRG-LRCEMSKLATLKEDAN- 880
|
730 740 750
....*....|....*....|....*....|....*...
gi 1335178301 1589 lVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMK 1626
Cdd:pfam12128 881 -SEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFK 917
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
839-1573 |
5.21e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 77.70 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 839 TKVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERK---HQQARATAEAGGDDETLHKNNALKVVRELQAQIA 915
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKreaEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 916 ELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQ-ELRFKANLEKNKQGLETDNKELACEVKVLQQVKA 994
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILeEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 995 ESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEET 1074
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIST 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1075 RQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRL 1154
Cdd:pfam02463 548 AVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEG 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1155 EEKALAYDKLEKTKNRLQQELDDlMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSL 1234
Cdd:pfam02463 628 ILKDTELTKLKESAKAKESGLRK-GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQ 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1235 ARALEEALEAKEEFERQNKQLRADM----EDLMSSKDDVGKNVHELEKSKR-ALEQQVEEMRTQLEELEDELQATEDAKL 1309
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQdkinEELKLLKQKIDEEEEEEEKSRLkKEEKEEEKSELSLKEKELAEEREKTEKL 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1310 RLEV----NMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKkmeidlkdleSQIEAANKA 1385
Cdd:pfam02463 787 KVEEekeeKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK----------LEKLAEEEL 856
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1386 RDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIAN 1465
Cdd:pfam02463 857 ERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEE 936
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1466 SASGKSALLDEKRRLEARIAQLEEELEEEQSNMELL-----NDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQN 1540
Cdd:pfam02463 937 PEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELgkvnlMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
730 740 750
....*....|....*....|....*....|...
gi 1335178301 1541 KELKAKLQELEGAVKSKFKATISALEAKIGQLE 1573
Cdd:pfam02463 1017 QRLKEFLELFVSINKGWNKVFFYLELGGSAELR 1049
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
859-1578 |
6.89e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.26 E-value: 6.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 859 EELLKVKEKQTKVEGELEEMERKHQQARATAEAGGD-DETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRD 937
Cdd:COG4913 241 HEALEDAREQIELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 938 LSEELEALKTELedtldttaAQQELRFKANLEKnkqgletdnkelacEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEG 1017
Cdd:COG4913 321 LREELDELEAQI--------RGNGGDRLEQLER--------------EIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1018 DRlrvELAEKANKLQNELDNVSSLLEEAEkkgikfsKDAASLESQLQDTQEllqeetrqklnlssRIRQLEEEKNSLQEQ 1097
Cdd:COG4913 379 AE---EFAALRAEAAALLEALEEELEALE-------EALAEAEAALRDLRR--------------ELRELEAEIASLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1098 qeeeeeaRKNLEKQVLALQSQL-TDTKKKVDD-----DLGTIESLEE----AKKKLLKdGEALS----QRLEEKALAYdk 1163
Cdd:COG4913 435 -------KSNIPARLLALRDALaEALGLDEAElpfvgELIEVRPEEErwrgAIERVLG-GFALTllvpPEHYAAALRW-- 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1164 LEKTKNRLQqelddlmVDLDHQRQIVSNLEKKQKKFDQLLAE---EKN-----ISARYAEERDRA---EAEAREKETKAL 1232
Cdd:COG4913 505 VNRLHLRGR-------LVYERVRTGLPDPERPRLDPDSLAGKldfKPHpfrawLEAELGRRFDYVcvdSPEELRRHPRAI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1233 SLARaleealeakeeferqnkqlradmedLMSSkddvGKNVHELEKSKRALEQQV--EEMRTQLEELEDELQATEDAKLR 1310
Cdd:COG4913 578 TRAG-------------------------QVKG----NGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAE 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1311 LEvnmqamkaQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAvaskkkmeidlkDLESQIEAANKARDEvi 1390
Cdd:COG4913 629 AE--------ERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIA------------ELEAELERLDASSDD-- 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1391 kqLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELassERARRHAEQERDELADEIANSASGK 1470
Cdd:COG4913 687 --LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERFAAALGD 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1471 SALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKT-TLQVDTLNAELAAERSAAQKsdnaRQQLERQN-KELKAKLQ 1548
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESLPEYLAL----LDRLEEDGlPEYEERFK 837
|
730 740 750
....*....|....*....|....*....|.
gi 1335178301 1549 ELEGAVKSKFKATI-SALEAKIGQLEEQLEQ 1578
Cdd:COG4913 838 ELLNENSIEFVADLlSKLRRAIREIKERIDP 868
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
976-1631 |
8.31e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.49 E-value: 8.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 976 ETDNKELACEVKVLQQVKAESEHKRKKLDAQVQElhAKVSEGDRLRVELAEKANKLQNELDnvSSLLEEAEKKGIKFSKD 1055
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE--ARKAEEAKKKAEDARKAEEARKAED--ARKAEEARKAEDAKRVE 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1056 AASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDdlgtIES 1135
Cdd:PTZ00121 1156 IARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA----VKK 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1136 LEEAKKKllkdgealsqrlEEKAlayDKLEKTKNRLQ-QELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNIS--AR 1212
Cdd:PTZ00121 1232 AEEAKKD------------AEEA---KKAEEERNNEEiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAK 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1213 YAEERDRAEAEAR--EKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEM 1290
Cdd:PTZ00121 1297 KAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1291 RTQLEELE---DELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKqralAVASKKK 1367
Cdd:PTZ00121 1377 KKKADAAKkkaEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK----ADEAKKK 1452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1368 MEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEifAQSKESEKKlkslEAEILQLQEELASSER 1447
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE--AKKAAEAKK----KADEAKKAEEAKKADE 1526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1448 ARRHAEQERdelADEIANSASGKSAllDEKRRLE-ARIAQLEEELEEEQSNMELLNDRFRKTTL--QVDTLNAELAAERS 1524
Cdd:PTZ00121 1527 AKKAEEAKK---ADEAKKAEEKKKA--DELKKAEeLKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARIEEVMKLY 1601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1525 AAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTE---KKLKEIF 1601
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkKKAEEAK 1681
|
650 660 670
....*....|....*....|....*....|
gi 1335178301 1602 MQVEDERRHADQYKEQMEKANaRMKQLKRQ 1631
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAK-KAEELKKK 1710
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1114-1632 |
3.65e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.95 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1114 ALQSQLTDTKKKVDDdLGTIESLEEAKKKLLKDGEALSQRLEekALAYDKLEKTKNRLQQELDDLMVDLDHQRQivsNLE 1193
Cdd:COG4913 239 RAHEALEDAREQIEL-LEPIRELAERYAAARERLAELEYLRA--ALRLWFAQRRLELLEAELEELRAELARLEA---ELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1194 KKQKKFDQLLAEEKNISARYAE-----------ERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDL 1262
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGnggdrleqlerEIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1263 mssKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEqneekkRL--- 1339
Cdd:COG4913 393 ---LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEA------ELpfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1340 --LIkQVRELEAE-----------------LEDERKQRALAV--ASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQA 1398
Cdd:COG4913 464 geLI-EVRPEEERwrgaiervlggfaltllVPPEHYAAALRWvnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDF 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1399 QMKDYQRELEE-------------ARASRDEIFA-----QSKES----EKKLKSLEAEILQLQeelASSERARRHAEQER 1456
Cdd:COG4913 543 KPHPFRAWLEAelgrrfdyvcvdsPEELRRHPRAitragQVKGNgtrhEKDDRRRIRSRYVLG---FDNRAKLAALEAEL 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1457 DELADEIANSASGKSALLDEKRRLEARIAQLEEeleeeqsnmeLLNDRFRKttLQVDTLNAELAA---ERSAAQKSDNAR 1533
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQR----------LAEYSWDE--IDVASAEREIAEleaELERLDASSDDL 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1534 QQLERQNKELKAKLQELEGAVKsKFKATISALEAKIGQLEEQLEQEAKERAAANKLVR-----RTEKKLKEIfMQVEDER 1608
Cdd:COG4913 688 AALEEQLEELEAELEELEEELD-ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAA-LGDAVER 765
|
570 580
....*....|....*....|....
gi 1335178301 1609 RHADQYKEQMEKANARMKQLKRQL 1632
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEEL 789
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1359-1599 |
4.20e-13 |
|
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: 72.87 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1359 ALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQL 1438
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1439 QEELasserarrhaEQERDELADEIAnsasgksALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAE 1518
Cdd:COG4942 96 RAEL----------EAQKEELAELLR-------ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1519 LAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLK 1598
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
.
gi 1335178301 1599 E 1599
Cdd:COG4942 238 A 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
908-1467 |
8.88e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.80 E-value: 8.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 908 RELQAQIAELQEDFESEKASRNKAEK--QKRDLSEELEALKTELEDTLDTTAAQQELRFKANLEKNKQGLETDNKELAC- 984
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDarEQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEEl 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 985 --EVKVLQQVKAESEHKRKKLDAQVQELHAKVSE--GDRLRvELAEKANKLQNELDNVSSLLEEAEKK----GIKFSKDA 1056
Cdd:COG4913 301 raELARLEAELERLEARLDALREELDELEAQIRGngGDRLE-QLEREIERLERELEERERRRARLEALlaalGLPLPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1057 ASLESQLQDTQELLQEETRQKLNLS-------SRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDD 1129
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEealaeaeAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1130 L-----------------GTIESL-----------EEAKKKLLK-------------------DGEALSQRLEEKALAYd 1162
Cdd:COG4913 460 LpfvgelievrpeeerwrGAIERVlggfaltllvpPEHYAAALRwvnrlhlrgrlvyervrtgLPDPERPRLDPDSLAG- 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1163 KLEKTKNRLQQELDDLMV------------DLDHQR-------QIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAE 1223
Cdd:COG4913 539 KLDFKPHPFRAWLEAELGrrfdyvcvdspeELRRHPraitragQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1224 AREKEtKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVG---KNVHELEKSKRALEQ---QVEEMRTQLEEL 1297
Cdd:COG4913 619 LAELE-EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAsaeREIAELEAELERLDAssdDLAALEEQLEEL 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1298 EDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEidlkDLES 1377
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE----NLEE 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1378 QIEAANKARDEVIKQLRKLqaqMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEIL-QLQEELAssERARRHAEQER 1456
Cdd:COG4913 774 RIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLpEYEERFK--ELLNENSIEFV 848
|
650
....*....|.
gi 1335178301 1457 DELADEIANSA 1467
Cdd:COG4913 849 ADLLSKLRRAI 859
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
803-1230 |
1.64e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 803 RKAFAKKQQQLSALKVLQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELLKVKEKQTKVE--GELEEMER 880
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEeaKKADEAKK 1451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 881 KHQQARATAEAGGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQ 960
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 961 ELRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLD----------------AQVQELHAKVSEGDRLRVEL 1024
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDknmalrkaeeakkaeeARIEEVMKLYEEEKKMKAEE 1611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1025 AEKANKLQNELDNVSSllEEAEKKGIKFSKDAAslESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEA 1104
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKK--AEEEKKKVEQLKKKE--AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1105 RKNLEkqvlALQSQLTDTKKkvdddlgtIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLDH 1184
Cdd:PTZ00121 1688 KKAAE----ALKKEAEEAKK--------AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1335178301 1185 QRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETK 1230
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1204-1659 |
1.84e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.87 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1204 AEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRAD----MEDLMSSKDD----VGKNVHE 1275
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEdarkAEEARKAEDAkrveIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1276 ---LEKSKRALE-QQVEEMRTQLE-ELEDELQATEDAKlRLEvnmQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAE 1350
Cdd:PTZ00121 1163 arkAEEARKAEDaKKAEAARKAEEvRKAEELRKAEDAR-KAE---AARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKD 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1351 LEDERKqralavASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAqmkDYQRELEEARASRdeifaQSKESEKKLKS 1430
Cdd:PTZ00121 1239 AEEAKK------AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA---DELKKAEEKKKAD-----EAKKAEEKKKA 1304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1431 LEAEilQLQEELASSERARRHAEQERDElADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTL 1510
Cdd:PTZ00121 1305 DEAK--KKAEEAKKADEAKKKAEEAKKK-ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1511 QVDTLNAELAAERSAAQKSDNARQQLERQNK--ELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1588
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKKKAEEDKKKADELKKaaAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEE 1461
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1335178301 1589 LVRRTEKKLK-EIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEA 1659
Cdd:PTZ00121 1462 AKKKAEEAKKaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA 1533
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
31-76 |
4.74e-12 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 62.06 E-value: 4.74e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1335178301 31 TAKKLVWIPSERHGFEAASIKEERGDEVMVELaENGKKAMVNKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1376-1599 |
5.68e-12 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 69.47 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1376 ESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELasserarrhaEQE 1455
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----------EER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1456 RDELADEIA------NSASGKSALLDekrrleariAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKs 1529
Cdd:COG3883 85 REELGERARalyrsgGSVSYLDVLLG---------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEA- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1530 dnARQQLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKE 1599
Cdd:COG3883 155 --KLAELEALKAELEAAKAELEAQQAEQ-EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1005-1632 |
1.14e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 70.00 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1005 AQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNLSSRI 1084
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1085 RQLEEEKNSLQEQQEEEEeaRKNLEKQVLAL---QSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEAL---SQRLEEKA 1158
Cdd:TIGR00618 267 ARIEELRAQEAVLEETQE--RINRARKAAPLaahIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHvkqQSSIEEQR 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1159 LAYDKLEKTKNRLQQELDDLMVDLDH--------------QRQIVSNLEKKQ---KKFDQLLAEEKNISARYAEERDRAE 1221
Cdd:TIGR00618 345 RLLQTLHSQEIHIRDAHEVATSIREIscqqhtltqhihtlQQQKTTLTQKLQslcKELDILQREQATIDTRTSAFRDLQG 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1222 AEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVgknvhELEKSKRALEQQVEEMRTQLEELEDEL 1301
Cdd:TIGR00618 425 QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKERE-----QQLQTKEQIHLQETRKKAVVLARLLEL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1302 QATED--AKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRalavaskkkmeidlKDLESQI 1379
Cdd:TIGR00618 500 QEEPCplCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQR--------------ASLKEQM 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1380 EAANKARDEVIKQLRKLQAQMKDYQRELEEArasRDEIFAQSKESEKKLKSLEAEILQLQEELAsSERARRHAEQERDEL 1459
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRL---QDLTEKLSEAEDMLACEQHALLRKLQPEQD-LQDVRLHLQQCSQEL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1460 ADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMEL--LNDRFRKTTLQVDTLNAELAAERSAAQK--------- 1528
Cdd:TIGR00618 642 ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALqkMQSEKEQLTYWKEMLAQCQTLLRELETHieeydrefn 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1529 -----SDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIG------QLEEQLEQEAKERAAANKLVRRTEKKL 1597
Cdd:TIGR00618 722 eienaSSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEevtaalQTGAELSHLAAEIQFFNRLREEDTHLL 801
|
650 660 670
....*....|....*....|....*....|....*.
gi 1335178301 1598 KEIFMQVEDERRHADQYKE-QMEKANARMKQLKRQL 1632
Cdd:TIGR00618 802 KTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRL 837
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
850-1478 |
1.64e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 69.37 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 850 QEEELQAKDEEL---LKVKEKQTKVEgELEEMERKHQQARATAEAGGDDETLHKNNALK----VVRELQAQIAELQEDFE 922
Cdd:pfam05483 200 EELRVQAENARLemhFKLKEDHEKIQ-HLEEEYKKEINDKEKQVSLLLIQITEKENKMKdltfLLEESRDKANQLEEKTK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 923 SEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRFKAN------LEKNKQGLETDNKELACEVKVLQQVKAES 996
Cdd:pfam05483 279 LQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticqlTEEKEAQMEELNKAKAAHSFVVTEFEATT 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 997 EHKRKKLDAQVQELHakvSEGDRLRVelaekankLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEEtrq 1076
Cdd:pfam05483 359 CSLEELLRTEQQRLE---KNEDQLKI--------ITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEK--- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1077 klnlssriRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLE-EAKKKLLKDGEALSQRle 1155
Cdd:pfam05483 425 --------KQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKtELEKEKLKNIELTAHC-- 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1156 ekalayDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ----KKFDQLLAEEKNISARYAEERDRAEAEAREKETKA 1231
Cdd:pfam05483 495 ------DKLLLENKELTQEASDMTLELKKHQEDIINCKKQEermlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1232 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQatedaklRL 1311
Cdd:pfam05483 569 DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVN-------KL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1312 EVNMQAMKAQFERDLQTRDEQNEEKKrllIKQVRELEaelEDERKQRALAVASKKKMEIDLkdlesqieaanKARDEVIK 1391
Cdd:pfam05483 642 ELELASAKQKFEEIIDNYQKEIEDKK---ISEEKLLE---EVEKAKAIADEAVKLQKEIDK-----------RCQHKIAE 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1392 QLRKLQAQMKDYQRELEEaRASRDEIFAQSKESEKKLK-SLEAEILQLQEELASSERARRHAEQERDELADEiansASGK 1470
Cdd:pfam05483 705 MVALMEKHKHQYDKIIEE-RDSELGLYKNKEQEQSSAKaALEIELSNIKAELLSLKKQLEIEKEEKEKLKME----AKEN 779
|
....*...
gi 1335178301 1471 SALLDEKR 1478
Cdd:pfam05483 780 TAILKDKK 787
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
807-1462 |
1.64e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 69.61 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 807 AKKQQQLSALKVLqRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELlkvKEKQTKVEGELEEMERKHQQAR 886
Cdd:TIGR00618 219 ERKQVLEKELKHL-REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEEL---RAQEAVLEETQERINRARKAAP 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 887 ATAEAGGDDETLHKnnALKVVRELQAQIAELqedfESEKASRNKAEKQKRDLSEELEALKTEL-EDTLDTTAAQQELRFK 965
Cdd:TIGR00618 295 LAAHIKAVTQIEQQ--AQRIHTELQSKMRSR----AKLLMKRAAHVKQQSSIEEQRRLLQTLHsQEIHIRDAHEVATSIR 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 966 ANLEKNKQgLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELA----------EKANKLQNEL 1035
Cdd:TIGR00618 369 EISCQQHT-LTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAhakkqqelqqRYAELCAAAI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1036 DNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEAR---------- 1105
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnpgplt 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1106 ---KNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLmvdL 1182
Cdd:TIGR00618 528 rrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL---S 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1183 DHQRQIV-SNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMED 1261
Cdd:TIGR00618 605 EAEDMLAcEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQK 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1262 LMSSKDDVGKNVHELEKSK---RALEQQVEEMRTQLEELEDELQATedaklrlevnmqamkaqfERDLQTRDEQNEEKKR 1338
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQtllRELETHIEEYDREFNEIENASSSL------------------GSDLAAREDALNQSLK 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1339 LLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIF 1418
Cdd:TIGR00618 747 ELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETL 826
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1335178301 1419 AQSKES-----EKKLKSLeAEILQLQEELASSERARRHAEQERDELADE 1462
Cdd:TIGR00618 827 VQEEEQflsrlEEKSATL-GEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1374-1676 |
1.65e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.71 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1374 DLESQIEAANKARDEVIKQLrklqAQMKDYQRELEEARASRDEIfaqsKESEKKLKSLEAEILQLQEELassERARRHAE 1453
Cdd:TIGR02169 143 DVTDFISMSPVERRKIIDEI----AGVAEFDRKKEKALEELEEV----EENIERLDLIIDEKRQQLERL---RREREKAE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1454 qERDELADEIANSASgkSALLDEKRRLEARIAQLEEELEEEQSNMEllndrfrKTTLQVDTLNAELAAersaaqksdnAR 1533
Cdd:TIGR02169 212 -RYQALLKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELE-------KLTEEISELEKRLEE----------IE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1534 QQLERQNKELKAKLQELEGAVKSK---FKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRH 1610
Cdd:TIGR02169 272 QLLEELNKKIKDLGEEEQLRVKEKigeLEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1335178301 1611 ADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1676
Cdd:TIGR02169 352 RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1275-1486 |
2.62e-11 |
|
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: 67.48 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1275 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfERDLQTRDEQNEEKKRLLIKQVRELEAELEDE 1354
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1355 RKQRA--LAVASKKKMEIDLKDLESQIEAANKARD-EVIKQL-RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKS 1430
Cdd:COG4942 103 KEELAelLRALYRLGRQPPLALLLSPEDFLDAVRRlQYLKYLaPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1335178301 1431 LEAEILQLQEELASSERARRHAEQERDELADEIAnsasgksALLDEKRRLEARIAQ 1486
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELA-------ELQQEAEELEALIAR 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
844-1301 |
2.78e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.55 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 844 LLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAGGDDETLhknnaLKVVRELQAQIAELQEDFES 923
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKR-----LSRLEEEINGIEERIKELEE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 924 EKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRfkaNLEKNKQGLETDnkELACEVKVLQQVKAESEHKRKKL 1003
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE---RLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKI 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1004 DAQVQELHAKVSEGDRLRVEL-------------------AEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQ 1064
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELkkakgkcpvcgrelteehrKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1065 DTQELLQEETrqklnLSSRIRQLEEEKNS--LQEQQEEEEEARK------NLEKQVLALQSQLT---DTKKKVDDDLGTI 1133
Cdd:PRK03918 491 KESELIKLKE-----LAEQLKELEEKLKKynLEELEKKAEEYEKlkekliKLKGEIKSLKKELEkleELKKKLAELEKKL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1134 ESLEEAKKKLLK--------DGEALSQRLEEKALAYDK---LEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQL 1202
Cdd:PRK03918 566 DELEEELAELLKeleelgfeSVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1203 LAEEKNISARYAEErdraeaEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRA 1282
Cdd:PRK03918 646 RKELEELEKKYSEE------EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKA 719
|
490
....*....|....*....
gi 1335178301 1283 LEqQVEEMRTQLEELEDEL 1301
Cdd:PRK03918 720 LE-RVEELREKVKKYKALL 737
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
859-1599 |
3.19e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 68.59 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 859 EELLKVKEKQTKVEGELEEMERKHQQARATAEAggddetlhknnALKVVRELQaqiaelqedFESEKASRNKAE--KQKR 936
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIIEA-----------QRKAIQELQ---------FENEKVSLKLEEeiQENK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 937 DLSEELEALKTELEDTLDTTA--AQQELRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKV 1014
Cdd:pfam05483 145 DLIKENNATRHLCNLLKETCArsAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1015 SEGDRlrvelaEKANKLQNELDNVSSLLEEAEKKGIKFsKDAASLESQLQDTQELLQEETRQKlnlSSRIRQLEEEKNSL 1094
Cdd:pfam05483 225 QHLEE------EYKKEINDKEKQVSLLLIQITEKENKM-KDLTFLLEESRDKANQLEEKTKLQ---DENLKELIEKKDHL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1095 QeqqeeeeearKNLEKQVLALQSQLTdTKKKVDDDL----GTIESLEEAKKKLLKDG--------------EALSQRLEE 1156
Cdd:pfam05483 295 T----------KELEDIKMSLQRSMS-TQKALEEDLqiatKTICQLTEEKEAQMEELnkakaahsfvvtefEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1157 K-ALAYDKLEKTKNRLQ---QELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAE------EKNISARYAEERDRAEAE--- 1223
Cdd:pfam05483 364 LlRTEQQRLEKNEDQLKiitMELQKKSSELEEMTKFKNNKEVELEELKKILAEdeklldEKKQFEKIAEELKGKEQElif 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1224 ---AREKETKALSLarALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDE 1300
Cdd:pfam05483 444 llqAREKEIHDLEI--QLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQED 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1301 LQATEDAKLRLEVNMQAMKaqfERDLQTRDEQnEEKKRLLIKQVRELEAELEderkqralavaskkKMEIDLKDLESQIE 1380
Cdd:pfam05483 522 IINCKKQEERMLKQIENLE---EKEMNLRDEL-ESVREEFIQKGDEVKCKLD--------------KSEENARSIEYEVL 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1381 AANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASserARRHAEQERDELA 1460
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS---AKQKFEEIIDNYQ 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1461 DEIANSASGKSALLDEKRRLEARIaqleeeleeeqsnmellnDRFRKTTLQVDTLNAELAAERSAAQKSDNAR--QQLER 1538
Cdd:pfam05483 661 KEIEDKKISEEKLLEEVEKAKAIA------------------DEAVKLQKEIDKRCQHKIAEMVALMEKHKHQydKIIEE 722
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1335178301 1539 QNKEL---KAKLQElEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKE 1599
Cdd:pfam05483 723 RDSELglyKNKEQE-QSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1336-1627 |
5.85e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 67.35 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1336 KKRLLIKQVRE---LEAELEDERKQRALAVAsKKKMEIDLKD-LESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEAR 1411
Cdd:COG3206 124 RKNLTVEPVKGsnvIEISYTSPDPELAAAVA-NALAEAYLEQnLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1412 ASRDEIF--AQSKESEKKLKSLEAEILQLQEELASSErARRHAEQERDELADEIANSASGKSALldekRRLEARIAQlee 1489
Cdd:COG3206 203 QKNGLVDlsEEAKLLLQQLSELESQLAEARAELAEAE-ARLAALRAQLGSGPDALPELLQSPVI----QQLRAQLAE--- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1490 eleeeqsnmellndrfrkttlqvdtLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKI 1569
Cdd:COG3206 275 -------------------------LEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1335178301 1570 GQLEEQLEQEAKERAAANKLvrrtEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQ 1627
Cdd:COG3206 330 ASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1274-1676 |
7.78e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 7.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1274 HELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFE-RDLQTRDEQNEEKkrllIKQVRELEAELE 1352
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERLEELEER----LEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1353 DERKQRA-LAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL 1431
Cdd:COG4717 167 ELEAELAeLQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1432 EAEILQLQEELASSERARRHAEQERDELADEIANSASG-----KSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFR 1506
Cdd:COG4717 247 EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1507 KTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKakLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAA 1586
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1587 NKLVRRTEKKLKEIfmqvedERRHADQYKEQMEkanARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANE--GLS 1664
Cdd:COG4717 405 EELEEQLEELLGEL------EELLEALDEEELE---EELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELL 475
|
410
....*....|..
gi 1335178301 1665 REVSTLKNRLRR 1676
Cdd:COG4717 476 QELEELKAELRE 487
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1150-1599 |
9.39e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 9.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1150 LSQRLEEKALAYDKLE-KTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEerDRAEAEAREKE 1228
Cdd:COG4717 47 LLERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE--LREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1229 TKALSLARALEEALEAKEEFERQNKQLRADMEDLmsskddvgknvHELEKSKRALEQQVEEMRTQLEELEDELQATEDAK 1308
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEEL-----------RELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1309 L-RLEVNMQAMKAQFERdLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRAL-----------AVASKKKMEIDLKDLE 1376
Cdd:COG4717 194 LqDLAEELEELQQRLAE-LEEELEEAQEELEELEEELEQLENELEAAALEERLkearlllliaaALLALLGLGGSLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1377 SQIEAA------------------NKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQL 1438
Cdd:COG4717 273 LTIAGVlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1439 QEELASSERARR--HAEQERDELADEIA----NSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDrfrktTLQV 1512
Cdd:COG4717 353 LREAEELEEELQleELEQEIAALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----ALDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1513 DTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGavkskfKATISALEAKIGQLEEQLEQEAKERAAAN---KL 1589
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELEQLEE------DGELAELLQELEELKAELRELAEEWAALKlalEL 501
|
490
....*....|
gi 1335178301 1590 VRRTEKKLKE 1599
Cdd:COG4717 502 LEEAREEYRE 511
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
809-1551 |
1.49e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.61 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 809 KQQQLSALKVLQRNCAAYLKLRHWqwwRVFTKVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKhqqarAT 888
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKE---ILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKN-----SL 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 889 AEAGGDDETLHKNNALKVVRELQAQiAELQEDFESEKASRNKAE---KQKRDLSEELEALKTELEDTLDTTAA-----QQ 960
Cdd:TIGR00606 496 TETLKKEVKSLQNEKADLDRKLRKL-DQEMEQLNHHTTTRTQMEmltKDKMDKDEQIRKIKSRHSDELTSLLGyfpnkKQ 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 961 ELRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEgdrlrvelAEKANKLQNELDNVSS 1040
Cdd:TIGR00606 575 LEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD--------VCGSQDEESDLERLKE 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1041 LLEEAEKKGIKFSKDAASLESQLQDtqelLQEETRQKLNLSSRIRQLEEEKNSLQeqqeeeeearKNLEKQVLALQSQLt 1120
Cdd:TIGR00606 647 EIEKSSKQRAMLAGATAVYSQFITQ----LTDENQSCCPVCQRVFQTEAELQEFI----------SDLQSKLRLAPDKL- 711
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1121 dtkkkvdddlgtiESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRqivSNLEKKQKKFD 1200
Cdd:TIGR00606 712 -------------KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK---NDIEEQETLLG 775
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1201 QLLAEEKniSARYAEErDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK 1280
Cdd:TIGR00606 776 TIMPEEE--SAKVCLT-DVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLI 852
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1281 RALEQQVEEMRTQLEELEDElqatedaKLRLEVNMQamkaqferdlqtRDEQNEEKKRLLIKQVRELEAELEDERKQRAL 1360
Cdd:TIGR00606 853 QDQQEQIQHLKSKTNELKSE-------KLQIGTNLQ------------RRQQFEEQLVELSTEVQSLIREIKDAKEQDSP 913
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1361 AVASKKKMEIDLKDLESQIEAANKardevikqlrKLQAQMKDYQRELEEARASRDEIFAQSKES-EKKLKSLEAEILQLQ 1439
Cdd:TIGR00606 914 LETFLEKDQQEKEELISSKETSNK----------KAQDKVNDIKEKVKNIHGYMKDIENKIQDGkDDYLKQKETELNTVN 983
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1440 EELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAEL 1519
Cdd:TIGR00606 984 AQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENI 1063
|
730 740 750
....*....|....*....|....*....|..
gi 1335178301 1520 AAERSAAQKSDNARQQLERQNKELKAKLQELE 1551
Cdd:TIGR00606 1064 DLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1254-1586 |
1.87e-10 |
|
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: 65.09 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1254 QLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLevnmQAMKAQFERDLQTRDEQN 1333
Cdd:pfam19220 31 QLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL----VARLAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1334 EEKKRLLIK---QVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEA 1410
Cdd:pfam19220 107 EELRIELRDktaQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1411 RASRDEIFAQSKESEKKLKSLEAEILQLQ----EELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1486
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEgqlaAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1487 LEEELEEEQSNMELLNDRFRKTTLQVDT-------LNAELAAERSAAQKSDNARQQLERQ----NKELKAKLQELEGAVK 1555
Cdd:pfam19220 267 ARNQLRDRDEAIRAAERRLKEASIERDTlerrlagLEADLERRTQQFQEMQRARAELEERaemlTKALAAKDAALERAEE 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1335178301 1556 S-------------KFKATISALEAKIGQLEEQLEQEAKERAAA 1586
Cdd:pfam19220 347 RiaslsdriaeltkRFEVERAALEQANRRLKEELQRERAERALA 390
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
846-1355 |
2.12e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 65.90 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 846 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAGGDD-------------------ETLHKNNALK- 905
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDlqiatkticqlteekeaqmEELNKAKAAHs 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 906 -VVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELED-TLDTTAAQQELRFKANLEKNKQGLETDNKELA 983
Cdd:pfam05483 349 fVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmTKFKNNKEVELEELKKILAEDEKLLDEKKQFE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 984 cevKVLQQVKAESEHKRKKLDAQVQELHakvsegdRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQL 1063
Cdd:pfam05483 429 ---KIAEELKGKEQELIFLLQAREKEIH-------DLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1064 QDTQELLQEETRQKLNLSSRirqlEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVdddlgtIESLEEAKKKL 1143
Cdd:pfam05483 499 LENKELTQEASDMTLELKKH----QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF------IQKGDEVKCKL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1144 LKDGE---ALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK-----------QKKFDQLLAEEKNI 1209
Cdd:pfam05483 569 DKSEEnarSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKgsaenkqlnayEIKVNKLELELASA 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1210 SARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRadmedlMSSKDDVGKNVHELEKSKRALEQQVEE 1289
Cdd:pfam05483 649 KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEID------KRCQHKIAEMVALMEKHKHQYDKIIEE 722
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1335178301 1290 MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFeRDLQTRDEQNEEKKRLLIKQVRELEAELEDER 1355
Cdd:pfam05483 723 RDSELGLYKNKEQEQSSAKAALEIELSNIKAEL-LSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
852-1652 |
3.10e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 65.45 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 852 EELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAGgDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKA 931
Cdd:TIGR00606 203 QEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSY-ENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQM 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 932 EKQKRDLSEELEALKTELEDTLDTTAA--QQELRFKA-NLEKNKQGLETDNKElaceVKVLQQVKAESEHKRKKLDAQVQ 1008
Cdd:TIGR00606 282 EKDNSELELKMEKVFQGTDEQLNDLYHnhQRTVREKErELVDCQRELEKLNKE----RRLLNQEKTELLVEQGRLQLQAD 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1009 ELHAKVSEGDRLRVELA--------EKANKLQNELDNVSSLLEEAEKKGikfSKDAASLESQLQDTQELLQE---ETRQK 1077
Cdd:TIGR00606 358 RHQEHIRARDSLIQSLAtrleldgfERGPFSERQIKNFHTLVIERQEDE---AKTAAQLCADLQSKERLKQEqadEIRDE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1078 LNLSSRIRQLEEEKnslqeqqeeeeearknLEKQvlalQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSqRLEEK 1157
Cdd:TIGR00606 435 KKGLGRTIELKKEI----------------LEKK----QEELKFVIKELQQLEGSSDRILELDQELRKAERELS-KAEKN 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1158 ALAYDKLEKTKNRLQQELDdlmvdldhqrqivsnLEKKQKKFDQLLAEEKnisaRYAEERDRAEAEAREKETKalslara 1237
Cdd:TIGR00606 494 SLTETLKKEVKSLQNEKAD---------------LDRKLRKLDQEMEQLN----HHTTTRTQMEMLTKDKMDK------- 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1238 leealeakeefERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEdaklrlevnmqA 1317
Cdd:TIGR00606 548 -----------DEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE-----------Q 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1318 MKAQFERDLQTRDEQneekkrllikqvrelEAELEDerkqRALAVASKKKMEIDLKDLESQIEAANKardevikQLRKLQ 1397
Cdd:TIGR00606 606 NKNHINNELESKEEQ---------------LSSYED----KLFDVCGSQDEESDLERLKEEIEKSSK-------QRAMLA 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1398 AQMKDYQRELEEARASR-------DEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGK 1470
Cdd:TIGR00606 660 GATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSII 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1471 SALLDEKRRLEARIAQLEEELEEEQSNMElLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQEL 1550
Cdd:TIGR00606 740 DLKEKEIPELRNKLQKVNRDIQRLKNDIE-EQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGS 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1551 EGAVK----SKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMK 1626
Cdd:TIGR00606 819 DLDRTvqqvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQ 898
|
810 820
....*....|....*....|....*.
gi 1335178301 1627 QLKRQLEEAEEEATRANASRRKLQRE 1652
Cdd:TIGR00606 899 SLIREIKDAKEQDSPLETFLEKDQQE 924
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
907-1567 |
3.37e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 65.24 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 907 VRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRFKANLEKNKQGLETDNKELACEV 986
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 987 KVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRV----ELAEKANKLQNELDNVSsllEEAEKKGIKFSKDAASLESQ 1062
Cdd:pfam12128 347 EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSkikeQNNRDIAGIKDKLAKIR---EARDRQLAVAEDDLQALESE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1063 LQDTQELLQEETR-QKLNLSSRIRQL----------EEEKNSLQEQQEEEEEARKNLE---KQVLALQSQLTDTKKKVD- 1127
Cdd:pfam12128 424 LREQLEAGKLEFNeEEYRLKSRLGELklrlnqatatPELLLQLENFDERIERAREEQEaanAEVERLQSELRQARKRRDq 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1128 --DDLGTIE--------SLEEAKKKLLKDGEALSQRLEEKALAYD----KLEKTKNRLQQELDDLMVDLDHQRQIV---S 1190
Cdd:pfam12128 504 asEALRQASrrleerqsALDELELQLFPQAGTLLHFLRKEAPDWEqsigKVISPELLHRTDLDPEVWDGSVGGELNlygV 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1191 NLEKKQKKFDQLLAEEKNISARYA--EERDRAEAEAREKETKALSLARALEEALEAKEEFERQNkqlradmedLMSSKDD 1268
Cdd:pfam12128 584 KLDLKRIDVPEWAASEEELRERLDkaEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA---------LKNARLD 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1269 VGKNVHELEKSKRALEQQVEEMRTQLEEledELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELE 1348
Cdd:pfam12128 655 LRRLFDEKQSEKDKKNKALAERKDSANE---RLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQL 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1349 AELederKQRALAVASKKKMEIDLKDLESQIEAANKARDEviKQLRKLQAQMKDYQRELEEARASRDEI-----FAQSKE 1423
Cdd:pfam12128 732 ALL----KAAIAARRSGAKAELKALETWYKRDLASLGVDP--DVIAKLKREIRTLERKIERIAVRRQEVlryfdWYQETW 805
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1424 SEKKLKsleaeilqLQEELASSERArrhAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNd 1503
Cdd:pfam12128 806 LQRRPR--------LATQLSNIERA---ISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLA- 873
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1335178301 1504 rfrktTLQVDTLNAELAAERSaaqksdnarqQLERQNKELKAKLQELEGAVKSK---FKATISALEA 1567
Cdd:pfam12128 874 -----TLKEDANSEQAQGSIG----------ERLAQLEDLKLKRDYLSESVKKYvehFKNVIADHSG 925
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1294-1676 |
3.88e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1294 LEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLlIKQVRELEAELEDERKQRALAVASKKKME--ID 1371
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEklLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1372 LKDLESQIEAANKARDEVIKQLRKLQAQMKDY---QRELEEARASRDEIFAQ--------SKESEKKLKSLEAEILQLQE 1440
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELrelEEELEELEAELAELQEEleelleqlSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1441 ELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELA 1520
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1521 A--------ERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKL-VR 1591
Cdd:COG4717 287 AllflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1592 RTEKKLKEIFMQV----EDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATR--ANASRRKLQRELDDATEANEGLSR 1665
Cdd:COG4717 367 ELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEE 446
|
410
....*....|.
gi 1335178301 1666 EVSTLKNRLRR 1676
Cdd:COG4717 447 ELEELREELAE 457
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1253-1676 |
5.23e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1253 KQLRADMEDLMSSKDDVGKNVHELEKSKR-ALEQQVEEMRTQLEELEDELQATEDAKLRLEvnmQAMKAQFERDLQTRDE 1331
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLwFAQRRLELLEAELEELRAELARLEAELERLE---ARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1332 QNEEKKRllikQVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAankARDEVIKQLRKLQAQMKDYQRELEEAR 1411
Cdd:COG4913 332 IRGNGGD----RLEQLEREIERLERELEERERRRARLEALLAALGLPLPA---SAEEFAALRAEAAALLEALEEELEALE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1412 ASRDEIFAQSKESEKKLKSLEAEILQLqeelasseRARR-----HAEQERDELADEIANSAS------------------ 1468
Cdd:COG4913 405 EALAEAEAALRDLRRELRELEAEIASL--------ERRKsnipaRLLALRDALAEALGLDEAelpfvgelievrpeeerw 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1469 -----------GKSALLDEKR--------------------RLEARIAQLEEELEEEQS----------------NMELL 1501
Cdd:COG4913 477 rgaiervlggfALTLLVPPEHyaaalrwvnrlhlrgrlvyeRVRTGLPDPERPRLDPDSlagkldfkphpfrawlEAELG 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1502 N----------DRFRKTTLQVdTLNAELAAERSAAQKSD------------NARQQLERqnkeLKAKLQELEgavkskfk 1559
Cdd:COG4913 557 RrfdyvcvdspEELRRHPRAI-TRAGQVKGNGTRHEKDDrrrirsryvlgfDNRAKLAA----LEAELAELE-------- 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1560 ATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKeiFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEA 1639
Cdd:COG4913 624 EELAEAEERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERLDASSDDLAALEEQLEELEAEL 701
|
490 500 510
....*....|....*....|....*....|....*..
gi 1335178301 1640 TRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1676
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
846-1219 |
5.29e-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: 64.75 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 846 QVTRQEEELQAKDEELLKVKEKQTKVEGElEEMERKhqqarATAEAGGDDETLHknNALKVVRELQAQIAELQEDFESEK 925
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSSLTAQLEST-KEMLRK-----VVEELTAKKMTLE--SSERTVSDLTASLQEKERAIEATN 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 926 ASRNKAeKQKRDLS-EELEALKTELEDTLDTTAAQQELRFKANlEKNK-----------------------QGLETDNKE 981
Cdd:pfam15921 517 AEITKL-RSRVDLKlQELQHLKNEGDHLRNVQTECEALKLQMA-EKDKvieilrqqienmtqlvgqhgrtaGAMQVEKAQ 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 982 LACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANK-------LQNELDNVSSLLEEAEKKGIKFSK 1054
Cdd:pfam15921 595 LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSErlravkdIKQERDQLLNEVKTSRNELNSLSE 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1055 DAASLESQLQDTQELLQEETRQ-KLNLSSRIRQLEEEKNSLQEQQEEEEEARknleKQVLALQSQLTDTKKKVDDDLGTI 1133
Cdd:pfam15921 675 DYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQTRNTLKSMEGSDGHAM----KVAMGMQKQITAKRGQIDALQSKI 750
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1134 ESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARY 1213
Cdd:pfam15921 751 QFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQ 830
|
....*.
gi 1335178301 1214 AEERDR 1219
Cdd:pfam15921 831 EQESVR 836
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
802-1461 |
5.98e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 802 ARKAFAKKQQQLSALKVLQRNCAAYLKLR-----------HWQWWRVFTKVKpLLQ--VTRQEEELQAKDEELLKVKEKQ 868
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARerlaeleylraALRLWFAQRRLE-LLEaeLEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 869 TKVEGELEEMERKHQQArataeaGGDDETlhknnalkvvrELQAQIAELQEDFESEKASRNKAEKQKRDL-------SEE 941
Cdd:COG4913 319 DALREELDELEAQIRGN------GGDRLE-----------QLEREIERLERELEERERRRARLEALLAALglplpasAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 942 LEALKTELEDTLDTTAAQQELrfkanLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQEL------HAKVS 1015
Cdd:COG4913 382 FAALRAEAAALLEALEEELEA-----LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALrdalaeALGLD 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1016 EGD-----------------------------------------------------RLRVELAEKANKLQNELDNVSSLL 1042
Cdd:COG4913 457 EAElpfvgelievrpeeerwrgaiervlggfaltllvppehyaaalrwvnrlhlrgRLVYERVRTGLPDPERPRLDPDSL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1043 eeAEKKGIKFSKDAASLESQLQ--------DTQELLQEETR----------------------------------QKLN- 1079
Cdd:COG4913 537 --AGKLDFKPHPFRAWLEAELGrrfdyvcvDSPEELRRHPRaitragqvkgngtrhekddrrrirsryvlgfdnrAKLAa 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1080 LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQ--SQLTDTKKKVDDDLGTIESLEEAKKKLLKDG---EALSQRL 1154
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASSddlAALEEQL 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1155 EEKALAYDKLEKTKN-------RLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKnisaRYAEERDRAEAEAREK 1227
Cdd:COG4913 695 EELEAELEELEEELDelkgeigRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER----FAAALGDAVERELREN 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1228 ETKALSLARaleealeakeefeRQNKQLRADMEDLMSS-KDDVGKNVHELEKSKRALEqQVEEMRTQLEelEDEL-QATE 1305
Cdd:COG4913 771 LEERIDALR-------------ARLNRAEEELERAMRAfNREWPAETADLDADLESLP-EYLALLDRLE--EDGLpEYEE 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1306 DAKLRLEVNMQAMKAQFERDLqtRDEQNEEKKRLlikqvRELEAELEDER--KQRALavaskkkmeidlkdlesQIEAAN 1383
Cdd:COG4913 835 RFKELLNENSIEFVADLLSKL--RRAIREIKERI-----DPLNDSLKRIPfgPGRYL-----------------RLEARP 890
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1335178301 1384 KARDEVikqlrklqaqmKDYQRELEEARASRDEIFAQskESEKKLKSLEaeilQLQEELASSEraRRHAEQERDELAD 1461
Cdd:COG4913 891 RPDPEV-----------REFRQELRAVTSGASLFDEE--LSEARFAALK----RLIERLRSEE--EESDRRWRARVLD 949
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1220-1445 |
6.78e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1220 AEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELED 1299
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1300 ELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLI----------KQVRELEAELEDERKQRALAVASKKKME 1369
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1335178301 1370 IDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIfaqskesEKKLKSLEAEILQLQEELASS 1445
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL-------EALIARLEAEAAAAAERTPAA 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1429-1673 |
6.79e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1429 KSLEAEILQLQEELASSERARRHAEQERDELAdeiansasgksaLLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKT 1508
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIE------------LLEPIRELAERYAAARERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1509 tlQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1588
Cdd:COG4913 289 --RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1589 LVRRTEkklkeifMQVEDErrhADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDateanegLSREVS 1668
Cdd:COG4913 367 LLAALG-------LPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIA 429
|
....*
gi 1335178301 1669 TLKNR 1673
Cdd:COG4913 430 SLERR 434
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1144-1676 |
6.96e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 64.30 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1144 LKDGEALSQRLEE--KALAYDKLEKTKNRLQQELDDLMVDLDHQRQIV-SNLEKKQKKFDQLLAEE------KNISARYA 1214
Cdd:TIGR00606 165 LSEGKALKQKFDEifSATRYIKALETLRQVRQTQGQKVQEHQMELKYLkQYKEKACEIRDQITSKEaqlessREIVKSYE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1215 EERDRAEAEAREKE---TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK-RALEQQVEEM 1290
Cdd:TIGR00606 245 NELDPLKNRLKEIEhnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTvREKERELVDC 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1291 RTQLEELEDELQATEDAKLRLEVNMQAMKAQFER-------------DLQTRDEQNEEKKRLLIKQVRELEAELEDERKQ 1357
Cdd:TIGR00606 325 QRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqehirardsliqSLATRLELDGFERGPFSERQIKNFHTLVIERQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1358 RALAVASKKKMEIDLKDLESQiEAANKARDEVI----------KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK 1427
Cdd:TIGR00606 405 DEAKTAAQLCADLQSKERLKQ-EQADEIRDEKKglgrtielkkEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKA 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1428 LKSL------------EAEILQLQEELASSERARRHAEQERDELADEIAN-----SASGKSALLDEK-RRLEARIAQLEE 1489
Cdd:TIGR00606 484 ERELskaeknsltetlKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTrtqmeMLTKDKMDKDEQiRKIKSRHSDELT 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1490 ELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVkskFKATIS-ALEAK 1568
Cdd:TIGR00606 564 SLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL---FDVCGSqDEESD 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1569 IGQLEEQLEQEAKERA---AANKL---------------------VRRTEKKLKEIFMQVEDERRHADQYKEQMEKANAR 1624
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAmlaGATAVysqfitqltdenqsccpvcqrVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKK 720
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1335178301 1625 MKqlKRQLEEAEEEATRANASRRKlQRELDDATEANEGLSREVSTLKNRLRR 1676
Cdd:TIGR00606 721 KE--KRRDEMLGLAPGRQSIIDLK-EKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1206-1658 |
8.43e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1206 EKNISARYAEERDRAEAEAREKETKALslARALEEALEAKEEFERQNKQLRADMEDLmsskdDVGKNVHELEKSKRALEQ 1285
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1286 QVEEMRTQLEELEDELQATEDAKLRLE-VNMQAMKAQFERDLQTRDEQNEEKKRL--LIKQVRELEAELEDERKQRALAV 1362
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEeLEAELAELQEELEELLEQLSLATEEELqdLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1363 ASKKKMEIDLKDLESQIEAANKArdEVIKQLRKLQAQM-------------KDYQRELEEARASRDEIFAQSKESEKKLK 1429
Cdd:COG4717 220 EELEELEEELEQLENELEAAALE--ERLKEARLLLLIAaallallglggslLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1430 sleAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTT 1509
Cdd:COG4717 298 ---ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1510 LqVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKA-TISALEAKIGQLEEQLEQEAKERAAANK 1588
Cdd:COG4717 375 L-LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELRE 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1589 LVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1658
Cdd:COG4717 454 ELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERASE 523
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1439-1677 |
1.09e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1439 QEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAE 1518
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1519 LAAERSAAQKSDNARQQLERQNK-ELKAKLQELEGAVKSkfkatISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKL 1597
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRR-----LQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1598 KEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRRG 1677
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1023-1654 |
1.55e-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: 62.82 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1023 ELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEE--TRQKLNLSSRIRQLEEEKNSLQEQQEE 1100
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENnaTRHLCNLLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1101 EEEA-----RKNLEKQVLALQSQLTDTKK-------KVDDDLGTIESLEEAKKKLLKDGEalsqrlEEKALAYDKLEKTK 1168
Cdd:pfam05483 180 ETRQvymdlNNNIEKMILAFEELRVQAENarlemhfKLKEDHEKIQHLEEEYKKEINDKE------KQVSLLLIQITEKE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1169 NRLQqeldDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEF 1248
Cdd:pfam05483 254 NKMK----DLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1249 ERQNKqlrADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQ--ATEDAKLRLEVN-MQAMKAQFERD 1325
Cdd:pfam05483 330 TEEKE---AQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiiTMELQKKSSELEeMTKFKNNKEVE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1326 LQTRDEQNEEKKRLLI--KQVRELEAELEDERKQRALAVASKKKmeiDLKDLESQIEAANKARDEVIKQLRKLQAQMKDY 1403
Cdd:pfam05483 407 LEELKKILAEDEKLLDekKQFEKIAEELKGKEQELIFLLQAREK---EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKE 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1404 QRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERarrhaeqERDELADEIANSASGKSALLDEkrrLEAR 1483
Cdd:pfam05483 484 KLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKK-------QEERMLKQIENLEEKEMNLRDE---LESV 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1484 IAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELaaeRSAAQKSDNARQQLERQNKELKaKLQELEGAVKSKFKA--- 1560
Cdd:pfam05483 554 REEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM---KILENKCNNLKKQIENKNKNIE-ELHQENKALKKKGSAenk 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1561 TISALEAKIGQLEEQLEqeakerAAANKLVRRTEKKLKEIfmqvEDERRHADQYKEQMEKANARMKQLKrqleeaeeeat 1640
Cdd:pfam05483 630 QLNAYEIKVNKLELELA------SAKQKFEEIIDNYQKEI----EDKKISEEKLLEEVEKAKAIADEAV----------- 688
|
650
....*....|....
gi 1335178301 1641 ranasrrKLQRELD 1654
Cdd:pfam05483 689 -------KLQKEID 695
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
968-1556 |
1.57e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 63.00 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 968 LEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLD---AQVQELHAKVSEGDRLRVELAEKANKLQNELDNvsslLEE 1044
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELEnikKQIADDEKSHSITLKEIERLSIEYNNAMDDYNN----LKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1045 AEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNLSSrirqLEEEKNSLQEQQEEeeeARKNLEKQVLALQSQLTDTKK 1124
Cdd:PRK01156 240 ALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKE----LEERHMKIINDPVY---KNRNYINDYFKYKNDIENKKQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1125 KVDDDLGTIESLEEAKKKLlkdgealsQRLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLA 1204
Cdd:PRK01156 313 ILSNIDAEINKYHAIIKKL--------SVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSK 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1205 EEKNISARYAEERDRAEAEAREketkalslaraleealeakeeferqnkqLRADMEDLMSSKDDVGKNVHELEKSKRALE 1284
Cdd:PRK01156 385 NIERMSAFISEILKIQEIDPDA----------------------------IKKELNEINVKLQDISSKVSSLNQRIRALR 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1285 QQVEEMRTQLEELE-------------------------DELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRL 1339
Cdd:PRK01156 437 ENLDELSRNMEMLNgqsvcpvcgttlgeeksnhiinhynEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINK 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1340 LI---KQVRELEAELED-ERKQRALAVASKKKME-------IDLKDLESQ---------------IEAANKARDEVIKQL 1393
Cdd:PRK01156 517 SIneyNKIESARADLEDiKIKINELKDKHDKYEEiknryksLKLEDLDSKrtswlnalavislidIETNRSRSNEIKKQL 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1394 RKLQAQMKDYQRELEEARASRDEIFaqsKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELAdeiansasGKSAL 1473
Cdd:PRK01156 597 NDLESRLQEIEIGFPDDKSYIDKSI---REIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA--------EIDSI 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1474 LDEKRRLEARIAQleeeleeeqsnmelLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGA 1553
Cdd:PRK01156 666 IPDLKEITSRIND--------------IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKI 731
|
...
gi 1335178301 1554 VKS 1556
Cdd:PRK01156 732 KKA 734
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1341-1578 |
1.75e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1341 IKQVRELEAELEDERKQRALavaskkkmeidLKDLESQIEAANKARDEvIKQLRKLQAQMKDYQRELEEARAsrdeifaq 1420
Cdd:COG4913 234 FDDLERAHEALEDAREQIEL-----------LEPIRELAERYAAARER-LAELEYLRAALRLWFAQRRLELL-------- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1421 skesEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSAsgksalLDEKRRLEARIAQLEEELEEEQSNMEL 1500
Cdd:COG4913 294 ----EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1501 LNDRFRKTTLQVDTLNAELAAERSAAQ----KSDNARQQLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQL 1576
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAalleALEEELEALEEALAEAEAALRDLRRELREL-EAEIASLERRKSNIPARL 442
|
..
gi 1335178301 1577 EQ 1578
Cdd:COG4913 443 LA 444
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1257-1674 |
2.25e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1257 ADMEDLMSSKDD----VGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQ 1332
Cdd:PRK03918 189 ENIEELIKEKEKeleeVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1333 NEEKKRL--LIKQVRELEAELEDERKQRALA------VASKKKMEIDLKDLESQIEAANKARDEV-------------IK 1391
Cdd:PRK03918 269 EELKKEIeeLEEKVKELKELKEKAEEYIKLSefyeeyLDELREIEKRLSRLEEEINGIEERIKELeekeerleelkkkLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1392 QLRKLQAQMKDYQRELEEARASRDEIFAQSK--------ESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEI 1463
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKAKKEELERLKKrltgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1464 A--NSASGK----SALLDEKRRLEArIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLE 1537
Cdd:PRK03918 429 EelKKAKGKcpvcGRELTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKE 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1538 RQNKELKAKLQELEGAVK--SKFKATISALEAKIGQLEEQLEQEA---KERAAANKLVRRTEKKLKEIFMQVEDERRhad 1612
Cdd:PRK03918 508 LEEKLKKYNLEELEKKAEeyEKLKEKLIKLKGEIKSLKKELEKLEelkKKLAELEKKLDELEEELAELLKELEELGF--- 584
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1335178301 1613 qykEQMEKANARMKQLKR------QLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1674
Cdd:PRK03918 585 ---ESVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1020-1481 |
2.67e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1020 LRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQE 1099
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1100 EEE--EARKNLEKQVLALQSQLTDTKKKVDddlgTIESLEEAKKKLLKDGEALSQRLEEKalaydkLEKTKNRLQQELDD 1177
Cdd:COG4717 127 LLPlyQELEALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEEL------LEQLSLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1178 LMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRA 1257
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1258 DMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQA-----MKAQFERDLQTRDEQ 1332
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPeelleLLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1333 NEEKKRLLIKQVRELEAEL--------EDERKQRALAVASKKKMEIDLKDLESQIEAANKAR---------DEVIKQLRK 1395
Cdd:COG4717 357 EELEEELQLEELEQEIAALlaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELeellealdeEELEEELEE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1396 LQAQMKDYQRELEEARasrdeifaqskeseKKLKSLEAEILQL--QEELASSERARRHAEQERDELADEIANSASGKSAL 1473
Cdd:COG4717 437 LEEELEELEEELEELR--------------EELAELEAELEQLeeDGELAELLQELEELKAELRELAEEWAALKLALELL 502
|
....*...
gi 1335178301 1474 LDEKRRLE 1481
Cdd:COG4717 503 EEAREEYR 510
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1211-1583 |
3.30e-09 |
|
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: 61.45 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1211 ARYAEERDRaEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEM 1290
Cdd:pfam07888 49 AQEAANRQR-EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1291 RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLlikQVRELEAELEDERKQRALAVASKKkmei 1370
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL---QAKLQQTEEELRSLSKEFQELRNS---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1371 dlkdLESQIEAANKARDEVIKQLRKL-QAQMKDYQRE--LEEARASRDEIFAQSKESEKklksleaeilqLQEELAS--S 1445
Cdd:pfam07888 201 ----LAQRDTQVLQLQDTITTLTQKLtTAHRKEAENEalLEELRSLQERLNASERKVEG-----------LGEELSSmaA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1446 ERARRHAEQERDEL-ADEIANSASGKSALLDEKRrleariAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERS 1524
Cdd:pfam07888 266 QRDRTQAELHQARLqAAQLTLQLADASLALREGR------ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERM 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1525 AAQK--------SDNARQQL---ERQNKELKAKLQELEGAvKSKFKATISALEAKIGQLEEQLEQEAKER 1583
Cdd:pfam07888 340 EREKlevelgreKDCNRVQLsesRRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1039-1456 |
3.57e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1039 SSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQV--LALQ 1116
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELekLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1117 SQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDL-MVDLDHQRQIVSNLEKK 1195
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1196 QKKFDQLLAEEK-------NISARYAEERDRAEAEAREKETKALS----------------------------------- 1233
Cdd:COG4717 205 QQRLAELEEELEeaqeeleELEEELEQLENELEAAALEERLKEARlllliaaallallglggsllsliltiagvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1234 --------LARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQ--A 1303
Cdd:COG4717 285 llallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1304 TEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLiKQVRELEAELEDERK--QRALAVASKKKMEIDLKDLESQIEA 1381
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK-EELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEE 443
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1335178301 1382 ANKARDEVIKQLRKLQAQMKDY--QRELEEARASRDEIFAQskesekkLKSLEAEILQLQEELASSERARRHAEQER 1456
Cdd:COG4717 444 LEEELEELREELAELEAELEQLeeDGELAELLQELEELKAE-------LRELAEEWAALKLALELLEEAREEYREER 513
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1274-1670 |
4.47e-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: 61.89 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1274 HELEKSKRAL---EQQVEEMRTQLEE-------LEDELQATEDaklRLEVNMQAMKAQfERDLQTRDEQNEEKKRLlikq 1343
Cdd:COG3096 292 RELFGARRQLaeeQYRLVEMARELEElsaresdLEQDYQAASD---HLNLVQTALRQQ-EKIERYQEDLEELTERL---- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1344 vRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEviKQLRKLQAQMKdyQRELEEARA-------SRDE 1416
Cdd:COG3096 364 -EEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDV--QQTRAIQYQQA--VQALEKARAlcglpdlTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1417 IFAQSKESEKKLKSLEAEILQLQEELASSERARR---HAEQERDELADEIANSASGKSA--LLDEKRRLEARIAQleeel 1491
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfeKAYELVCKIAGEVERSQAWQTAreLLRRYRSQQALAQR----- 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1492 eeeqsnmellndrfrkttlqVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEgavkskfkatisALEAKIGQ 1571
Cdd:COG3096 514 --------------------LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE------------ELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1572 LEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHA--------------DQYKEQMEKANARMKQLKRQLEEAee 1637
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawlaaqdalerlrEQSGEALADSQEVTAAMQQLLERE-- 639
|
410 420 430
....*....|....*....|....*....|...
gi 1335178301 1638 eatranasrRKLQRELDDATEANEGLSREVSTL 1670
Cdd:COG3096 640 ---------REATVERDELAARKQALESQIERL 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1331-1535 |
5.02e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1331 EQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEE- 1409
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1410 --------------ARASRDEIFAQSKESEKKLKSLE----------AEILQLQEELASSERARRHAEQERDELADEIAN 1465
Cdd:COG4942 103 keelaellralyrlGRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1466 SASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQ 1535
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1086-1629 |
6.79e-09 |
|
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: 60.91 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1086 QLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEeakKKLLKDGEALSQRLEEkALAYDKLE 1165
Cdd:pfam05557 10 RLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLE---KREAEAEEALREQAEL-NRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1166 KTKNRLQQELDDLMVDLdhqRQIVSNLekkqkkfdqllaeeKNISARYAEERDRAEAEAREKETKalslaraleealeak 1245
Cdd:pfam05557 86 EALNKKLNEKESQLADA---REVISCL--------------KNELSELRRQIQRAELELQSTNSE--------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1246 eeferqnkqlradMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRT---QLEELEDELQATEDAKLRLEvNMQAMKAQF 1322
Cdd:pfam05557 134 -------------LEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQSQEQDSEIVK-NSKSELARI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1323 ---ERDLQTRDEQNE------EKKRLLIKQVRELEAELEDERKQRALAVA---SKKKMEIDLK----------------- 1373
Cdd:pfam05557 200 pelEKELERLREHNKhlneniENKLLLKEEVEDLKRKLEREEKYREEAATlelEKEKLEQELQswvklaqdtglnlrspe 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1374 DLESQIEAANKaRDEVIK--------QLRKLQAQMKDYQRELEEARasrdeifAQSKESEKKLKSLEAEILQLQEELASS 1445
Cdd:pfam05557 280 DLSRRIEQLQQ-REIVLKeenssltsSARQLEKARRELEQELAQYL-------KKIEDLNKKLKRHKALVRRLQRRVLLL 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1446 ERARRHAEQERDELADEIANSASGKSaLLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSA 1525
Cdd:pfam05557 352 TKERDGYRAILESYDKELTMSNYSPQ-LLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQ 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1526 AQKSDNA-------------------RQQLERQNKELKAKL--QELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERA 1584
Cdd:pfam05557 431 ESLADPSyskeevdslrrkletleleRQRLREQKNELEMELerRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQ 510
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1335178301 1585 AANKLVRRTEKKLKEIFMQV--------EDERRHADQYKEQMEKANARMKQLK 1629
Cdd:pfam05557 511 AEIERLKRLLKKLEDDLEQVlrlpettsTMNFKEVLDLRKELESAELKNQRLK 563
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1131-1676 |
9.96e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 60.62 E-value: 9.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1131 GTIESLEEAKKKLlkdgEALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLdhqRQIVSNLEKK-QKKFDQLLAEEKni 1209
Cdd:pfam12128 241 PEFTKLQQEFNTL----ESAELRLSHLHFGYKSDETLIASRQEERQETSAEL---NQLLRTLDDQwKEKRDELNGELS-- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1210 SARYAEERDRAEAEAREKETKALSLARALEEALEAKeeferQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQV-E 1288
Cdd:pfam12128 312 AADAAVAKDRSELEALEDQHGAFLDADIETAAADQE-----QLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIkE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1289 EMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLqtRDEQNEEKKRLLIKQVReLEAELEDERKQRALAVASKKKM 1368
Cdd:pfam12128 387 QNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL--REQLEAGKLEFNEEEYR-LKSRLGELKLRLNQATATPELL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1369 EidlkDLESQIEAANKARDEvikqLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASS--- 1445
Cdd:pfam12128 464 L----QLENFDERIERAREE----QEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQagt 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1446 --ERARRHAEQERDELADEIA-------------NSASGKSAL------LDEKR-----------RLEARIAQLEEELEE 1493
Cdd:pfam12128 536 llHFLRKEAPDWEQSIGKVISpellhrtdldpevWDGSVGGELnlygvkLDLKRidvpewaaseeELRERLDKAEEALQS 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1494 EQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLE 1573
Cdd:pfam12128 616 AREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1574 EQLeQEAKERAAANKLVRRTEKklKEIFMQVEDERRHA-DQYKEQMEkanARMKQLKRQLEEAEEEATRANASRrklqre 1652
Cdd:pfam12128 696 KKH-QAWLEEQKEQKREARTEK--QAYWQVVEGALDAQlALLKAAIA---ARRSGAKAELKALETWYKRDLASL------ 763
|
570 580
....*....|....*....|....
gi 1335178301 1653 lDDATEANEGLSREVSTLKNRLRR 1676
Cdd:pfam12128 764 -GVDPDVIAKLKREIRTLERKIER 786
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1284-1496 |
1.12e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.07 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1284 EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVA 1363
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1364 SKKKMEIDLKDLESQIEAANKArdEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELA 1443
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFS--DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1335178301 1444 SSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQS 1496
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
846-1616 |
1.23e-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: 60.35 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 846 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAGGDdetlHKN---NAL----KVVReLQAQIAELQ 918
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASD----HLNlvqTALrqqeKIER-YQEDLEELT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 919 EDFESEKASRNKAEKQKRDLSEELEA-------LKTELED---TLDT--TAA---QQELRfkaNLEKNKQGLETDNKELA 983
Cdd:COG3096 361 ERLEEQEEVVEEAAEQLAEAEARLEAaeeevdsLKSQLADyqqALDVqqTRAiqyQQAVQ---ALEKARALCGLPDLTPE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 984 CEVKVLQQVKAESEhkrkKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSllEEAEKKGIKFSKDAASLESQL 1063
Cdd:COG3096 438 NAEDYLAAFRAKEQ----QATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVER--SQAWQTARELLRRYRSQQALA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1064 QDTQELLQE--ETRQKLNLSSRIRQLEEEknsLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKK 1141
Cdd:COG3096 512 QRLQQLRAQlaELEQRLRQQQNAERLLEE---FCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1142 KLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLmVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEE----- 1216
Cdd:COG3096 589 QLRARIKELAARAPAWLAAQDALERLREQSGEALADS-QEVTAAMQQLLEREREATVERDELAARKQALESQIERlsqpg 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1217 ----------------------------RDRAEAEAREKETKA------LSLARaleealeakeefeRQNKQLRADMEDL 1262
Cdd:COG3096 668 gaedprllalaerlggvllseiyddvtlEDAPYFSALYGPARHaivvpdLSAVK-------------EQLAGLEDCPEDL 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1263 M------SSKDDVGKNVHELEK------SKRAL----------------EQQVEEMRTQLEELEDELqatedAKLRLEVN 1314
Cdd:COG3096 735 YliegdpDSFDDSVFDAEELEDavvvklSDRQWrysrfpevplfgraarEKRLEELRAERDELAEQY-----AKASFDVQ 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1315 -MQAMKAQFERDLQTR-----DEQNEEKKRLLIKQVRELEAELEDERKQralavaskkkmeidLKDLESQIEAANkardE 1388
Cdd:COG3096 810 kLQRLHQAFSQFVGGHlavafAPDPEAELAALRQRRSELERELAQHRAQ--------------EQQLRQQLDQLK----E 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1389 VIKQLRKLQAQM------------KDYQRELEEARASRDEIFAQSK---ESEKKLKSLEAEILQ---LQEELASSERARR 1450
Cdd:COG3096 872 QLQLLNKLLPQAnlladetladrlEELREELDAAQEAQAFIQQHGKalaQLEPLVAVLQSDPEQfeqLQADYLQAKEQQR 951
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1451 HAEQERDELADEIANSA----SGKSALLDEKRRLEARIAQLEEELEEEQSNmelLNDRFRKTTLQVDTLNAELAAERSAA 1526
Cdd:COG3096 952 RLKQQIFALSEVVQRRPhfsyEDAVGLLGENSDLNEKLRARLEQAEEARRE---AREQLRQAQAQYSQYNQVLASLKSSR 1028
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1527 qksDNARQQLerqnKELKAKLQELEGAV-----------KSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEK 1595
Cdd:COG3096 1029 ---DAKQQTL----QELEQELEELGVQAdaeaeerarirRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAER 1101
|
890 900
....*....|....*....|.
gi 1335178301 1596 KLKeifmqveDERRHADQYKE 1616
Cdd:COG3096 1102 DYK-------QEREQVVQAKA 1115
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1266-1486 |
1.32e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.65 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1266 KDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQAtedakLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIkQVR 1345
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARA-ELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1346 ELEAELEDERKQRALAVASKKKMEID--LKDLESQIEAANKARDEVIK-------QLRKLQAQMKDYQREL-EEARASRD 1415
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLqQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1335178301 1416 EIFAQSKESEKKLKSLEAEILQLQEELAS-SERARRHAEQERD-ELADEIANSasgksaLLdeKRRLEARIAQ 1486
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAElPELEAELRRLEREvEVARELYES------LL--QRLEEARLAE 381
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1023-1670 |
1.35e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 60.24 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1023 ELAEKANKLQNELDNVSSLleEAEKKGIKFS-KDAASLESQLQDTQELLQEETRQKLnlSSRIRQLEEEKNSLQEQQEEE 1101
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESA--ELRLSHLHFGyKSDETLIASRQEERQETSAELNQLL--RTLDDQWKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1102 EEARKNLEKQVLALQSQLtdtKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQelddlMVD 1181
Cdd:pfam12128 314 DAAVAKDRSELEALEDQH---GAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRS-----KIK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1182 LDHQRQIVSNLEKKQKKFD----QLLAEEKNISARYAEERDRAEA---EAREKETKALSLARALEEALEAKEEFERQNKQ 1254
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREardrQLAVAEDDLQALESELREQLEAgklEFNEEEYRLKSRLGELKLRLNQATATPELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1255 LRADMEDLMSSKDDVGKNVHELEKSKRAL-----------------EQQVEEMRTQLEELEDELQA----------TEDA 1307
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQSELrqarkrrdqasealrqaSRRLEERQSALDELELQLFPqagtllhflrKEAP 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1308 KLRLEVNMQAMKAQFER--------DLQTRDEQNEEKKRLLIKQVRELE-AELEDERKQRAlavaskKKMEIDLKDLESQ 1378
Cdd:pfam12128 546 DWEQSIGKVISPELLHRtdldpevwDGSVGGELNLYGVKLDLKRIDVPEwAASEEELRERL------DKAEEALQSAREK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1379 IEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQsKESEKklksleaeiLQLQEELassERARRHAEQERDE 1458
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDE-KQSEK---------DKKNKAL---AERKDSANERLNS 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1459 LADEIANSASGKSALLDEKRR--LEARIAQLeeeleeeQSNMELLNDRfrktTLQVDTLNAELAAERSAAqksDNARQQL 1536
Cdd:pfam12128 687 LEAQLKQLDKKHQAWLEEQKEqkREARTEKQ-------AYWQVVEGAL----DAQLALLKAAIAARRSGA---KAELKAL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1537 ERQNK-ELKAKLQELEgavkskfkaTISALEAKIGQLEEQLEQEAKERAAanklVRRTEKKLKEIFMQvederrHADQYK 1615
Cdd:pfam12128 753 ETWYKrDLASLGVDPD---------VIAKLKREIRTLERKIERIAVRRQE----VLRYFDWYQETWLQ------RRPRLA 813
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1335178301 1616 EQMEKANARMK----QLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTL 1670
Cdd:pfam12128 814 TQLSNIERAISelqqQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL 872
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
908-1142 |
1.37e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 908 RELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRfkaNLEKNKQGLETDNKELACEVK 987
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA------ALARRIR---ALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 988 VLQQVKAEsehKRKKLDAQVQELHaKVSEGDRLRVEL-AEKANKLQNELDNVSSLLEEAEKKgikfskdAASLESQLQDT 1066
Cdd:COG4942 94 ELRAELEA---QKEELAELLRALY-RLGRQPPLALLLsPEDFLDAVRRLQYLKYLAPARREQ-------AEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1335178301 1067 QELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKK 1142
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
933-1365 |
2.03e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 933 KQKRDLSEELEALKTELEDTLDTTAAQQELRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHA 1012
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1013 KVSEGDRLRVELAEKANKLQNELDNVSsllEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKN 1092
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLS---LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1093 SLQEQQEEEEEARK-NLEKQVLALQSQLTDTKKKVDDDLG----TIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKT 1167
Cdd:COG4717 238 AAALEERLKEARLLlLIAAALLALLGLGGSLLSLILTIAGvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1168 KNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEER---------DRAEAEAREKETKALSLARAL 1238
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEleqeiaallAEAGVEDEEELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1239 EEALEAKEEFERQNKQLRADMEDLMS--SKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDaklrlEVNMQ 1316
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEalDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELA 472
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1335178301 1317 AMKAQFERDLQTRDEQNEE--KKRLLIKQVRELEAELEDERKQRALAVASK 1365
Cdd:COG4717 473 ELLQELEELKAELRELAEEwaALKLALELLEEAREEYREERLPPVLERASE 523
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
940-1485 |
2.07e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.53 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 940 EELEALKTELEDTLDTTAA--------QQELRFKAN-LEKNKQGLETDNKELACEVKVLQQVKAESEHKRKK---LDAQV 1007
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRAeisnidylEEKLKSSNLeLENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDynnLKSAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1008 QELHAKVSEGDRLRVELAEKANKLQNELDNVSSlLEEAEKKGIKFSKDAA-----------SLESQLQDTQELLQ----- 1071
Cdd:PRK01156 242 NELSSLEDMKNRYESEIKTAESDLSMELEKNNY-YKELEERHMKIINDPVyknrnyindyfKYKNDIENKKQILSnidae 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1072 ----EETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLK-- 1145
Cdd:PRK01156 321 inkyHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKiq 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1146 --DGEALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQK--KFDQLLAEEK--NISARYAEERDR 1219
Cdd:PRK01156 401 eiDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpVCGTTLGEEKsnHIINHYNEKKSR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1220 AEAEAR--EKETKALSLARALEEALEAKEEFERQNKQLRADmeDLMSSKDdvgknvHELEKSKRAlEQQVEEMRTQLEEL 1297
Cdd:PRK01156 481 LEEKIReiEIEVKDIDEKIVDLKKRKEYLESEEINKSINEY--NKIESAR------ADLEDIKIK-INELKDKHDKYEEI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1298 EDELQAT--EDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLL---IKQVRELEAELEDErkqRALAVASKKKMEIDL 1372
Cdd:PRK01156 552 KNRYKSLklEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLndlESRLQEIEIGFPDD---KSYIDKSIREIENEA 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1373 KDLESQIEAANKARdeviKQLRKLQAQMKDYQRELEEARA---SRDEIFAQSKESEKKLKSLEAeilQLQEELASSERAR 1449
Cdd:PRK01156 629 NNLNNKYNEIQENK----ILIEKLRGKIDNYKKQIAEIDSiipDLKEITSRINDIEDNLKKSRK---ALDDAKANRARLE 701
|
570 580 590
....*....|....*....|....*....|....*.
gi 1335178301 1450 RHAEQERDELaDEIANSASGKSALLDEKRRLEARIA 1485
Cdd:PRK01156 702 STIEILRTRI-NELSDRINDINETLESMKKIKKAIG 736
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1038-1611 |
3.46e-08 |
|
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: 58.60 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1038 VSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNslqeqqEEEEEARKNLEKQVLALQS 1117
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREA------EAEEALREQAELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1118 QLTDTKKKVDDDLgTIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQK 1197
Cdd:pfam05557 85 LEALNKKLNEKES-QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1198 kfdqllaeeknisaryaeerDRAEAEAREKETKalslARALEEALEAKEEFERQNKQLR-ADMEDLMSSKDDVGKNVHEL 1276
Cdd:pfam05557 164 --------------------SLAEAEQRIKELE----FEIQSQEQDSEIVKNSKSELARiPELEKELERLREHNKHLNEN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1277 EKSKRALEQQVEEMRTQLEELE---DELQATEDAKLRLEVNMQAMKAQFE---------RDLQTRDEQNEEKKRLLIKQV 1344
Cdd:pfam05557 220 IENKLLLKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQELQSWVKLAQdtglnlrspEDLSRRIEQLQQREIVLKEEN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1345 RELEAELEDERKQRalavaskKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARA---SRDEIFAQS 1421
Cdd:pfam05557 300 SSLTSSARQLEKAR-------RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1422 KESEKKLKSLE--AEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNME 1499
Cdd:pfam05557 373 NYSPQLLERIEeaEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLET 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1500 LL--NDRFR--KTTLQVDTLNAELAAERSAA-----QKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIG 1570
Cdd:pfam05557 453 LEleRQRLReqKNELEMELERRCLQGDYDPKktkvlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLR 532
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1335178301 1571 QLEEQLEQEAKERAAANKLVRRTEKK---LKEIFMQVEDERRHA 1611
Cdd:pfam05557 533 LPETTSTMNFKEVLDLRKELESAELKnqrLKEVFQAKIQEFRDV 576
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1104-1367 |
3.76e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1104 ARKNLEKQVLALQSQLTDTKKKvdddlgtIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLmvdld 1183
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKE-------LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1184 hqrqivsnlekkQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLM 1263
Cdd:COG4942 89 ------------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1264 SSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqferdLQTRDEQNEEKKRLLIKQ 1343
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE--------LAAELAELQQEAEELEAL 228
|
250 260
....*....|....*....|....
gi 1335178301 1344 VRELEAELEDERKQRALAVASKKK 1367
Cdd:COG4942 229 IARLEAEAAAAAERTPAAGFAALK 252
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1053-1483 |
5.33e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1053 SKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEeARKNLEKQVLALQSQLtdtkKKVDDDLGT 1132
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAS-DHLNLVQTALRQQEKI----ERYQADLEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1133 IES-LEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRL---QQELDDLMVDLDHQRQIVSNLEKKQ----------KK 1198
Cdd:PRK04863 360 LEErLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLadyQQALDVQQTRAIQYQQAVQALERAKqlcglpdltaDN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1199 FDQLLAEEKNISARYAEERDRAE------AEAREKETKALSLARaleealeakeeferqnkQLRADMEdlMSSKDDVGKN 1272
Cdd:PRK04863 440 AEDWLEEFQAKEQEATEELLSLEqklsvaQAAHSQFEQAYQLVR-----------------KIAGEVS--RSEAWDVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1273 VHELEKSKRALEQQVEEMRTQLEELEDELQATEDAklrlevnmQAMKAQFERDLQTRDEQNEEKKRLLIkqvrELEAELE 1352
Cdd:PRK04863 501 LLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA--------ERLLAEFCKRLGKNLDDEDELEQLQE----ELEARLE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1353 DERKQRALAVASKKKMEIDLKDLESQIEaankardevikQLRKLQAQMKDYQRELEEARASRDEIFAQSKesekklkSLE 1432
Cdd:PRK04863 569 SLSESVSEARERRMALRQQLEQLQARIQ-----------RLAARAPAWLAAQDALARLREQSGEEFEDSQ-------DVT 630
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1335178301 1433 AEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEAR 1483
Cdd:PRK04863 631 EYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1317-1484 |
6.39e-08 |
|
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: 55.32 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1317 AMKAQFER--DLQTRDEQNEEkkrlLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLR 1394
Cdd:COG1579 1 AMPEDLRAllDLQELDSELDR----LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1395 KLQAQM---------KDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIAN 1465
Cdd:COG1579 77 KYEEQLgnvrnnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*....
gi 1335178301 1466 SAsgkSALLDEKRRLEARI 1484
Cdd:COG1579 157 EL---EELEAEREELAAKI 172
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1275-1553 |
1.11e-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: 56.67 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1275 ELEKSKRALEQQVEEM--RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRdeQNEEKKRLL-----------I 1341
Cdd:pfam17380 297 EQERLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELerirqeeiameI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1342 KQVRELE--------------AELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQREL 1407
Cdd:pfam17380 375 SRMRELErlqmerqqknervrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1408 EEARASRDEIFAQsKESEKKLKSLEAEILQLQEELASSERaRRHAEQERDEladeiansasGKSALLDEKRR---LEARI 1484
Cdd:pfam17380 455 EQERQQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQR-RKILEKELEE----------RKQAMIEEERKrklLEKEM 522
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1335178301 1485 AQLEEELEEEQSNMELLNDRFRKTTL----QVDTLNAELAAERSAAQKSDNARQQLeRQNKELKAKLQELEGA 1553
Cdd:pfam17380 523 EERQKAIYEEERRREAEEERRKQQEMeerrRIQEQMRKATEERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
931-1158 |
1.32e-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: 55.93 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 931 AEKQKRDLSEELEALKTELEDTLDTTAAQQELRfkANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQEL 1010
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEE--KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1011 HAKVsegDRLRVELAEKANKLQ--NELDNVSSLLEEAEKKgiKFSKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLE 1088
Cdd:COG4942 96 RAEL---EAQKEELAELLRALYrlGRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1089 EEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKA 1158
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1085-1632 |
1.56e-07 |
|
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: 56.67 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1085 RQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKAlayDKL 1164
Cdd:pfam15921 78 RVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV---HEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1165 EKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSlaraleealea 1244
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAIS----------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1245 keeferqnKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEdaklrlEVNMQAMKaqfER 1324
Cdd:pfam15921 224 --------KILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEH------EVEITGLT---EK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1325 DLQTRDEQNEEKKRLLIKQvreleaelEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKlqaQMKDYQ 1404
Cdd:pfam15921 287 ASSARSQANSIQSQLEIIQ--------EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEK---QLVLAN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1405 RELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELaSSERARRHAEQERDeladeiansaSGKSALLDEKRR-LEAR 1483
Cdd:pfam15921 356 SELTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL-SLEKEQNKRLWDRD----------TGNSITIDHLRReLDDR 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1484 IAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKskfkaTIS 1563
Cdd:pfam15921 425 NMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER-----TVS 499
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1335178301 1564 ALEAKIGQLEEQLEQEAKEraaANKLVRRTEKKLKEI--FMQVEDERRHA----DQYKEQMEKANARMKQLKRQL 1632
Cdd:pfam15921 500 DLTASLQEKERAIEATNAE---ITKLRSRVDLKLQELqhLKNEGDHLRNVqtecEALKLQMAEKDKVIEILRQQI 571
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1340-1630 |
2.18e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.53 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1340 LIKQVRELEAELEDERKQRALAVAskkkmeiDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFA 1419
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNE-------ELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1420 QSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKsALLDEKRRLEARIAQLEEELEEEQSNME 1499
Cdd:COG1340 86 KLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK-ELVEKIKELEKELEKAKKALEKNEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1500 LLNdRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELegavkskfKATISALEAKIGQLEEQLEQE 1579
Cdd:COG1340 165 LRA-ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL--------HKEIVEAQEKADELHEEIIEL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1335178301 1580 AKEraaanklVRRTEKKLKEIFMQVEDERRHADQyKEQMEKANARMKQLKR 1630
Cdd:COG1340 236 QKE-------LRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKK 278
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1361-1528 |
2.31e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.78 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1361 AVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQE 1440
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1441 ELASSERARrhaeqERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELA 1520
Cdd:COG1579 81 QLGNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
....*...
gi 1335178301 1521 AERSAAQK 1528
Cdd:COG1579 156 AELEELEA 163
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1168-1676 |
2.43e-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: 56.00 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1168 KNRLQ-QELDDLMVDLDHQRQIVSN---LEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARAleeale 1243
Cdd:pfam12128 215 KSRLNrQQVEHWIRDIQAIAGIMKIrpeFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAEL------ 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1244 akeeferqNKQLRADmedlmssKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFE 1323
Cdd:pfam12128 289 --------NQLLRTL-------DDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1324 RDLQTRDEQNE-------------EKKRLLIKQ--VRELEAELEDERKQRALAVASKKKMEIDLKDLESQIeaankaRDE 1388
Cdd:pfam12128 354 SELENLEERLKaltgkhqdvtakyNRRRSKIKEqnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL------REQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1389 VIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKlksleaEILQLQEELASSERARRHAEQERDELADEIANSAS 1468
Cdd:pfam12128 428 LEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQL------ENFDERIERAREEQEAANAEVERLQSELRQARKRR 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1469 GKS--ALLDEKRRLEAR-----------IAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNA--- 1532
Cdd:pfam12128 502 DQAseALRQASRRLEERqsaldelelqlFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELnly 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1533 --RQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK---LVRRTEKKLKEIFMQVEDE 1607
Cdd:pfam12128 582 gvKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASReetFARTALKNARLDLRRLFDE 661
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1335178301 1608 RRhadQYKEQMEKANARMKQLKRQleeaeeEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1676
Cdd:pfam12128 662 KQ---SEKDKKNKALAERKDSANE------RLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQ 721
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1089-1545 |
3.44e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.34 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1089 EEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDdlgtiesLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTK 1168
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEE-------LSARESDLEQDYQAASDHLNLVQTALRQQEKIE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1169 nRLQQELDDLMVDLDHQRQIVSNLekkqkkfdqllaeeknisaryAEERDRAEAEAREKETKALSLARALEEALEAKEEF 1248
Cdd:COG3096 351 -RYQEDLEELTERLEEQEEVVEEA---------------------AEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1249 ERQNKQLRadmedlmsskddvgKNVHELEKSKRALEQ---QVEEMRTQLEELEDELQATEDAKLRLEVNM---QAMKAQF 1322
Cdd:COG3096 409 QTRAIQYQ--------------QAVQALEKARALCGLpdlTPENAEDYLAAFRAKEQQATEEVLELEQKLsvaDAARRQF 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1323 ERDLQtrdeqneekkrLLIKQVRELEAE---------LEDERKQRALAvASKKKMEIDLKDLESQIEaankardevikQL 1393
Cdd:COG3096 475 EKAYE-----------LVCKIAGEVERSqawqtarelLRRYRSQQALA-QRLQQLRAQLAELEQRLR-----------QQ 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1394 RKLQAQMKDYQRELEEARASRDEIFAQSKEsekklksLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSAL 1473
Cdd:COG3096 532 QNAERLLEEFCQRIGQQLDAAEELEELLAE-------LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAW 604
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1335178301 1474 LDEKRRLEARIAQLEEELEEEQSNMEllndrFRKTTLQVDTlNAELAAERSAAQKsdnarQQLERQNKELKA 1545
Cdd:COG3096 605 LAAQDALERLREQSGEALADSQEVTA-----AMQQLLERER-EATVERDELAARK-----QALESQIERLSQ 665
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1149-1402 |
3.57e-07 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 55.03 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1149 ALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLD--HQRQIVS--NLEKKQKKFDQllAEEKNISARYAEERDRAEAEA 1224
Cdd:pfam05667 230 GLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTeaTSGASRSaqDLAELLSSFSG--SSTTDTGLTKGSRFTHTEKLQ 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1225 REKETKALSLARALEEALEAKEEFERQNK--QLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQ 1302
Cdd:pfam05667 308 FTNEAPAATSSPPTKVETEEELQQQREEEleELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1303 ATEDAKLRL---EVNMQAMKAQFE---RDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQralavASKKKMEI-DLKDL 1375
Cdd:pfam05667 388 VKKKTLDLLpdaEENIAKLQALVDasaQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDE-----SQRKLEEIkELREK 462
|
250 260
....*....|....*....|....*..
gi 1335178301 1376 ESQIEAANKARDEVIKQlrkLQAQMKD 1402
Cdd:pfam05667 463 IKEVAEEAKQKEELYKQ---LVAEYER 486
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1134-1388 |
8.73e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1134 ESLEEAKKKLlkdgEALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKkfdqllaeeknisary 1213
Cdd:COG4942 20 DAAAEAEAEL----EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA---------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1214 AEERDRAEAEAREKETKAlSLARALEEALEAKEEFERQNKQLRADMedLMSSKD--DVGKNVHELEKSKRALEQQVEEMR 1291
Cdd:COG4942 80 ALEAELAELEKEIAELRA-ELEAQKEELAELLRALYRLGRQPPLAL--LLSPEDflDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1292 TQLEELE---DELQATEDAKLRLevnmqamkaqferdlqtRDEQNEEKKRL--LIKQVRELEAELEDERKQRALAVASKK 1366
Cdd:COG4942 157 ADLAELAalrAELEAERAELEAL-----------------LAELEEERAALeaLKAERQKLLARLEKELAELAAELAELQ 219
|
250 260
....*....|....*....|..
gi 1335178301 1367 KMEIDLKDLESQIEAANKARDE 1388
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAE 241
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1110-1676 |
1.03e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.07 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1110 KQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEekalayDKLEKTKNRLQQELDDLMVDLDHQRQIV 1189
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLD------DQWKEKRDELNGELSAADAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1190 SNLEKKQKKFDQLLAEEKnisARYAEERD--RAEAEAREKETKALSlarALEEALEAKEEFERQNKQLRadmedlmsSKD 1267
Cdd:pfam12128 325 EALEDQHGAFLDADIETA---AADQEQLPswQSELENLEERLKALT---GKHQDVTAKYNRRRSKIKEQ--------NNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1268 DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDA------------KLRL-EVNMQAMKAQFERDLQTRDEQNE 1334
Cdd:pfam12128 391 DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAgklefneeeyrlKSRLgELKLRLNQATATPELLLQLENFD 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1335 EkkrlLIKQVRELE--AELEDERKQRALAVASKKKMEID--LKDLESQIEAANKARDEVIKQLRK--------LQAQMKD 1402
Cdd:pfam12128 471 E----RIERAREEQeaANAEVERLQSELRQARKRRDQASeaLRQASRRLEERQSALDELELQLFPqagtllhfLRKEAPD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1403 YQRELEEARASR--------DEIFAQSKESEKKLKS--LEAEILQLQEELASSERARRHAEQERDELADEIANSAsgksa 1472
Cdd:pfam12128 547 WEQSIGKVISPEllhrtdldPEVWDGSVGGELNLYGvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQA----- 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1473 lldekrRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQ--------LERQNKELK 1544
Cdd:pfam12128 622 ------AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDsanerlnsLEAQLKQLD 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1545 ----------------------AKLQELEGAVKSK---FKATISALE----AKIGQLEEQLEQEAKERAAANKLVRRTEK 1595
Cdd:pfam12128 696 kkhqawleeqkeqkreartekqAYWQVVEGALDAQlalLKAAIAARRsgakAELKALETWYKRDLASLGVDPDVIAKLKR 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1596 KLKEIFMQVEDERR------------------HADQYKEQMEKANARMKQLKRQLEEAEEEATRANAsrrKLQRELDDAT 1657
Cdd:pfam12128 776 EIRTLERKIERIAVrrqevlryfdwyqetwlqRRPRLATQLSNIERAISELQQQLARLIADTKLRRA---KLEMERKASE 852
|
650
....*....|....*....
gi 1335178301 1658 EANEGLSREVSTLKNRLRR 1676
Cdd:pfam12128 853 KQQVRLSENLRGLRCEMSK 871
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1330-1673 |
1.07e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1330 DEQNEEKKRLLIKQVRELEAELEDERKQRAlavASKKKMEIdlkdleSQIEAANKARD-EVIKQLRKLQ-AQMKDYQREL 1407
Cdd:PTZ00121 1090 DEATEEAFGKAEEAKKTETGKAEEARKAEE---AKKKAEDA------RKAEEARKAEDaRKAEEARKAEdAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1408 EEARasRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDEladeiansasgksallDEKRRLEARIAQL 1487
Cdd:PTZ00121 1161 EDAR--KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAE----------------EERKAEEARKAED 1222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1488 EEELEEEQSNMEllndrfrkttlqvdtlnaelaaersAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEA 1567
Cdd:PTZ00121 1223 AKKAEAVKKAEE-------------------------AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA 1277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1568 KigQLEEQleQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRR 1647
Cdd:PTZ00121 1278 R--KADEL--KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
330 340
....*....|....*....|....*.
gi 1335178301 1648 KLQRELDDATEANEGLSREVSTLKNR 1673
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
850-1090 |
1.46e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 850 QEEELQAKDEELLKVKEKQTKVEGELEEMERKhqqarataeaggddetlhKNNALKVVRELQAQIAELQEDFESEKASRN 929
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKE------------------EKALLKQLAALERRIAALARRIRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 930 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRFKANLEKNKQGL--ETDNKELACEVKVLQQVKAESEHKRKKLDAQV 1007
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1008 QELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKgikfskdAASLESQLQDTQELLQEETRQKLNLSSRIRQL 1087
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKL-------LARLEKELAELAAELAELQQEAEELEALIARL 232
|
...
gi 1335178301 1088 EEE 1090
Cdd:COG4942 233 EAE 235
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1250-1676 |
1.70e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1250 RQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQferdlqtr 1329
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQ-------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1330 deqneEKKRLLIKQVRELEAELEDErkQRALAVASKKKMEidlkdLESQIEAANKARDEvikqlrkLQAQMKDYQRELEE 1409
Cdd:PRK04863 348 -----EKIERYQADLEELEERLEEQ--NEVVEEADEQQEE-----NEARAEAAEEEVDE-------LKSQLADYQQALDV 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1410 A--RASR--------DEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDeLADEIANSasgksalLDEKRR 1479
Cdd:PRK04863 409 QqtRAIQyqqavqalERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLS-VAQAAHSQ-------FEQAYQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1480 LEARIAQLEEELEEEQSNMELLNdRFRKTTLQVDTLNAeLAAERSAAQKSDNARQQLERQNKELKAKL-QELEGAvkSKF 1558
Cdd:PRK04863 481 LVRKIAGEVSRSEAWDVARELLR-RLREQRHLAEQLQQ-LRMRLSELEQRLRQQQRAERLLAEFCKRLgKNLDDE--DEL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1559 KATISALEAKIGQLEEQLEQEAKERAAanklvrrTEKKLKEIFMQVEDERRHADQYKEqmekANARMKQLKRQLEEAEEE 1638
Cdd:PRK04863 557 EQLQEELEARLESLSESVSEARERRMA-------LRQQLEQLQARIQRLAARAPAWLA----AQDALARLREQSGEEFED 625
|
410 420 430
....*....|....*....|....*....|....*...
gi 1335178301 1639 ATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1676
Cdd:PRK04863 626 SQDVTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1253-1472 |
1.96e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1253 KQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDEL-------QATEDAKLRLEV------------ 1313
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraralYRSGGSVSYLDVllgsesfsdfld 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1314 NMQAMKAQFERDLQTRDEQNEEKKRLlikqvRELEAELEDERKQralAVASKKKMEIDLKDLESQIEAANKARDEVIKQL 1393
Cdd:COG3883 120 RLSALSKIADADADLLEELKADKAEL-----EAKKAELEAKLAE---LEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1335178301 1394 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSA 1472
Cdd:COG3883 192 AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1320-1658 |
2.20e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.03 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1320 AQFERDLQ-TRDEQNEEKKRLlIKQVREL------EAELEDE---------RKQRALAVASK-KKMEIDLKDLESQIEAA 1382
Cdd:COG3096 288 LELRRELFgARRQLAEEQYRL-VEMARELeelsarESDLEQDyqaasdhlnLVQTALRQQEKiERYQEDLEELTERLEEQ 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1383 NKARDEVIKQLRKLQAQmkdyqreLEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARR-------HAEQE 1455
Cdd:COG3096 367 EEVVEEAAEQLAEAEAR-------LEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARAlcglpdlTPENA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1456 RDELADEIANSASGKSALLDEKRRLeariaqleeeleeeqSNMELLNDRFRKTTLQVDTLNAELaaERSAAqkSDNARQQ 1535
Cdd:COG3096 440 EDYLAAFRAKEQQATEEVLELEQKL---------------SVADAARRQFEKAYELVCKIAGEV--ERSQA--WQTAREL 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1536 LeRQNKELKAKLQELEgavkskfkatisALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKeifmqvederrHADQYK 1615
Cdd:COG3096 501 L-RRYRSQQALAQRLQ------------QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----------AAEELE 556
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1335178301 1616 EQMEKANARMKQLKRQLEeaeeeatRANASRRKLQRELDDATE 1658
Cdd:COG3096 557 ELLAELEAQLEELEEQAA-------EAVEQRSELRQQLEQLRA 592
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
910-1566 |
2.22e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.52 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 910 LQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEdTLDTTAAQQELRFkanlEKNKQGLETDNKELACEVKVL 989
Cdd:pfam10174 93 LQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELF-LLRKTLEEMELRI----ETQKQTLGARDESIKKLLEML 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 990 Q-----QVKAESEHKRKK----LDAQVQE----LHAKVSEGDRLRVELAEKaNKLQNELDNVSSLLEEAEKKGIKFSkda 1056
Cdd:pfam10174 168 QskglpKKSGEEDWERTRriaeAEMQLGHlevlLDQKEKENIHLREELHRR-NQLQPDPAKTKALQTVIEMKDTKIS--- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1057 aSLESQlqdtqellqeetrqklnlssrIRQLEEEKNSLQEQQEEEEEARKNLEKQV------------------------ 1112
Cdd:pfam10174 244 -SLERN---------------------IRDLEDEVQMLKTNGLLHTEDREEEIKQMevykshskfmknkidqlkqelskk 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1113 ----LALQSQLTDTKKKVDDDLGTIESLEE---AKKK----LLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLMVD 1181
Cdd:pfam10174 302 eselLALQTKLETLTNQNSDCKQHIEVLKEsltAKEQraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGE 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1182 LDHQRQIVSNLEKK----QKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLaraleealeakeeferqnkqlrA 1257
Cdd:pfam10174 382 IRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL----------------------T 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1258 DMEDLMSSKDDVGKNV-HELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQferdlQTRDEQNEEK 1336
Cdd:pfam10174 440 TLEEALSEKERIIERLkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEH-----ASSLASSGLK 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1337 KRLLIKQvreLEAELEDERKQRALAVASKKKMEidlkdlesQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDE 1416
Cdd:pfam10174 515 KDSKLKS---LEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVER 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1417 IFAQSKESE-------KKLKSLEAEILQLQEELASSERARRHAEQERDEladeiansasgKSALLDEkrrlEARIAQLEE 1489
Cdd:pfam10174 584 LLGILREVEnekndkdKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK-----------KGAQLLE----EARRREDNL 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1490 ELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSD----NARQQLERQNKE-LKAKLQELEGAVKSKfKATISA 1564
Cdd:pfam10174 649 ADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDghltNLRAERRKQLEEiLEMKQEALLAAISEK-DANIAL 727
|
..
gi 1335178301 1565 LE 1566
Cdd:pfam10174 728 LE 729
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1081-1305 |
2.24e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1081 SSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKvdddlgtIESLEEAKKKLLKDGEALSQRLEEKALA 1160
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR-------IAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1161 YDKLEKTKNRLQQELDDLMVDL-DHQRQIVSNLEKKQKKFDQLLAEEKNIsaRYAEERDRAEAEAREKETKAL-SLARAL 1238
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYL--KYLAPARREQAEELRADLAELaALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1335178301 1239 EEALEAKEEFERQNKQLRADMEDLMSSKDDVgknVHELEKSKRALEQQVEEMRTQLEELEDELQATE 1305
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1275-1676 |
2.44e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.66 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1275 ELEKSKRALEQQVEEMRTQLEELEDELQATEDA---------KLRLEVNMQAMKAQFERDLQTRDEQnEEKKRLLIKQVR 1345
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREAlqqtqqshaYLTQKREAQEEQLKKQQLLKQLRAR-IEELRAQEAVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1346 ELEAELEDERKQRALAVASKKKMEIDLKDLE--SQIEAANKARDEVIKQLRKLQAQMKDY--QRELEEARASRDEIFAQS 1421
Cdd:TIGR00618 281 ETQERINRARKAAPLAAHIKAVTQIEQQAQRihTELQSKMRSRAKLLMKRAAHVKQQSSIeeQRRLLQTLHSQEIHIRDA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1422 KESEK-------KLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSAsgksALLDEKRRLEARIAQLEEELEEE 1494
Cdd:TIGR00618 361 HEVATsireiscQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATID----TRTSAFRDLQGQLAHAKKQQELQ 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1495 QSNMELLNDRFRKTTlqvDTLNAELAAERSAAQKSDNARQQLerQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEE 1574
Cdd:TIGR00618 437 QRYAELCAAAITCTA---QCEKLEKIHLQESAQSLKEREQQL--QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCI 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1575 QLEQEAKERAAANKLVRRT----------EKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQleeaeeeATRANA 1644
Cdd:TIGR00618 512 HPNPARQDIDNPGPLTRRMqrgeqtyaqlETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC-------DNRSKE 584
|
410 420 430
....*....|....*....|....*....|..
gi 1335178301 1645 SRRKLQRELDDATEANEGLSREVSTLKNRLRR 1676
Cdd:TIGR00618 585 DIPNLQNITVRLQDLTEKLSEAEDMLACEQHA 616
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1221-1650 |
2.59e-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: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1221 EAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDE 1300
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1301 LQATEDAKLRLEVNMQAMKAQFErDLQTRDEQNEEKKRLLIKQ--------VRELEAELEDERKQRALAVASKKKMEIDL 1372
Cdd:pfam05483 178 REETRQVYMDLNNNIEKMILAFE-ELRVQAENARLEMHFKLKEdhekiqhlEEEYKKEINDKEKQVSLLLIQITEKENKM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1373 KDLE----------SQIEAANKARDEVIKQLRKLQAQMkdyQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEEL 1442
Cdd:pfam05483 257 KDLTflleesrdkaNQLEEKTKLQDENLKELIEKKDHL---TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1443 ASSERARRHAEQERDELADEI-ANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNaELAA 1521
Cdd:pfam05483 334 EAQMEELNKAKAAHSFVVTEFeATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE-ELKK 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1522 ERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFK----------ATISALEAKIGQLEEQLEQEAKERAAANKLVR 1591
Cdd:pfam05483 413 ILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKeihdleiqltAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA 492
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1335178301 1592 RTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQ 1650
Cdd:pfam05483 493 HCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELE 551
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1371-1665 |
2.95e-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: 51.61 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1371 DLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARR 1450
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1451 HAEQERDELADEIANsasgKSALLdekRRLEARIAQLEEELEeeqsNMELLNDRFRKTTLQVDTLNAELAAER-SAAQKS 1529
Cdd:pfam19220 101 EAEAAKEELRIELRD----KTAQA---EALERQLAAETEQNR----ALEEENKALREEAQAAEKALQRAEGELaTARERL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1530 DNARQQLERQNK----------ELKAKLQELEG----------AVKSKFKATISALEAKIGQLEEQLEQEAKERA----- 1584
Cdd:pfam19220 170 ALLEQENRRLQAlseeqaaelaELTRRLAELETqldatrarlrALEGQLAAEQAERERAEAQLEEAVEAHRAERAslrmk 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1585 --AANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEG 1662
Cdd:pfam19220 250 leALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEM 329
|
...
gi 1335178301 1663 LSR 1665
Cdd:pfam19220 330 LTK 332
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
853-1035 |
3.04e-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: 50.31 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 853 ELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAggddetlhknnALKVVRELQAQIAELQEDFESEKASRNKAE 932
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEA-----------AKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 933 KQKRDLS--EELEALKTELEdtldTTAAQQELRFKANLEKNKQgLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQEL 1010
Cdd:COG1579 80 EQLGNVRnnKEYEALQKEIE----SLKRRISDLEDEILELMER-IEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170 180
....*....|....*....|....*
gi 1335178301 1011 HAkvsEGDRLRVELAEKANKLQNEL 1035
Cdd:COG1579 155 EA---ELEELEAEREELAAKIPPEL 176
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1162-1405 |
3.39e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.94 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1162 DKLEKTKNR-LQQELDDLMVDLDH-QRQIVS--------------NLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAR 1225
Cdd:PHA02562 169 DKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1226 EKETKALSLARALEEALEAKEEFERQNKQLRadmedlMSSKDDV----GKNVHELEKSKRALEQQVEEMRTQLEELEDEL 1301
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEQFQKVIK------MYEKGGVcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1302 QatEDAKLRLEVNMQAMKAqfeRDLQTRDEQNEEKKRLLIKQVRELEAELEderkqralavaskkKMEIDLKDLESQIEA 1381
Cdd:PHA02562 323 D--ELEEIMDEFNEQSKKL---LELKNKISTNKQSLITLVDKAKKVKAAIE--------------ELQAEFVDNAEELAK 383
|
250 260
....*....|....*....|....
gi 1335178301 1382 ANKARDEVIKQLRKLqaQMKDYQR 1405
Cdd:PHA02562 384 LQDELDKIVKTKSEL--VKEKYHR 405
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
844-1486 |
3.61e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.26 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 844 LLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAGGDDetlhknnalkvVRELQAQIAELQEDFEs 923
Cdd:COG3096 339 VQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEE-----------VDSLKSQLADYQQALD- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 924 EKASRNKAEKQKRDLSEELEALkTELEDTLDTTAAQQELRFKANLEknkqgletdnkELACEVKVLQQVKAESEHKRKKL 1003
Cdd:COG3096 407 VQQTRAIQYQQAVQALEKARAL-CGLPDLTPENAEDYLAAFRAKEQ-----------QATEEVLELEQKLSVADAARRQF 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1004 DAQVQELHAKVSEGDRLR-----VELAEKANKLQNELDNVSSL-------------LEEAEKKGIKFSKDAASLESQLQD 1065
Cdd:COG3096 475 EKAYELVCKIAGEVERSQawqtaRELLRRYRSQQALAQRLQQLraqlaeleqrlrqQQNAERLLEEFCQRIGQQLDAAEE 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1066 TQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQV---LALQSQLTDTKKKVDDDLGTIESLEEAKKK 1142
Cdd:COG3096 555 LEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawLAAQDALERLREQSGEALADSQEVTAAMQQ 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1143 LLKDGEALSQRLEEKALAYDKLEKTKNRLQQ-------EL----------------DDLMVD--------LDHQRQ--IV 1189
Cdd:COG3096 635 LLEREREATVERDELAARKQALESQIERLSQpggaedpRLlalaerlggvllseiyDDVTLEdapyfsalYGPARHaiVV 714
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1190 SNLEKKQKKFDQLLAEEKNI------------SARYAEERDRAEA---------------------EAREKETKALSLAR 1236
Cdd:COG3096 715 PDLSAVKEQLAGLEDCPEDLyliegdpdsfddSVFDAEELEDAVVvklsdrqwrysrfpevplfgrAAREKRLEELRAER 794
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1237 ALEEALEAKEEFERQNKQ-LRADMEDLMSSKDDVG--------------------KNVHELEKSKRALEQQVEEMRTQL- 1294
Cdd:COG3096 795 DELAEQYAKASFDVQKLQrLHQAFSQFVGGHLAVAfapdpeaelaalrqrrseleRELAQHRAQEQQLRQQLDQLKEQLq 874
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1295 ---------------------EELEDELQATEDAKLRLEVNMQAMkAQFER---DLQTRDEQNEEkkrlLIKQVRELEAE 1350
Cdd:COG3096 875 llnkllpqanlladetladrlEELREELDAAQEAQAFIQQHGKAL-AQLEPlvaVLQSDPEQFEQ----LQADYLQAKEQ 949
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1351 LEDERKQ---------RALAVASKKKMEI-----DLKD-LESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRD 1415
Cdd:COG3096 950 QRRLKQQifalsevvqRRPHFSYEDAVGLlgensDLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRD 1029
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1335178301 1416 EIFAQSKESEKKLKSLEaeilqLQEELASSERARrhaeQERDELADEIANSASGKSALLDEKRRLEARIAQ 1486
Cdd:COG3096 1030 AKQQTLQELEQELEELG-----VQADAEAEERAR----IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1136-1543 |
4.06e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1136 LEEAKKKLlkdgEALSQRLEEKALAYDKLEKTKNRLQQELDDL-------MVDLDHQRQI---VSNLEKKQKKfdqlLAE 1205
Cdd:PRK04863 295 LYTSRRQL----AAEQYRLVEMARELAELNEAESDLEQDYQAAsdhlnlvQTALRQQEKIeryQADLEELEER----LEE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1206 EKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKskraLEQ 1285
Cdd:PRK04863 367 QNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLCGLPDLTADN----AED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1286 QVEEMRTQLEELEDELQATEDaKLRLEvnmQAMKAQFERDLQtrdeqneekkrLLIKQVRELEAE---------LEDERK 1356
Cdd:PRK04863 443 WLEEFQAKEQEATEELLSLEQ-KLSVA---QAAHSQFEQAYQ-----------LVRKIAGEVSRSeawdvarelLRRLRE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1357 QRALAvASKKKMEIDLKDLESQIE---AANKARDEVIKQLRKLQAQMKDYQRELEEarasrdeifaqskesekklksLEA 1433
Cdd:PRK04863 508 QRHLA-EQLQQLRMRLSELEQRLRqqqRAERLLAEFCKRLGKNLDDEDELEQLQEE---------------------LEA 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1434 EILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLND---RFRKTTL 1510
Cdd:PRK04863 566 RLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQlleRERELTV 645
|
410 420 430
....*....|....*....|....*....|...
gi 1335178301 1511 QVDtlnaelaaeRSAAQKsdnarQQLERQNKEL 1543
Cdd:PRK04863 646 ERD---------ELAARK-----QALDEEIERL 664
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1138-1646 |
4.49e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1138 EAKKKLLKDGEALSQRLEEKALAYD-------KLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNIS 1210
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAkkkslhgKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1211 ARYAEERDRAEAEAREKetkalslaraleealeakeefeRQNKQLRADMEDLMSSKDDVGKNVHELEKSKRAL-----EQ 1285
Cdd:TIGR00618 243 AYLTQKREAQEEQLKKQ----------------------QLLKQLRARIEELRAQEAVLEETQERINRARKAAplaahIK 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1286 QVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQferdlqtrdEQNEEKKRLLIKQVRELEAELEDERKQRALAVASK 1365
Cdd:TIGR00618 301 AVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ---------QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIS 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1366 KKMEID---LKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEEL 1442
Cdd:TIGR00618 372 CQQHTLtqhIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1443 ASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIA-----------------------QLEEELEEEQSNME 1499
Cdd:TIGR00618 452 QCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLArllelqeepcplcgscihpnparQDIDNPGPLTRRMQ 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1500 LLNDRFRKTTLQVDTLNAELAAERSAAQkSDNARQQLERQN--------KELKAKLQELEGAVKSKFKATISALEAKIGQ 1571
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQLTSERKQRA-SLKEQMQEIQQSfsiltqcdNRSKEDIPNLQNITVRLQDLTEKLSEAEDML 610
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1335178301 1572 LEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQY---KEQMEKANARMKQLKRQLEEAEEEATRANASR 1646
Cdd:TIGR00618 611 ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLtltQERVREHALSIRVLPKELLASRQLALQKMQSE 688
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1003-1361 |
4.51e-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: 51.22 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1003 LDAQVQEL---HAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKkgikfskDAASLESQLQDTQELLQEETRQKLN 1079
Cdd:pfam19220 36 IEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEG-------ELEELVARLAKLEAALREAEAAKEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1080 LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKAL 1159
Cdd:pfam19220 109 LRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1160 AYDKLEKTKNRLQQELDDlmvdldhQRQIVSNLEKKqkkfdqlLAEEKNISARYAEERDrAEAEAREKETKALSLarALE 1239
Cdd:pfam19220 189 ELAELTRRLAELETQLDA-------TRARLRALEGQ-------LAAEQAERERAEAQLE-EAVEAHRAERASLRM--KLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1240 EALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLE--VNM-- 1315
Cdd:pfam19220 252 ALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEerAEMlt 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1335178301 1316 ---QAMKAQFER------DLQTRDEQNE---EKKRLLIKQ-VRELEAELEDERKQRALA 1361
Cdd:pfam19220 332 kalAAKDAALERaeeriaSLSDRIAELTkrfEVERAALEQaNRRLKEELQRERAERALA 390
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1346-1592 |
4.53e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.84 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1346 ELEAELeDERKQRALAVASKKKMEIDLK---DLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1422
Cdd:PRK11281 40 DVQAQL-DALNKQKLLEAEDKLVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1423 ES------EKKLKSLEAEILQLQEELAS-----------SERARR---HAEQERDELADEIANSASGKSALLDEKR-RLE 1481
Cdd:PRK11281 119 STlslrqlESRLAQTLDQLQNAQNDLAEynsqlvslqtqPERAQAalyANSQRLQQIRNLLKGGKVGGKALRPSQRvLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1482 ARIAQleeeleeeqsnMELLNDRFRK-----TTLQvDTLNA--ELAAERSaaqksdnarQQLERQnkelkakLQELEGAV 1554
Cdd:PRK11281 199 AEQAL-----------LNAQNDLQRKslegnTQLQ-DLLQKqrDYLTARI---------QRLEHQ-------LQLLQEAI 250
|
250 260 270
....*....|....*....|....*....|....*...
gi 1335178301 1555 KSKfkatisALEAKIGQLEEQLEQEAKERAAANKLVRR 1592
Cdd:PRK11281 251 NSK------RLTLSEKTVQEAQSQDEAARIQANPLVAQ 282
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1288-1673 |
4.57e-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: 51.56 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1288 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFerdlqTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKK 1367
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEK 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1368 MEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL------------KSLEAEI 1435
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIsdlnnqkeqdwnKELKSEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1436 LQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTL 1515
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1516 NAELAAERSAAQKSDNARQQLErQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQeakeraaANKLVRRTEK 1595
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQ-QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN-------LDNTRESLET 468
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1335178301 1596 KLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQleeaeeeatranasRRKLQRELDDateanegLSREVSTLKNR 1673
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE--------------KKELEEKVKD-------LTKKISSLKEK 525
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
952-1231 |
5.37e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 51.76 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 952 TLDTTAAQQELRFKANLEKNKQGLETDNKELACEVKvlQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVElAEKankl 1031
Cdd:NF012221 1506 KLTAKAGSNRLEFKGTGHNDGLGYILDNVVATSESS--QQADAVSKHAKQDDAAQNALADKERAEADRQRLE-QEK---- 1578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1032 QNELDNVSSLLEEAEkkgikfSKDAASLESQLQDTQELLQEETRQ-KLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEK 1110
Cdd:NF012221 1579 QQQLAAISGSQSQLE------STDQNALETNGQAQRDAILEESRAvTKELTTLAQGLDALDSQATYAGESGDQWRNPFAG 1652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1111 QVLA-LQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKAlaydklEKTKNRLQQELDDLMVDLDHQRQ-- 1187
Cdd:NF012221 1653 GLLDrVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG------EQNQANAEQDIDDAKADAEKRKDda 1726
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1335178301 1188 IVSNLEKKQKKFDQLLAEEKnisARYAEERDRAEAEAREKETKA 1231
Cdd:NF012221 1727 LAKQNEAQQAESDANAAAND---AQSRGEQDASAAENKANQAQA 1767
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1113-1676 |
6.49e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 51.29 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1113 LALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNL 1192
Cdd:pfam07111 55 LEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1193 EK-KQKKFD--QLLAEEKNISARYAEERDRA----EAEAREKETKALSLARalEEALEAKEEFERQNKQLRadmEDLMSS 1265
Cdd:pfam07111 135 EEgSQRELEeiQRLHQEQLSSLTQAHEEALSsltsKAEGLEKSLNSLETKR--AGEAKQLAEAQKEAELLR---KQLSKT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1266 KDDVGKNVHELEKSKRALEQQV------EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEkkrl 1339
Cdd:pfam07111 210 QEELEAQVTLVESLRKYVGEQVppevhsQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEE---- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1340 LIKQVRELEA-ELEDERKQRALAVASKKKMEIdlkdLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIF 1418
Cdd:pfam07111 286 LTRKIQPSDSlEPEFPKKCRSLLNRWREKVFA----LMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRAL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1419 aQSKESEKKLKSLEAEILQLqeELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEeeleeeqSNM 1498
Cdd:pfam07111 362 -QDKAAEVEVERMSAKGLQM--ELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAV-------ARI 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1499 ELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNA-----------------RQQLERQNKELKAKLQELEGAVKSKFKAT 1561
Cdd:pfam07111 432 PSLSNRLSYAVRKVHTIKGLMARKVALAQLRQEScpppppappvdadlsleLEQLREERNRLDAELQLSAHLIQQEVGRA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1562 ISALEAKIGQLEE---QLEQEakeraaanklVRRTEKKLKEIFMQVEDERRHADQYKEqmEKANARMKQLKRQLEEAEEE 1638
Cdd:pfam07111 512 REQGEAERQQLSEvaqQLEQE----------LQRAQESLASVGQQLEVARQGQQESTE--EAASLRQELTQQQEIYGQAL 579
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1335178301 1639 ATRANASRRKLQRELDDA----TEANEGLSREVSTLKNRLRR 1676
Cdd:pfam07111 580 QEKVAEVETRLREQLSDTkrrlNEARREQAKAVVSLRQIQHR 621
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
851-1445 |
6.67e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 851 EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAGGDD-----ETLHKNNAL-KVVRELQAQIAELQEDFESE 924
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDynnlkSALNELSSLeDMKNRYESEIKTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 925 KASRNK----AEKQKRDLSEELEALKTELEDTLDTTAAQQELR-FKANLEKNKQGLETDNKELAcevkVLQQVKAESEHK 999
Cdd:PRK01156 269 LEKNNYykelEERHMKIINDPVYKNRNYINDYFKYKNDIENKKqILSNIDAEINKYHAIIKKLS----VLQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1000 RKKLDaqvqelhakvsEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKfSKDAASLESQLQDTQELLQEETRQKLN 1079
Cdd:PRK01156 345 KSRYD-----------DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKN-IERMSAFISEILKIQEIDPDAIKKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1080 -LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQltDTKKKVDDDLGtieslEEAKKKLLKDGEALSQRLEEKA 1158
Cdd:PRK01156 413 eINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQ--SVCPVCGTTLG-----EEKSNHIINHYNEKKSRLEEKI 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1159 laydklektkNRLQQELDDLMVDLDHQRQIVSNLEKkqKKFDQLLAEEKNISARYAEERD--RAEAEAREKETKAlSLAR 1236
Cdd:PRK01156 486 ----------REIEIEVKDIDEKIVDLKKRKEYLES--EEINKSINEYNKIESARADLEDikIKINELKDKHDKY-EEIK 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1237 ALEEALEAKEEFERQNKQLRA-------DMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRT----QLEELEDELQATE 1305
Cdd:PRK01156 553 NRYKSLKLEDLDSKRTSWLNAlavisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSyidkSIREIENEANNLN 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1306 DAKLRLEVNMQAMkaqferdlqtrdeqneEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKA 1385
Cdd:PRK01156 633 NKYNEIQENKILI----------------EKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKAN 696
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1386 RDEvikqLRKLQAQMKDYQRELEEARASRDEIFaqskESEKKLKSLEAEILQLQEELASS 1445
Cdd:PRK01156 697 RAR----LESTIEILRTRINELSDRINDINETL----ESMKKIKKAIGDLKRLREAFDKS 748
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
845-1166 |
6.93e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 845 LQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERkhqqarataeaggddetlhknnaLKVVRELQAQIAELQEDFES- 923
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESE-----------------------LIKLKELAEQLKELEEKLKKy 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 924 --EKASRNKAEKQKrdLSEELEALKTELEDTLDttaaqqELRFKANLEKNKQGLETDNKELacevkvlqqvkaesEHKRK 1001
Cdd:PRK03918 516 nlEELEKKAEEYEK--LKEKLIKLKGEIKSLKK------ELEKLEELKKKLAELEKKLDEL--------------EEELA 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1002 KLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKgikfskdAASLESQLQDTQELLQEETRQKLNLS 1081
Cdd:PRK03918 574 ELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKE-------LKKLEEELDKAFEELAETEKRLEELR 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1082 SRIRQL-----EEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALS--QRL 1154
Cdd:PRK03918 647 KELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALErvEEL 726
|
330
....*....|..
gi 1335178301 1155 EEKALAYDKLEK 1166
Cdd:PRK03918 727 REKVKKYKALLK 738
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
846-1605 |
8.31e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 846 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAGGDDETLhKNNAL----KVVR------ELQAQIA 915
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNL-VQTALrqqeKIERyqadleELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 916 ELQEDFESEKASRNKAEKQKRDLSEELEALKTELED---TLDT--TAAQQELRFKANLEKNKQGLETDNKELACEVKVLQ 990
Cdd:PRK04863 366 EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADyqqALDVqqTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 991 QVKAESehkrKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSllEEAEKKGIKFSKDAASLESQLQDTQELl 1070
Cdd:PRK04863 446 EFQAKE----QEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSR--SEAWDVARELLRRLREQRHLAEQLQQL- 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1071 qeetRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEAL 1150
Cdd:PRK04863 519 ----RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAR 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1151 SQRLEEKALAYDKLEKTKNRLQ----------QELDDLMVD-LDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDR 1219
Cdd:PRK04863 595 IQRLAARAPAWLAAQDALARLReqsgeefedsQDVTEYMQQlLERERELTVERDELAARKQALDEEIERLSQPGGSEDPR 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1220 AEAEAREKETKALSL-------------------ARaLEEALEAKEEFERQNKQLRADMEDLM------SSKDDVGKNVH 1274
Cdd:PRK04863 675 LNALAERFGGVLLSEiyddvsledapyfsalygpAR-HAIVVPDLSDAAEQLAGLEDCPEDLYliegdpDSFDDSVFSVE 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1275 ELEKS----------------------KRALEQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFERDLQTR-- 1329
Cdd:PRK04863 754 ELEKAvvvkiadrqwrysrfpevplfgRAAREKRIEQLRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGSHla 828
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1330 ---DEQNEEKKRLLIKQVRELEAELED----ERKQRALAVASKKKMEiDLKDLESQIEAAnkARDEVIKQLRKLQAQMKd 1402
Cdd:PRK04863 829 vafEADPEAELRQLNRRRVELERALADhesqEQQQRSQLEQAKEGLS-ALNRLLPRLNLL--ADETLADRVEEIREQLD- 904
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1403 yqrELEEARASRDE---IFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSAS----------G 1469
Cdd:PRK04863 905 ---EAEEAKRFVQQhgnALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHfsyedaaemlA 981
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1470 KSALLDEKrrLEARIAQleeeleeEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAqksDNARQQLerqnKELKAKLQE 1549
Cdd:PRK04863 982 KNSDLNEK--LRQRLEQ-------AEQERTRAREQLRQAQAQLAQYNQVLASLKSSY---DAKRQML----QELKQELQD 1045
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1335178301 1550 L-----EGAV------KSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVE 1605
Cdd:PRK04863 1046 LgvpadSGAEerararRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVV 1112
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1273-1674 |
9.68e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 50.41 E-value: 9.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1273 VHELEKSKrALEQQVEEMRTQLEELEDELQATEDAKLR----LEVN---MQAMKAQFERdLQTRDEQNEEKKRLLIKQVR 1345
Cdd:pfam05701 31 IQTVERRK-LVELELEKVQEEIPEYKKQSEAAEAAKAQvleeLESTkrlIEELKLNLER-AQTEEAQAKQDSELAKLRVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1346 ELEAELEDErkqraLAVASKKKMEIDLKDLESQIEAANKARDEvikqLRKLQAQMKDYQRELEEARASRDEIFAQSKESE 1425
Cdd:pfam05701 109 EMEQGIADE-----ASVAAKAQLEVAKARHAAAVAELKSVKEE----LESLRKEYASLVSERDIAIKRAEEAVSASKEIE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1426 KKLKSLEAEILQLQEELASSERARRHAEQERDELA-----DEIANSASGKSALlDEKRRLEARIAQLEEELEEEQSNMEL 1500
Cdd:pfam05701 180 KTVEELTIELIATKESLESAHAAHLEAEEHRIGAAlareqDKLNWEKELKQAE-EELQRLNQQLLSAKDLKSKLETASAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1501 LNDrfrkttlqvdtLNAELAAERSAAQKSDNARQQLERQ-NKELKAKL----QELEGAVKSKFKAT--ISALEAKIGQLE 1573
Cdd:pfam05701 259 LLD-----------LKAELAAYMESKLKEEADGEGNEKKtSTSIQAALasakKELEEVKANIEKAKdeVNCLRVAAASLR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1574 EQLEQEAKERAAanklVRRTEKKLKEIFMQVEDERRHADQ----YKEQMEKANARMKQLKRQLEEAEEEATRANASRRKL 1649
Cdd:pfam05701 328 SELEKEKAELAS----LRQREGMASIAVSSLEAELNRTKSeialVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAA 403
|
410 420
....*....|....*....|....*
gi 1335178301 1650 QRELDDATEANEGLSREVSTLKNRL 1674
Cdd:pfam05701 404 REELRKAKEEAEQAKAAASTVESRL 428
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1053-1657 |
1.09e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.72 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1053 SKDAASLESQLQDTQELLQEETRQKLNLSsriRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQltdtkKKVD---DD 1129
Cdd:COG3096 284 SERALELRRELFGARRQLAEEQYRLVEMA---RELEELSARESDLEQDYQAASDHLNLVQTALRQQ-----EKIEryqED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1130 LGTIES-LEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRL---QQELDDLMVDLDHQRQIVSNLEKKQKkfdqlLAE 1205
Cdd:COG3096 356 LEELTErLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyQQALDVQQTRAIQYQQAVQALEKARA-----LCG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1206 EKNISARYAEERdRAEAEAREKE-TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKD--DVGKNVHELEKSKRA 1282
Cdd:COG3096 431 LPDLTPENAEDY-LAAFRAKEQQaTEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQawQTARELLRRYRSQQA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1283 LEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqAMKAQFERDLQTRDEQNEEKKrllikqvrELEAELEDERKQRALAV 1362
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQQQNAERLLE----EFCQRIGQQLDAAEELEELLA--------ELEAQLEELEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1363 ASKKKMEIDLKDLESQI--------------EAANKARDEVIKQLRKLQAQMKDYQRELE---EARASRDEIFAQSKESE 1425
Cdd:COG3096 578 EQRSELRQQLEQLRARIkelaarapawlaaqDALERLREQSGEALADSQEVTAAMQQLLErerEATVERDELAARKQALE 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1426 KKLKSL-------EAEILQLQEELA------------------------------------------------------- 1443
Cdd:COG3096 658 SQIERLsqpggaeDPRLLALAERLGgvllseiyddvtledapyfsalygparhaivvpdlsavkeqlagledcpedlyli 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1444 ------------------------SSERARR-----------------HAEQ---ERDELADEIANSASGKSALLDEKRR 1479
Cdd:COG3096 738 egdpdsfddsvfdaeeledavvvkLSDRQWRysrfpevplfgraarekRLEElraERDELAEQYAKASFDVQKLQRLHQA 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1480 LEARIAQLEEELEEEQSNMELLNDRFRKTTLQvDTLNAELAAERSAAQKSDNARQQLERQNK------------------ 1541
Cdd:COG3096 818 FSQFVGGHLAVAFAPDPEAELAALRQRRSELE-RELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanlladetladrle 896
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1542 ELKAKLQELEGAVKS--KFKATISALEAKIGQL------EEQLEQEAKERAAANKLVRRTEKKLKEIFmqvedERRHADQ 1613
Cdd:COG3096 897 ELREELDAAQEAQAFiqQHGKALAQLEPLVAVLqsdpeqFEQLQADYLQAKEQQRRLKQQIFALSEVV-----QRRPHFS 971
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1335178301 1614 YKE--QMEKANARM-KQLKRQLEEAEEEATRANASRRKLQRELDDAT 1657
Cdd:COG3096 972 YEDavGLLGENSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYN 1018
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
657-681 |
1.11e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 47.34 E-value: 1.11e-05
10 20
....*....|....*....|....*
gi 1335178301 657 YKESLTKLMATLRNTNPNFVRCIIP 681
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
846-1228 |
1.25e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 846 QVTRQEEELQAKDEELLKVKEKQTKV-EGELEEMERKHQQARATAEAGGDDEtLHKNNALKVVRELQaQIAELQEDFESE 924
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKAdEAKKAEEAKKADEAKKAEEAKKADE-AKKAEEKKKADELK-KAEELKKAEEKK 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 925 KASRNKAEKQKRDLS----------------EELEALKTELEDTLDTTAAQQELRFKA----NLEKNKQGLETDNKELAC 984
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMAlrkaeeakkaeearieEVMKLYEEEKKMKAEEAKKAEEAKIKAeelkKAEEEKKKVEQLKKKEAE 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 985 EVKVLQQ---------VKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKD 1055
Cdd:PTZ00121 1645 EKKKAEElkkaeeenkIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA 1724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1056 AASLESQLQDTQELLQEETRQklnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALqsqltdTKKKVDDDLGTIES 1135
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV------IEEELDEEDEKRRM 1794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1136 LEEAKKKLLKDGEALSQRLEEKALAYdkLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAE 1215
Cdd:PTZ00121 1795 EVDKKIKDIFDNFANIIEGGKEGNLV--INDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNK 1872
|
410
....*....|...
gi 1335178301 1216 ERDRAEAEAREKE 1228
Cdd:PTZ00121 1873 EKDLKEDDEEEIE 1885
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1315-1715 |
1.32e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1315 MQAMKAQFERDLQTRDEQ----NEEKKRLLIKQVRELEAELEDERKQralaVASKKKMEIDLKDLESQIEAANKARDEVI 1390
Cdd:COG4717 40 LAFIRAMLLERLEKEADElfkpQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1391 KQLRKLQaQMKDYQRELEEARASRDEIfaqsKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGK 1470
Cdd:COG4717 116 EELEKLE-KLLQLLPLYQELEALEAEL----AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1471 SA----LLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAE-----------LAAERSAAQKSDNARQQ 1535
Cdd:COG4717 191 EEelqdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearllllIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1536 LERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYK 1615
Cdd:COG4717 271 LILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1616 EQMEKANARMKQLKRQLEEAEEEA--TRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR-GGPISFSSSRSGRRQL 1692
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAAllAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEElLGELEELLEALDEEEL 430
|
410 420
....*....|....*....|...
gi 1335178301 1693 HIEGASLELSDDDTESKTSDVNE 1715
Cdd:COG4717 431 EEELEELEEELEELEEELEELRE 453
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1283-1674 |
1.43e-05 |
|
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: 50.02 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1283 LEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQF------ERDLQTRDEQNEEKKRLLIKQVRELEAELEDERK 1356
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIkileqqIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1357 QralavasKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAqmkdyqrELEEARASRDEIFAQSKESEKKLKSLEAEIL 1436
Cdd:TIGR04523 118 Q-------KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEK-------ELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1437 QLQEELASSERARRHAEQerdeladeianSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTln 1516
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLEL-----------LLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN-- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1517 aelaaersAAQKSDNARQQLERQNKELKAKLQELEGAvkskfKATISALEAKIGQLEEQLEQEAKERAAAnklvrrTEKK 1596
Cdd:TIGR04523 251 --------TQTQLNQLKDEQNKIKKQLSEKQKELEQN-----NKKIKELEKQLNQLKSEISDLNNQKEQD------WNKE 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1335178301 1597 LKEIFMQVEDERRhadQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1674
Cdd:TIGR04523 312 LKSELKNQEKKLE---EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1018-1376 |
1.52e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.51 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1018 DRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLeSQLQDTQELLQEETRQklnlssRIRQLEEEKNSLQEQ 1097
Cdd:pfam07888 72 ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL-SEEKDALLAQRAAHEA------RIRELEEDIKTLTQR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1098 QEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDD 1177
Cdd:pfam07888 145 VLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1178 LmvdldHQRQIVSNLEKKQKKFDQllaEEKNISARYAE-----------ERDRAEAEAREKETKA------LSLARALEE 1240
Cdd:pfam07888 225 A-----HRKEAENEALLEELRSLQ---ERLNASERKVEglgeelssmaaQRDRTQAELHQARLQAaqltlqLADASLALR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1241 ALEAKEEFERQNKQLRADMEdlmssKDDVGKNVHELEKskraLEQQVEEMRTQLEELEDELQATEDAKL----RLEVNMQ 1316
Cdd:pfam07888 297 EGRARWAQERETLQQSAEAD-----KDRIEKLSAELQR----LEERLQEERMEREKLEVELGREKDCNRvqlsESRRELQ 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1335178301 1317 AMKAQFeRDLQTRDEQNEEKKRLLIKQVRELEAELEDE--RKQRALAVASKKKMEIDLKDLE 1376
Cdd:pfam07888 368 ELKASL-RVAQKEKEQLQAEKQELLEYIRQLEQRLETVadAKWSEAALTSTERPDSPLSDSE 428
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
851-1674 |
1.60e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 851 EEELQAKDEELLKV------KEKQTKVEGELEEM-ERKHQQARATAEAGGDDETL--HKNNALKVVRELQAQIAELQE-- 919
Cdd:PRK04863 327 EQDYQAASDHLNLVqtalrqQEKIERYQADLEELeERLEEQNEVVEEADEQQEENeaRAEAAEEEVDELKSQLADYQQal 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 920 DFESEKASRNKAEKQKRDLSEELEALKT----ELEDTLDTTAAQ-QELRFKANLEKNKQGLETDNK-------ELACevK 987
Cdd:PRK04863 407 DVQQTRAIQYQQAVQALERAKQLCGLPDltadNAEDWLEEFQAKeQEATEELLSLEQKLSVAQAAHsqfeqayQLVR--K 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 988 VLQQVKAESEH-KRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNElDNVSSLLEEAEKKGIKFSKDAASLEsQLQDT 1066
Cdd:PRK04863 485 IAGEVSRSEAWdVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQ-QRAERLLAEFCKRLGKNLDDEDELE-QLQEE 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1067 QELLQEEtrqklnLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQV---LALQSQLTDTKKKVDDDLGTIESLEEAKKKL 1143
Cdd:PRK04863 563 LEARLES------LSESVSEARERRMALRQQLEQLQARIQRLAARApawLAAQDALARLREQSGEEFEDSQDVTEYMQQL 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1144 LkdgealsQRLEEKALAYDKLEKTKNRLQQELDDLmvdldHQRQiVSNLEKKQKKFDQL-------------LAEEKNIS 1210
Cdd:PRK04863 637 L-------ERERELTVERDELAARKQALDEEIERL-----SQPG-GSEDPRLNALAERFggvllseiyddvsLEDAPYFS 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1211 ARYAEER------DraeaeareketkaLSLARaleealeakeefeRQNKQLRADMEDLM------SSKDDVGKNVHELEK 1278
Cdd:PRK04863 704 ALYGPARhaivvpD-------------LSDAA-------------EQLAGLEDCPEDLYliegdpDSFDDSVFSVEELEK 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1279 S----------------------KRALEQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFERDLQTR-----D 1330
Cdd:PRK04863 758 AvvvkiadrqwrysrfpevplfgRAAREKRIEQLRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGSHlavafE 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1331 EQNEEKKRLLIKQVRELEAELED----ERKQRALAVASKKKM--------EIDLKDLESQIEAANKARDEvIKQLRKLQA 1398
Cdd:PRK04863 833 ADPEAELRQLNRRRVELERALADhesqEQQQRSQLEQAKEGLsalnrllpRLNLLADETLADRVEEIREQ-LDEAEEAKR 911
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1399 QMKDYQRELEEArasrDEIFAQSKESEKKLKSLEAEILQLQEELA---------SSERARRHA---EQERDELADEIANS 1466
Cdd:PRK04863 912 FVQQHGNALAQL----EPIVSVLQSDPEQFEQLKQDYQQAQQTQRdakqqafalTEVVQRRAHfsyEDAAEMLAKNSDLN 987
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1467 ASGKSALLD-EKRRLEARIAQLEEELEEEQSNMEL--LNDRFRKTTLQVDTLNAEL----------AAERSAAQK----- 1528
Cdd:PRK04863 988 EKLRQRLEQaEQERTRAREQLRQAQAQLAQYNQVLasLKSSYDAKRQMLQELKQELqdlgvpadsgAEERARARRdelha 1067
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1529 ----SDNARQQLERQNKELKAKLQELEGAVKskfkatisALEAKIGQLEEQLEQEAKERAAANKLVRR--TEKKLkeifM 1602
Cdd:PRK04863 1068 rlsaNRSRRNQLEKQLTFCEAEMDNLTKKLR--------KLERDYHEMREQVVNAKAGWCAVLRLVKDngVERRL----H 1135
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1603 QVEDERRHADQYKEQMEKANARMKQ------LKRQLEEAEEEATRAN-------ASRRKLQREL-------DDATEANEG 1662
Cdd:PRK04863 1136 RRELAYLSADELRSMSDKALGALRLavadneHLRDVLRLSEDPKRPErkvqfyiAVYQHLRERIrqdiirtDDPVEAIEQ 1215
|
970
....*....|..
gi 1335178301 1663 LSREVSTLKNRL 1674
Cdd:PRK04863 1216 MEIELSRLTEEL 1227
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1345-1459 |
1.68e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.47 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1345 RELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEifaqSKES 1424
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR----EIRK 463
|
90 100 110
....*....|....*....|....*....|....*
gi 1335178301 1425 EKKLKSLEAEILQLQEELASSERARRHAEQERDEL 1459
Cdd:COG2433 464 DREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1391-1676 |
1.82e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1391 KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAE---QERDELADEIANSA 1467
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1468 SGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttlqvdtlnaelAAERSAAQKSDNARQQLERQNKELKAKL 1547
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---------------VKELKELKEKAEEYIKLSEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1548 QELEgavkskfkATISALEAKIGQLEEQLeqeaKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANaRMKQ 1627
Cdd:PRK03918 310 REIE--------KRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-ELER 376
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1335178301 1628 LKRQLeeaeeeatrANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1676
Cdd:PRK03918 377 LKKRL---------TGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1253-1469 |
1.90e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1253 KQLRADMEDLMSSKDDVGKnvhELEKSKR---ALEQQVEEMRTQLEELEDELQATEDaklRLEVNMQAMKAQFeRDLQTR 1329
Cdd:COG3883 26 SELQAELEAAQAELDALQA---ELEELNEeynELQAELEALQAEIDKLQAEIAEAEA---EIEERREELGERA-RALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1330 DEQNEEKKRLL--------IKQVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMK 1401
Cdd:COG3883 99 GGSVSYLDVLLgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1335178301 1402 DYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASG 1469
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1253-1588 |
2.04e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.51 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1253 KQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMR---TQLEELEDELQATEDAKLRLEVNMQAMKAQ------FE 1323
Cdd:PRK01156 176 DMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSitlKEIERLSIEYNNAMDDYNNLKSALNELSSLedmknrYE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1324 RDLQTRDE--QNEEKKRLLIKQVRELEAELEDE----RKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQ 1397
Cdd:PRK01156 256 SEIKTAESdlSMELEKNNYYKELEERHMKIINDpvykNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1398 AQMKDY---QRELEEARASRDEIfaqsKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALL 1474
Cdd:PRK01156 336 KDYNDYikkKSRYDDLNNQILEL----EGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKEL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1475 DEKRR-----------LEARIAQLEEELEEEQSNMELLNDRFR-----------KTTLQVDTLNAELAAERSAAQKSDNA 1532
Cdd:PRK01156 412 NEINVklqdisskvssLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlgeeKSNHIINHYNEKKSRLEEKIREIEIE 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1335178301 1533 RQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1588
Cdd:PRK01156 492 VKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDK 547
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
802-1174 |
2.57e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 802 ARKAFAKKQQQLSALKVLQRNCAAYLKLrhwqwWRVFTKVKPLLQVTRQ-EEELQAKDEELLKVKEKQTKVEGELEEMER 880
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEK-----LEKLLQLLPLYQELEAlEAELAELPERLEELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 881 KHQQARATAEAGGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQ 960
Cdd:COG4717 168 LEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 961 ELRF----------------KANLEKNKQG---------------LETDNKELACEVKVLQQVKAESEHKRKKLDAQVQE 1009
Cdd:COG4717 248 ARLLlliaaallallglggsLLSLILTIAGvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1010 LHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQ--EETRQKLNLSSRIRQL 1087
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEEL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1088 EEEKNSLQEQQEEEEEA--RKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDG---------EALSQRLEE 1156
Cdd:COG4717 408 EEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelaellqelEELKAELRE 487
|
410 420
....*....|....*....|....*
gi 1335178301 1157 KA-------LAYDKLEKTKNRLQQE 1174
Cdd:COG4717 488 LAeewaalkLALELLEEAREEYREE 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1106-1334 |
2.65e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1106 KNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQ 1185
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1186 RQIVSNLEK--KQKKFDQLLaeeknisaryaeerDRAEAeareketkalsLARALEEALEAKEEFERQNKQLRADMEDLM 1263
Cdd:COG3883 99 GGSVSYLDVllGSESFSDFL--------------DRLSA-----------LSKIADADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1335178301 1264 SSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNE 1334
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
961-1630 |
2.72e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.98 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 961 ELRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAkvsegdrlrVELAEKANKLQNELDNVSS 1040
Cdd:pfam07111 54 ELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDA---------LAVAEKAGQAEAEGLRAAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1041 LLEEAEKKGIKFSKdaaslESQLQDTQELLQEETRQKL--------NLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQV 1112
Cdd:pfam07111 125 AGAEMVRKNLEEGS-----QRELEEIQRLHQEQLSSLTqaheealsSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1113 LALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDgEALSQRLEekaLAYDKLEKTKNRLQQELDDLmvdldhqRQIVSNL 1192
Cdd:pfam07111 200 ELLRKQLSKTQEELEAQVTLVESLRKYVGEQVPP-EVHSQTWE---LERQELLDTMQHLQEDRADL-------QATVELL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1193 EKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAkeeferqnkQLRADMEDLMSSKDDVGKN 1272
Cdd:pfam07111 269 QVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMV---------QLKAQDLEHRDSVKQLRGQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1273 VHELEK--SKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNmQAMKAQfeRDLQTRDEQNEEKKRLLIKQVRELEAE 1350
Cdd:pfam07111 340 VAELQEqvTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELS-RAQEAR--RRQQQQTASAEEQLKFVVNAMSSTQIW 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1351 LEDERKQRALAVASKKKMEIDLKDLESQIEAANK--ARDEVIKQLRKLQAQM--------KDYQRELEEARASRDEifaq 1420
Cdd:pfam07111 417 LETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGlmARKVALAQLRQESCPPpppappvdADLSLELEQLREERNR---- 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1421 skesekklksLEAEiLQLQEELASSE--RARRHAEQERDELaDEIAnsasgksalldekRRLEARIAQLEEELEEEQSNM 1498
Cdd:pfam07111 493 ----------LDAE-LQLSAHLIQQEvgRAREQGEAERQQL-SEVA-------------QQLEQELQRAQESLASVGQQL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1499 EllndrfrkttlqvdtlnAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKigqLEEQLEQ 1578
Cdd:pfam07111 548 E-----------------VARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRR---LNEARRE 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1335178301 1579 EAKERAAANKLVRRT--EKKLKEIFMQVEDERRhadqyKEQMEKANARMKQLKR 1630
Cdd:pfam07111 608 QAKAVVSLRQIQHRAtqEKERNQELRRLQDEAR-----KEEGQRLARRVQELER 656
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1378-1658 |
3.22e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1378 QIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASR----DEIFAQSKESEKKLKSLEAEILQLQEElassERARRHAE 1453
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQE----ERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1454 QERDELADEIANSASGKSALLDEKRRLEaRIAQLEEELEEEQSNMEllnDRFRKTTLQVDTLNaELAAERSAAQKSDNAR 1533
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNE-RVRQELEAARKVKILEE---ERQRKIQQQKVEME-QIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1534 QQLERQNKELKAKLQELEgavKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRT-EKKLKEIFMQ-VEDERRHA 1611
Cdd:pfam17380 440 LEEERAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmIEEERKRK 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1335178301 1612 DQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1658
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
908-1676 |
3.67e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 908 RELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALK---TELEDTLDTTAA-----QQELRFKANLEKNKQGLEtdn 979
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSareSDLEQDYQAASDhlnlvQTALRQQEKIERYQEDLE--- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 980 kELACEVKVLQQVKAESEHKRKKLDAQvqeLHAKVSEGDRLRVELAEKANKL-------------QNELDNVSSLLEEAE 1046
Cdd:COG3096 358 -ELTERLEEQEEVVEEAAEQLAEAEAR---LEAAEEEVDSLKSQLADYQQALdvqqtraiqyqqaVQALEKARALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1047 KKGIKFSKDAASLESQLQD-TQELLqeETRQKLNLSSRIRQLEEEKNSLQEQ-------QEEEEEAR---------KNLE 1109
Cdd:COG3096 434 LTPENAEDYLAAFRAKEQQaTEEVL--ELEQKLSVADAARRQFEKAYELVCKiageverSQAWQTARellrryrsqQALA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1110 KQVLALQSQLTDTKKKVdddlgtiESLEEAKKKLlkdgEALSQRLEEKALAYDKLEKTKNRLQQELDDLmvdLDHQRQIV 1189
Cdd:COG3096 512 QRLQQLRAQLAELEQRL-------RQQQNAERLL----EEFCQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1190 SNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALeealeakeeferqnkQLRADMEDLMSSKDDV 1269
Cdd:COG3096 578 EQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQ---------------EVTAAMQQLLEREREA 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1270 GKNVHELEKSKRALEQQVEEMR-------TQLEELEDELQAT-----------EDAKLRLEVNMQAMKAQFERDLQTrde 1331
Cdd:COG3096 643 TVERDELAARKQALESQIERLSqpggaedPRLLALAERLGGVllseiyddvtlEDAPYFSALYGPARHAIVVPDLSA--- 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1332 qneekkrlLIKQVRELEAELED----ERKQRALAVASKKKMEIDLKDL------------------------ESQIEAAN 1383
Cdd:COG3096 720 --------VKEQLAGLEDCPEDlyliEGDPDSFDDSVFDAEELEDAVVvklsdrqwrysrfpevplfgraarEKRLEELR 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1384 KARDEVIKQLRKLQAQMKDYQR---ELEEARASRDEI-FAQSKESEkkLKSLEAEILQLQEELASSERARRHAEQERDEL 1459
Cdd:COG3096 792 AERDELAEQYAKASFDVQKLQRlhqAFSQFVGGHLAVaFAPDPEAE--LAALRQRRSELERELAQHRAQEQQLRQQLDQL 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1460 ADEIA--NSASGKSALLDEkrrleariaqleeeleeeqsnmELLNDRfrkttlqVDTLNAELAAERSAA---QKSDNARQ 1534
Cdd:COG3096 870 KEQLQllNKLLPQANLLAD----------------------ETLADR-------LEELREELDAAQEAQafiQQHGKALA 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1535 QLER----------QNKELKAKLQELEgAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANklvRRTEKKLKEIFMQV 1604
Cdd:COG3096 921 QLEPlvavlqsdpeQFEQLQADYLQAK-EQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGEN---SDLNEKLRARLEQA 996
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1605 EDERRHAD----QYKEQMEKANARMKQLKrqleeaeeeaTRANASR---RKLQRELDD-----ATEANEGLSREVSTLKN 1672
Cdd:COG3096 997 EEARREAReqlrQAQAQYSQYNQVLASLK----------SSRDAKQqtlQELEQELEElgvqaDAEAEERARIRRDELHE 1066
|
....
gi 1335178301 1673 RLRR 1676
Cdd:COG3096 1067 ELSQ 1070
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1004-1231 |
3.75e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1004 DAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQklnLSSR 1083
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE---LGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1084 IRQLEEEKNSLqeqqeeeeearkNLEKQVLALQS------QLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEk 1157
Cdd:COG3883 92 ARALYRSGGSV------------SYLDVLLGSESfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1335178301 1158 alaydkLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKA 1231
Cdd:COG3883 159 ------LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1279-1434 |
3.83e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.83 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1279 SKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERD-LQTRDEQNEEKKRLLIKQVRELEAE------- 1350
Cdd:pfam09787 41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEaESSREQLQELEEQLATERSARREAEaelerlq 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1351 ------LEDERKQRALAVASKKKMEIDLKDLESQIEA---ANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQS 1421
Cdd:pfam09787 121 eelrylEEELRRSKATLQSRIKDREAEIEKLRNQLTSksqSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQL 200
|
170
....*....|...
gi 1335178301 1422 KESEKKLKSLEAE 1434
Cdd:pfam09787 201 ERMEQQIKELQGE 213
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1371-1602 |
3.95e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 48.53 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1371 DLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIfaqskeSEKKLKSLE-AEILQLQEELASSERAR 1449
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEEL------EAAALQPGEeEELEEERRRLSNAEKLR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1450 RHAEQERDELADEIANSASgksaLLDE-KRRLEaRIAQleeeleeEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQk 1528
Cdd:COG0497 226 EALQEALEALSGGEGGALD----LLGQaLRALE-RLAE-------YDPSLAELAERLESALIELEEAASELRRYLDSLE- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1529 SDNAR-QQLE-RQN--------------------KELKAKLQELEGAvkskfKATISALEAKIGQLEEQLEQEAKE---- 1582
Cdd:COG0497 293 FDPERlEEVEeRLAllrrlarkygvtveellayaEELRAELAELENS-----DERLEELEAELAEAEAELLEAAEKlsaa 367
|
250 260
....*....|....*....|.
gi 1335178301 1583 -RAAANKLVRRTEKKLKEIFM 1602
Cdd:COG0497 368 rKKAAKKLEKAVTAELADLGM 388
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
866-1674 |
4.10e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.89 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 866 EKQTKVEGELEEMERKHQQARATAEAGGDDETLHKNNALKVVRELQAQIAE-----LQEDFESEKASRNKAEKQKRDLSE 940
Cdd:TIGR01612 961 EKSYKDKFDNTLIDKINELDKAFKDASLNDYEAKNNELIKYFNDLKANLGKnkenmLYHQFDEKEKATNDIEQKIEDANK 1040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 941 ELEALKTELEDTLDTTAAQQELRFKANLEK-NKQGLETDNKELACEVKVLQQVK------------AESEHKRKKLDAQV 1007
Cdd:TIGR01612 1041 NIPNIEIAIHTSIYNIIDEIEKEIGKNIELlNKEILEEAEINITNFNEIKEKLKhynfddfgkeenIKYADEINKIKDDI 1120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1008 QELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIkFSKDAASLESQLQ------DTQELLQEETRQKLNls 1081
Cdd:TIGR01612 1121 KNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAI-SNDDPEEIEKKIEnivtkiDKKKNIYDEIKKLLN-- 1197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1082 sRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLalqSQLTDTKKKVDDDLGT----IESLEEAKKKllkdgealSQRLEEK 1157
Cdd:TIGR01612 1198 -EIAEIEKDKTSLEEVKGINLSYGKNLGKLFL---EKIDEEKKKSEHMIKAmeayIEDLDEIKEK--------SPEIENE 1265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1158 ALAYDKLEKTKNRLQQELDD----LMVDLDHQRQIvSNLEKKQKKFDQLLAEEKNIS------ARYAEERDRAEAEAREK 1227
Cdd:TIGR01612 1266 MGIEMDIKAEMETFNISHDDdkdhHIISKKHDENI-SDIREKSLKIIEDFSEESDINdikkelQKNLLDAQKHNSDINLY 1344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1228 ETKALSLARALEEALEakeeferqnKQLRADMEDLMSSKDDVGKNVH-ELEKSKRALEQQVEEmrTQLEELEDELQATED 1306
Cdd:TIGR01612 1345 LNEIANIYNILKLNKI---------KKIIDEVKEYTKEIEENNKNIKdELDKSEKLIKKIKDD--INLEECKSKIESTLD 1413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1307 AKLRLEV--NMQAMKAQF---ERDLQT---RDEQNEEKKRLLIKQVreleaELEDERKQRALAVA---SKKKMEIDLKDL 1375
Cdd:TIGR01612 1414 DKDIDECikKIKELKNHIlseESNIDTyfkNADENNENVLLLFKNI-----EMADNKSQHILKIKkdnATNDHDFNINEL 1488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1376 ESQIEAANKARDEV---IKQLRKLQAQMKDYQRE---------------------------LEEARASRDEIFAQSKESE 1425
Cdd:TIGR01612 1489 KEHIDKSKGCKDEAdknAKAIEKNKELFEQYKKDvtellnkysalaiknkfaktkkdseiiIKEIKDAHKKFILEAEKSE 1568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1426 KKLKSLEAEILQLQEELASSERARRHAEQERDELAD------EIANSASGKSALLDEKRRLEARIA------------QL 1487
Cdd:TIGR01612 1569 QKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENfenkflKISDIKKKINDCLKETESIEKKISsfsidsqdtelkEN 1648
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1488 EEELEEEQSNMELLNDRFRkttlQVDTLNAELAAERSAAQKSDNARQQlERQNKELK--AKLQELEGAVKSKFKATISAL 1565
Cdd:TIGR01612 1649 GDNLNSLQEFLESLKDQKK----NIEDKKKELDELDSEIEKIEIDVDQ-HKKNYEIGiiEKIKEIAIANKEEIESIKELI 1723
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1566 EAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANAS 1645
Cdd:TIGR01612 1724 EPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITYDEIKNTRINAQNEFLKIIEI 1803
|
890 900
....*....|....*....|....*....
gi 1335178301 1646 RRKLQRELDDaTEANEgLSREVSTLKNRL 1674
Cdd:TIGR01612 1804 EKKSKSYLDD-IEAKE-FDRIINHFKKKL 1830
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
921-1621 |
4.99e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 48.26 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 921 FESEKASRNKAEK--------------QKRDLSEELEALkTELEDTLdtTAAQQelrfkaNLEKNKQGLeTDNKELACEV 986
Cdd:PRK10246 190 FEQHKSARTELEKlqaqasgvalltpeQVQSLTASLQVL-TDEEKQL--LTAQQ------QQQQSLNWL-TRLDELQQEA 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 987 KVLQQVKAESEHKRKKLDAQVQEL-HAKVSEGDR---LRV-ELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLES 1061
Cdd:PRK10246 260 SRRQQALQQALAAEEKAQPQLAALsLAQPARQLRphwERIqEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1062 QLQDTQELLQeetrQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKnlekQVLALQSQLTDTKKKVDD--DLGTIESLEEA 1139
Cdd:PRK10246 340 ELQAQQQSLN----TWLAEHDRFRQWNNELAGWRAQFSQQTSDRE----QLRQWQQQLTHAEQKLNAlpAITLTLTADEV 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1140 KKKL--LKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEER 1217
Cdd:PRK10246 412 AAALaqHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQEARIK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1218 DRAEAEAREKETKALSL-ARALEEALEAKEEFERQNKQLRADmedlmsskddvgknvhELEKSKRALEQQVEEMRTQLEE 1296
Cdd:PRK10246 492 DLEAQRAQLQAGQPCPLcGSTSHPAVEAYQALEPGVNQSRLD----------------ALEKEVKKLGEEGAALRGQLDA 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1297 LEDELQATEDAKLRLEVNMQAMKAQFER---DLQTRDEQNEEKKRLLIKQvreleaeledERKQRALAVASKKKMeidlk 1373
Cdd:PRK10246 556 LTKQLQRDESEAQSLRQEEQALTQQWQAvcaSLNITLQPQDDIQPWLDAQ----------EEHERQLRLLSQRHE----- 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1374 dLESQIEAANkardeviKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQeelassERARRHAE 1453
Cdd:PRK10246 621 -LQGQIAAHN-------QQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQ------QRQNELTA 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1454 -QER--------DELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDT-LNAELAAER 1523
Cdd:PRK10246 687 lQNRiqqltpllETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTaLQASVFDDQ 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1524 SA---AQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQL--EQEAKERAAANKLVRRTEKKLK 1598
Cdd:PRK10246 767 QAflaALLDEETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVtvEQIQQELAQLAQQLRENTTRQG 846
|
730 740
....*....|....*....|....*.
gi 1335178301 1599 EIFMQV---EDERRHADQYKEQMEKA 1621
Cdd:PRK10246 847 EIRQQLkqdADNRQQQQALMQQIAQA 872
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
842-1236 |
5.00e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 842 KPLLQVTRQEEELQAKD--EELLKVKEKQTKVEGELEEMERK----HQQARATAEAGGDDETLHKNNALKV---VRELQA 912
Cdd:pfam07888 1 KPLDELVTLEEESHGEEggTDMLLVVPRAELLQNRLEECLQEraelLQAQEAANRQREKEKERYKRDREQWerqRRELES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 913 QIAELQEDFESEKASRNKAEKQKRDLSEELEALKTElEDTLDTTAAQQELRFK------ANLEKNKQGLETDNKELACEV 986
Cdd:pfam07888 81 RVAELKEELRQSREKHEELEEKYKELSASSEELSEE-KDALLAQRAAHEARIReleediKTLTQRVLERETELERMKERA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 987 KVLQQVKAESEHKRK----KLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLEsQ 1062
Cdd:pfam07888 160 KKAGAQRKEEEAERKqlqaKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE-E 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1063 LQDTQELLQEETRqklnlssRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGT--------IE 1134
Cdd:pfam07888 239 LRSLQERLNASER-------KVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARwaqeretlQQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1135 SLEEAKKKLLKDGEALsQRLEEkALAYDKLEKTKNR--LQQELDDLMVDLDHQR----QIVSNLEKKQKKFDQLLAEEKN 1208
Cdd:pfam07888 312 SAEADKDRIEKLSAEL-QRLEE-RLQEERMEREKLEveLGREKDCNRVQLSESRrelqELKASLRVAQKEKEQLQAEKQE 389
|
410 420 430
....*....|....*....|....*....|
gi 1335178301 1209 I--SARYAEERDRAEAEAREKETKALSLAR 1236
Cdd:pfam07888 390 LleYIRQLEQRLETVADAKWSEAALTSTER 419
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1161-1603 |
5.46e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.98 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1161 YDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLaeEKNISARYAEERDRAEAEAREKETKALsLARALEE 1240
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKAL-MDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1241 ALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1320
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1321 QFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQM 1400
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1401 KDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRL 1480
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1481 EARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKA 1560
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1335178301 1561 TISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQ 1603
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAA 520
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
850-1483 |
6.83e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 850 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAggddetlhknnalkvVRELQAQIAELQEDFESEKASRN 929
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDE---------------LEQLQEELEARLESLSESVSEAR 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 930 KAEKQKRDLSEELEALKTELED------TLDTTAAQQELRFKANLEkNKQGLETDNKELACEVKVLQQVKAESEHKRKKL 1003
Cdd:PRK04863 579 ERRMALRQQLEQLQARIQRLAArapawlAAQDALARLREQSGEEFE-DSQDVTEYMQQLLERERELTVERDELAARKQAL 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1004 DAQVQELHAK-VSEGDRLRVeLAEKANK-----------------------------LQNELDNVSSLLEEAEK------ 1047
Cdd:PRK04863 658 DEEIERLSQPgGSEDPRLNA-LAERFGGvllseiyddvsledapyfsalygparhaiVVPDLSDAAEQLAGLEDcpedly 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1048 --KGIKFSKDAASLESQLQDTQELLQEETRQklnlsSRIRQLEEEKnslqeqqeeeEEARKNLEKQVLALQSQLTDTKKK 1125
Cdd:PRK04863 737 liEGDPDSFDDSVFSVEELEKAVVVKIADRQ-----WRYSRFPEVP----------LFGRAAREKRIEQLRAEREELAER 801
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1126 VDddlgtieSLEEAKKKLLKDGEALSQRL-EEKALAYD-----KLEKTKNRLQQ---ELDDLMVDLDHQRQIVSNLEKKQ 1196
Cdd:PRK04863 802 YA-------TLSFDVQKLQRLHQAFSRFIgSHLAVAFEadpeaELRQLNRRRVElerALADHESQEQQQRSQLEQAKEGL 874
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1197 KKFDQLLAEekniSARYAEER--DRAEaEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVH 1274
Cdd:PRK04863 875 SALNRLLPR----LNLLADETlaDRVE-EIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQ 949
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1275 ELEKSK---RALEqQVEEMRTQLeeledelqATEDAklrleVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAEL 1351
Cdd:PRK04863 950 TQRDAKqqaFALT-EVVQRRAHF--------SYEDA-----AEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQL 1015
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1352 eDERKQRalavaskkkmeidLKDLESQIEAANKARDEVIKQLRKLQAQmkdYQRELEE-ARASRDEIFAQSKESEKKLKS 1430
Cdd:PRK04863 1016 -AQYNQV-------------LASLKSSYDAKRQMLQELKQELQDLGVP---ADSGAEErARARRDELHARLSANRSRRNQ 1078
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1335178301 1431 LEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALL------DEKRRLEAR 1483
Cdd:PRK04863 1079 LEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLrlvkdnGVERRLHRR 1137
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
846-1082 |
7.64e-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: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 846 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAggddetlhKNNALKvvrELQAQIAELQEDFESEK 925
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA--------LQAEID---KLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 926 A---SRNKAEKQKRDLSEELEALK--TELEDTLDTTAAQQELrfkanleknkqgLETDNKELacevKVLQQVKAESEHKR 1000
Cdd:COG3883 86 EelgERARALYRSGGSVSYLDVLLgsESFSDFLDRLSALSKI------------ADADADLL----EELKADKAELEAKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1001 KKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNL 1080
Cdd:COG3883 150 AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
..
gi 1335178301 1081 SS 1082
Cdd:COG3883 230 AA 231
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1517-1630 |
7.65e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1517 AELAAERSAAQKSDNARQ--QLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTE 1594
Cdd:COG2433 397 AEREKEHEERELTEEEEEirRLEEQVERLEAEVEELEAELEEK-DERIERLERELSEARSEERREIRKDREISRLDREIE 475
|
90 100 110
....*....|....*....|....*....|....*.
gi 1335178301 1595 KKLKEIfmqvEDERRHADQYKEQMEkanaRMKQLKR 1630
Cdd:COG2433 476 RLEREL----EEERERIEELKRKLE----RLKELWK 503
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1127-1667 |
8.66e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1127 DDDLGTIESLEEAKKKLLKDGEALSQ--------------RLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNL 1192
Cdd:pfam05483 67 DSDFENSEGLSRLYSKLYKEAEKIKKwkvsieaelkqkenKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1193 EKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEdlMSSKDDVGKN 1272
Cdd:pfam05483 147 IKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMH--FKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1273 VHELEKSKRAL---EQQVEEMRTQLEELEDELQateDAKLRLEVNMQAMKaQFERDLQTRDEQNEEkkrlLIKQVRELEA 1349
Cdd:pfam05483 225 QHLEEEYKKEIndkEKQVSLLLIQITEKENKMK---DLTFLLEESRDKAN-QLEEKTKLQDENLKE----LIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1350 ELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKE----SE 1425
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrlekNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1426 KKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANsasgKSALLDEKRRLEaRIAQLEEELEeeQSNMELLNDRF 1505
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE----DEKLLDEKKQFE-KIAEELKGKE--QELIFLLQARE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1506 RkttlQVDTLNAELAAERSAaqksdnaRQQLERQNKELKAKLQelegavKSKFKAT-ISALEAKIGQLEEQLEQEA---- 1580
Cdd:pfam05483 450 K----EIHDLEIQLTAIKTS-------EEHYLKEVEDLKTELE------KEKLKNIeLTAHCDKLLLENKELTQEAsdmt 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1581 ----KERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDA 1656
Cdd:pfam05483 513 lelkKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
570
....*....|.
gi 1335178301 1657 TEANEGLSREV 1667
Cdd:pfam05483 593 ENKCNNLKKQI 603
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1329-1599 |
8.99e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1329 RDEQNEEKKRLLIKQVRELEAELEDERKQRA-LAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQREL 1407
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLrKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1408 EEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQL 1487
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1488 EEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEA 1567
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270
....*....|....*....|....*....|..
gi 1335178301 1568 KIGQLEEQLEQEAKERAAANKLVRRTEKKLKE 1599
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1275-1486 |
9.92e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.76 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1275 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqferdlqtRDEQNEEKKRLLIKQVRELEAELEDE 1354
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK--------------------QAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1355 RKQRALAVASKKKMEidlkdlesqiEAANKARDEVIKqlrKLQAQMKdyqRELEEARASRDEIFAQSKESEKKLKSLEAE 1434
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1335178301 1435 ILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1486
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAE 247
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
994-1171 |
1.07e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 994 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKgikfskdAASLESQLQD--TQELLQ 1071
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-------IKKYEEQLGNvrNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1072 EETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDlgtIESLEEAKKKLLKDGEALS 1151
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEAEREELA 169
|
170 180
....*....|....*....|.
gi 1335178301 1152 QRLEEKALA-YDKLEKTKNRL 1171
Cdd:COG1579 170 AKIPPELLAlYERIRKRKNGL 190
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1333-1669 |
1.12e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.25 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1333 NEEKKRLLIKQVRELEAELEDERKQRALA----VASKKKMEiDLKDLESQIEAA-NKARDEVIKQLRKLQAQMK--DYQR 1405
Cdd:COG3096 276 HANERRELSERALELRRELFGARRQLAEEqyrlVEMARELE-ELSARESDLEQDyQAASDHLNLVQTALRQQEKieRYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1406 ELEEArasrdeifaqskesEKKLKSLEAEILQLQEELASSERARRHAEQERDELadeiansasgKSALLDEKRRLEAria 1485
Cdd:COG3096 355 DLEEL--------------TERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSL----------KSQLADYQQALDV--- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1486 QLEEELEEEQSNMELLNDRfrkTTLQVDTLNAELAAERSAAQKSDnaRQQLERQNKELKAKLQeLEGAVKSKFKATISAL 1565
Cdd:COG3096 408 QQTRAIQYQQAVQALEKAR---ALCGLPDLTPENAEDYLAAFRAK--EQQATEEVLELEQKLS-VADAARRQFEKAYELV 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1566 EAKIGQLE-EQLEQEAKEraaanklVRRTEKKLKEIFMQVEDERRhadQYKEqMEKANARMKQLKRQLEEAEEEATRANA 1644
Cdd:COG3096 482 CKIAGEVErSQAWQTARE-------LLRRYRSQQALAQRLQQLRA---QLAE-LEQRLRQQQNAERLLEEFCQRIGQQLD 550
|
330 340
....*....|....*....|....*
gi 1335178301 1645 SRRKLQRELDDATEANEGLSREVST 1669
Cdd:COG3096 551 AAEELEELLAELEAQLEELEEQAAE 575
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
989-1116 |
1.17e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 989 LQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAAslESQLQDTQE 1068
Cdd:PRK00409 518 LNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEA--DEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1335178301 1069 LLQEETRqklnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQ 1116
Cdd:PRK00409 596 LQKGGYA-----SVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1386-1551 |
1.28e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.11 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1386 RDEVIKQLRKLQAQMKDyQRELEEARASrdeifaqskesekklkSLEAEILQLQEELASSERARRHAEQERDELADEiAN 1465
Cdd:PRK09039 51 KDSALDRLNSQIAELAD-LLSLERQGNQ----------------DLQDSVANLRASLSAAEAERSRLQALLAELAGA-GA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1466 SASGKSALLDEKRRLEARIAQLEeeleeeQSNMELLNDrfrkttlQVDTLNAELAAERSAAQKSDNARQQLERQ------ 1539
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARA------LAQVELLNQ-------QIAALRRQLAALEAALDASEKRDRESQAKiadlgr 179
|
170
....*....|....
gi 1335178301 1540 --NKELKAKLQELE 1551
Cdd:PRK09039 180 rlNVALAQRVQELN 193
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1275-1443 |
1.35e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.20 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1275 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQ-----NEEKKRLLIKQVRELEA 1349
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAE-KWEEKARLalekgREDLAREALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1350 ELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQ---------------------MKDYQRELE 1408
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQekvnealsgidsddatsalerMEEKIEEME 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1335178301 1409 EARASRDEIfAQSKESEKKLKSLEAEIlQLQEELA 1443
Cdd:COG1842 179 ARAEAAAEL-AAGDSLDDELAELEADS-EVEDELA 211
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
838-1171 |
1.38e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.75 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 838 FTKVKPLLQVTRQ-----EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAGGDD--ETLhknnalkvvREL 910
Cdd:PRK04778 100 FRKAKHEINEIESlldliEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSfgPAL---------DEL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 911 QAQIAELQEDFE-----SEKASRNKAEKQKRDLSEELEALKTELED------TLDTTaaqqelrFKANLEKNKQGLetdn 979
Cdd:PRK04778 171 EKQLENLEEEFSqfvelTESGDYVEAREILDQLEEELAALEQIMEEipellkELQTE-------LPDQLQELKAGY---- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 980 KELACEVKVLQQVKAESEHKRkkLDAQVQELHAKVSEgdrLRVELAEKANK-LQNELDNVSSLLE---EAEKKGIKFSKD 1055
Cdd:PRK04778 240 RELVEEGYHLDHLDIEKEIQD--LKEQIDENLALLEE---LDLDEAEEKNEeIQERIDQLYDILErevKARKYVEKNSDT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1056 AASLESQLQDTQELLQEETrQKLNLSSRIRQLEEEKnslqeqqeeeeeaRKNLEKQVLALQSQLTDTKKKVDDD------ 1129
Cdd:PRK04778 315 LPDFLEHAKEQNKELKEEI-DRVKQSYTLNESELES-------------VRQLEKQLESLEKQYDEITERIAEQeiayse 380
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1335178301 1130 -----LGTIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRL 1171
Cdd:PRK04778 381 lqeelEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
915-1173 |
1.48e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 915 AELQEDFESEKASRN---KAEKQKrDLSEELEALKTELEDTLDttaaqqelrFKANLEKNKQGLETDNKELACEVKVLQQ 991
Cdd:PRK11281 29 AASNGDLPTEADVQAqldALNKQK-LLEAEDKLVQQDLEQTLA---------LLDKIDRQKEETEQLKQQLAQAPAKLRQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 992 VKAESEHKRKKLDAQVQELHAKVSEgDRLRVELAEKANKL---QNELDNVSSLL-------EEAEKKGIKFSKDAASLES 1061
Cdd:PRK11281 99 AQAELEALKDDNDEETRETLSTLSL-RQLESRLAQTLDQLqnaQNDLAEYNSQLvslqtqpERAQAALYANSQRLQQIRN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1062 QL---QDTQELLQEETRQK-------LNLSSRIRQLEEEKNS----LQEQQEEEEEARKN-LEKQVLALQS-----QLTD 1121
Cdd:PRK11281 178 LLkggKVGGKALRPSQRVLlqaeqalLNAQNDLQRKSLEGNTqlqdLLQKQRDYLTARIQrLEHQLQLLQEainskRLTL 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1335178301 1122 TKKKVDDdlgtIESLEEAKK----KLLKDGEA----LSQRLEEK-----ALAYDKLeKTKN---RLQQ 1173
Cdd:PRK11281 258 SEKTVQE----AQSQDEAARiqanPLVAQELEinlqLSQRLLKAteklnTLTQQNL-RVKNwldRLTQ 320
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1343-1533 |
1.57e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1343 QVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1422
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1423 ESEKKLKSLEA--------------------------EILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDE 1476
Cdd:COG3883 97 RSGGSVSYLDVllgsesfsdfldrlsalskiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1335178301 1477 KRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNAR 1533
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1056-1235 |
1.80e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1056 AASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDD------- 1128
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelge 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1129 ----------DLGTIESLEEAK--KKLLKDGEALSQ-------RLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRQIV 1189
Cdd:COG3883 91 raralyrsggSVSYLDVLLGSEsfSDFLDRLSALSKiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1335178301 1190 SNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLA 1235
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1406-1623 |
1.92e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1406 ELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASserarrhAEQERDELADEIANsasgksalldekrrLEARIA 1485
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE-------LQAELEALQAEIDK--------------LQAEIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1486 QLEEELEEEQsnmELLNDRFR---KTTLQVDTLNAELAAE--RSAAQKSDNARQQLERQNK---ELKAKLQELEGAvKSK 1557
Cdd:COG3883 76 EAEAEIEERR---EELGERARalyRSGGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADlleELKADKAELEAK-KAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1335178301 1558 FKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANA 1623
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1280-1434 |
1.92e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1280 KRALEQQVEEMRTQ----LEELEDELQATEDAKLrLEVNMQAM--KAQFERDLQTRDEQNEEKKRLLIKQVRELEAELED 1353
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKEEIHklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1354 ERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRE--LEEARA-SRDEIFAQSKESEKKLKs 1430
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEEeARHEAAVLIKEIEEEAK- 183
|
....
gi 1335178301 1431 LEAE 1434
Cdd:PRK12704 184 EEAD 187
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
931-1161 |
2.05e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 931 AEKQKRDLSEELEALKTELEDTLDTTAAQQElrfkaNLEKNKQGLETDNKELAcevkvlqqvkaESEHKRKKLDAQVQEL 1010
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQA-----ELEELNEEYNELQAELE-----------ALQAEIDKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1011 HAKVsegDRLRVELAEKANKLQNELDNVSSLLEEAEKKGI-KFSKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEE 1089
Cdd:COG3883 78 EAEI---EERREELGERARALYRSGGSVSYLDVLLGSESFsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1335178301 1090 EKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEEKALAY 1161
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
846-1355 |
2.19e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 846 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAGGDDETLhknnalkvvRELQAQIAELQEDFESEK 925
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL---------EALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 926 AsrnkAEKQKRDLSEELEALKTELEDtldttaAQQELRFKanLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDA 1005
Cdd:COG4717 153 E----RLEELRELEEELEELEAELAE------LQEELEEL--LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1006 QVQELHAKVSEGDRLRVELAEKANKLQNELDN-----VSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNL 1080
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1081 SSRIRQLEEeknslqeQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLlkdgEALSQRLEEKALA 1160
Cdd:COG4717 301 GKEAEELQA-------LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA----EELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1161 yDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKalslaralee 1240
Cdd:COG4717 370 -QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELE---------- 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1241 aleakeefeRQNKQLRADMEDLMSSKDDVGKNVHELEKSKRaleqqVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKa 1320
Cdd:COG4717 439 ---------EELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAELRELAEEWAALKLALELLE- 503
|
490 500 510
....*....|....*....|....*....|....*
gi 1335178301 1321 qferdlQTRDEQNEEKKRLLIKQVRELEAELEDER 1355
Cdd:COG4717 504 ------EAREEYREERLPPVLERASEYFSRLTDGR 532
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1190-1410 |
2.36e-04 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 45.90 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1190 SNLEKKQKKFDQLLaEEKNISARYAEERdRAEAEAREKETKALslaraleealeakeeferqNKQLRADMEDLMSSKDDV 1269
Cdd:COG1193 507 ELLGEESIDVEKLI-EELERERRELEEE-REEAERLREELEKL-------------------REELEEKLEELEEEKEEI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1270 GKNVH-ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEvnmQAMKAQFERDLQTRDEQNEEKKRLLIK-----Q 1343
Cdd:COG1193 566 LEKAReEAEEILREARKEAEELIRELREAQAEEEELKEARKKLE---ELKQELEEKLEKPKKKAKPAKPPEELKvgdrvR 642
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1335178301 1344 VRELEAE---LEDERKQRALAVASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQREL-------EEA 1410
Cdd:COG1193 643 VLSLGQKgevLEIPKGGEAEVQVGILKMTVKLSDLEKVEKKKPKKPKKRPAGVSVSVSKASTVSPELdlrgmrvEEA 719
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1252-1384 |
2.52e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 45.82 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1252 NKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDE 1331
Cdd:pfam05911 683 NKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYE-DLETRLT 761
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1335178301 1332 QNEEKKRLLIKQVRELEAELEDERKqralavaSKKKMEIDLKDLESQIEAANK 1384
Cdd:pfam05911 762 ELEAELNELRQKFEALEVELEEEKN-------CHEELEAKCLELQEQLERNEK 807
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
905-1048 |
2.69e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 905 KVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKT---ELEDTLDTTAAQQELRfkaNLEKNKQGLETDNKE 981
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikKYEEQLGNVRNNKEYE---ALQKEIESLKRRISD 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1335178301 982 LAcevKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKK 1048
Cdd:COG1579 108 LE---DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
989-1197 |
2.85e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 989 LQQVKAESEHKRKKLDAQVQELHAKVSE-GDRLR--------VELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASL 1059
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEaEAALEefrqknglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1060 ESQLQDTQELLQE--ETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVdddlgtIESLE 1137
Cdd:COG3206 246 RAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI------LASLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1138 EAKKKLLKDGEALSQRLEEKALAYDKLektkNRLQQELDDLMVDLDHQRQIVSNLEKKQK 1197
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
850-1384 |
3.04e-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: 45.50 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 850 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAGGDDETLHKNNALKVVRELQAQIAELQEdfesekaSRN 929
Cdd:pfam05557 67 AEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEE-------LQE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 930 KAEKQKRDLSeELEALKTELEDTLDTTAAqQELRFKaNLEKNKQGLETDnkelACEVKVLQQvKAESEHKRKKLDAQVQE 1009
Cdd:pfam05557 140 RLDLLKAKAS-EAEQLRQNLEKQQSSLAE-AEQRIK-ELEFEIQSQEQD----SEIVKNSKS-ELARIPELEKELERLRE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1010 LHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKdaasLESQLQDTQELLQE---ETRQKLNLSSRIRQ 1086
Cdd:pfam05557 212 HNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEK----LEQELQSWVKLAQDtglNLRSPEDLSRRIEQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1087 LE-------EEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLLKDGEALSQRLEekal 1159
Cdd:pfam05557 288 LQqreivlkEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILE---- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1160 AYDKLEKTKNRLQQELDDLmvdldhqRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKalslarale 1239
Cdd:pfam05557 364 SYDKELTMSNYSPQLLERI-------EEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQAL--------- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1240 ealeakeefeRQNKQLrADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELedELQATEDAK----LRLEVNM 1315
Cdd:pfam05557 428 ----------RQQESL-ADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERR--CLQGDYDPKktkvLHLSMNP 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1316 QAM-KAQFERDLQTRDEQNEEKKRLlikqVRELEAELEDerkQRALAVASKKKMEIDLKDLESQIEAANK 1384
Cdd:pfam05557 495 AAEaYQQRKNQLEKLQAEIERLKRL----LKKLEDDLEQ---VLRLPETTSTMNFKEVLDLRKELESAEL 557
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
858-1048 |
3.21e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 858 DEELLKVKEKQTKVEGELEEMERKHQQARATAEAGGDDETLhknnalkvvRELQAQIAELQEDFESEKASRNKAEKQKRD 937
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQL---------SELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 938 L---------SEELEALKTELEDtLDTTAAQQELRFKAN------LEKNKQGLETDNKELACEVKVLQQVKAES-EHKRK 1001
Cdd:COG3206 252 GpdalpellqSPVIQQLRAQLAE-LEAELAELSARYTPNhpdviaLRAQIAALRAQLQQEAQRILASLEAELEAlQAREA 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1335178301 1002 KLDAQVQELHAKVSEGDRLRVELAEkankLQNELDNVSSLLEEAEKK 1048
Cdd:COG3206 331 SLQAQLAQLEARLAELPELEAELRR----LEREVEVARELYESLLQR 373
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1324-1630 |
3.28e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1324 RDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLK-------DLESQIEAANKARDEVIKQLRKL 1396
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQaaqaelaQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1397 QAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELA----DEIANSASGKSA 1472
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldelLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1473 LLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEG 1552
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1335178301 1553 AVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKR 1630
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1378-1652 |
3.56e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.45 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1378 QIEAANKArdevIKQLRKLQAQMKDYQR---ELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQ 1454
Cdd:COG5022 763 RYLQALKR----IKKIQVIQHGFRLRRLvdyELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEV 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1455 ERDELADEIANSASgkSALLDEKRrleARIAQLEEELEEEQSNMELLNDRFRkttlqvdtlnaELAAERSAAQKSDNARQ 1534
Cdd:COG5022 839 EFSLKAEVLIQKFG--RSLKAKKR---FSLLKKETIYLQSAQRVELAERQLQ-----------ELKIDVKSISSLKLVNL 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1535 QLERQNKELKAKLQELEGAvKSKFKATISALEAKI---GQLEEQLEQEAKERAAANKLvRRTEKKLKEIFMQVEDERRHA 1611
Cdd:COG5022 903 ELESEIIELKKSLSSDLIE-NLEFKTELIARLKKLlnnIDLEEGPSIEYVKLPELNKL-HEVESKLKETSEEYEDLLKKS 980
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1335178301 1612 DQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRE 1652
Cdd:COG5022 981 TILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKEL 1021
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1372-1630 |
3.59e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.07 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1372 LKDLESQIEAANKARDEVIKQLRKLQAQMKdyQRELEEARASRdeifaQSKESEKKLKSLEAEILQLQEELASSERarRH 1451
Cdd:PRK11637 49 LKSIQQDIAAKEKSVRQQQQQRASLLAQLK--KQEEAISQASR-----KLRETQNTLNQLNKQIDELNASIAKLEQ--QQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1452 AEQERDeLADEIaNSA------SGKSALL--DEKRRLEaRIaqleeeleeeQSNMELLNDRFRKTTLQVDTLNAELAAER 1523
Cdd:PRK11637 120 AAQERL-LAAQL-DAAfrqgehTGLQLILsgEESQRGE-RI----------LAYFGYLNQARQETIAELKQTREELAAQK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1524 SAAQKSDNARQQLERQNKELKAKLQELEGAVKSkfkaTISALEAKIGQLEEQLEQeakeraaanklVRRTEKKLKEIFMQ 1603
Cdd:PRK11637 187 AELEEKQSQQKTLLYEQQAQQQKLEQARNERKK----TLTGLESSLQKDQQQLSE-----------LRANESRLRDSIAR 251
|
250 260
....*....|....*....|....*...
gi 1335178301 1604 VEDE-RRHADQYKEQMEKANARMKQLKR 1630
Cdd:PRK11637 252 AEREaKARAEREAREAARVRDKQKQAKR 279
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1275-1483 |
3.75e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1275 ELEKSKRALEQQVEEMRTQLEELEdeLQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRL------LIKQVRELE 1348
Cdd:PRK04778 253 DIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLpdflehAKEQNKELK 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1349 AELEderkqralavASKKKMEIDLKDLESQieaankarDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1428
Cdd:PRK04778 331 EEID----------RVKQSYTLNESELESV--------RQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQL 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1335178301 1429 KSLEAEILQLQEELASSERARRHAEQERDELadeiansasgKSALLDEKRRLEAR 1483
Cdd:PRK04778 393 EEIEKEQEKLSEMLQGLRKDELEAREKLERY----------RNKLHEIKRYLEKS 437
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1389-1632 |
3.75e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 44.33 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1389 VIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEE----LASSERARRHAE---QERDELAD 1461
Cdd:pfam06008 10 ALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKatqtLAKAQQVNAESErtlGHAKELAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1462 EIANSASGKSALLDEKRRL-----EARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTlnaelaAERSAAQKSDNarqQL 1536
Cdd:pfam06008 90 AIKNLIDNIKEINEKVATLgendfALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAE------AELKAAQDLLS---RI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1537 ERQNKELKAKLQELEGAVKSKfkatISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKE 1616
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDS----LAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEE 236
|
250
....*....|....*.
gi 1335178301 1617 QMEKANARMKQLKRQL 1632
Cdd:pfam06008 237 TLKTARDSLDAANLLL 252
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1359-1575 |
4.13e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1359 ALAVASKKKMEIDLKDLESqieAANKARDEVIKQL---------RKLQAQ-MKDYQRELEE----ARASRDEIFAQSKE- 1423
Cdd:PRK10929 19 AATAPDEKQITQELEQAKA---AKTPAQAEIVEALqsalnwleeRKGSLErAKQYQQVIDNfpklSAELRQQLNNERDEp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1424 ----SEKKLKSLEAEILQLQEELAssERARRhAEQERDElADEIANSASGKSALLDEKRRL----EARI-AQLEEELEEE 1494
Cdd:PRK10929 96 rsvpPNMSTDALEQEILQVSSQLL--EKSRQ-AQQEQDR-AREISDSLSQLPQQQTEARRQlneiERRLqTLGTPNTPLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1495 QSNMELLNDRFRKTTLQVDTLnaELAaersaaQKSDNARQQLER--------QNKELKAKLQELEGAVKS-KFKATISAL 1565
Cdd:PRK10929 172 QAQLTALQAESAALKALVDEL--ELA------QLSANNRQELARlrselakkRSQQLDAYLQALRNQLNSqRQREAERAL 243
|
250
....*....|
gi 1335178301 1566 EaKIGQLEEQ 1575
Cdd:PRK10929 244 E-STELLAEQ 252
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1383-1629 |
4.59e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1383 NKARDEVIKQLRKLQA-QMKDYQRE-----LEEARASRDEI------FAQSKESEKKLKSLEAEIlqlqeELASSERARR 1450
Cdd:PRK05771 15 KSYKDEVLEALHELGVvHIEDLKEElsnerLRKLRSLLTKLsealdkLRSYLPKLNPLREEKKKV-----SVKSLEELIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1451 HAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEqSNMELLNDrFRKTTLQVDTLNAELAAERSAAQKSD 1530
Cdd:PRK05771 90 DVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNFD-LDLSLLLG-FKYVSVFVGTVPEDKLEELKLESDVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1531 NA-----------------RQQLERQNKELK-AKLQELEGAVKSKFKATISALEAKIGQLEEQLEqeakeraaanklvrR 1592
Cdd:PRK05771 168 NVeyistdkgyvyvvvvvlKELSDEVEEELKkLGFERLELEEEGTPSELIREIKEELEEIEKERE--------------S 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 1335178301 1593 TEKKLKEIFMQVEDERRHADQYKEQM-EKANARMKQLK 1629
Cdd:PRK05771 234 LLEELKELAKKYLEELLALYEYLEIElERAEALSKFLK 271
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1141-1628 |
5.21e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.68 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1141 KKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQL-----LAEEKNISARYAE 1215
Cdd:pfam05622 3 SEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLqkqleQLQEENFRLETAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1216 ERDRAEAEAREKETKALSLaraleealeakeeferQNKQLRADMEDLMSSKDDVGKNVHELEKSKRaLEQQVEEMRTQLE 1295
Cdd:pfam05622 83 DDYRIKCEELEKEVLELQH----------------RNEELTSLAEEAQALKDEMDILRESSDKVKK-LEATVETYKKKLE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1296 ELEDelqATEDAKLRLEVNMQAMKaqferdlQTRDEQNEEKK--------RLLIKQVRELEAELEDERKQralavasKKK 1367
Cdd:pfam05622 146 DLGD---LRRQVKLLEERNAEYMQ-------RTLQLEEELKKanalrgqlETYKRQVQELHGKLSEESKK-------ADK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1368 MEIDLKDLESQIEAANKARDEVIKQ----------LRKLQAQmkdyQRELEEARASRDEIFAQSKESEKKLKSLE--AEI 1435
Cdd:pfam05622 209 LEFEYKKLEEKLEALQKEKERLIIErdtlretneeLRCAQLQ----QAELSQADALLSPSSDPGDNLAAEIMPAEirEKL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1436 LQLQEElasSERARRHAEQERDELADEIansasgkSALLDEKRRLEARIaqleeeleeeQSNMELLNDRFRKTTLQVDTL 1515
Cdd:pfam05622 285 IRLQHE---NKMLRLGQEGSYRERLTEL-------QQLLEDANRRKNEL----------ETQNRLANQRILELQQQVEEL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1516 NAELAAERSAAQKSDNARQQLERQNKELK---AKLQELEGAVKSKFKATISALEAKIGQLEEQLEQeakeraaanklvrr 1592
Cdd:pfam05622 345 QKALQEQGSKAEDSSLLKQKLEEHLEKLHeaqSELQKKKEQIEELEPKQDSNLAQKIDELQEALRK-------------- 410
|
490 500 510
....*....|....*....|....*....|....*.
gi 1335178301 1593 tekklKEIFMQVEDERrhadqYKEQMEKANARMKQL 1628
Cdd:pfam05622 411 -----KDEDMKAMEER-----YKKYVEKAKSVIKTL 436
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1185-1632 |
5.60e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.75 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1185 QRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMS 1264
Cdd:pfam09731 43 GEEVVLYALGEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1265 SKDDVGKnvheLEKSKRALEQQVEEMRTQLEELEDE-LQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQ 1343
Cdd:pfam09731 123 EQEKEKA----LEEVLKEAISKAESATAVAKEAKDDaIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1344 VRELEAELEDerKQRALAVASKKKMEIDLKDLESQIEAANKARDE--VIKQLRKLQAQMKDY-QRELEearASRDEIFAQ 1420
Cdd:pfam09731 199 INLAKQSEEE--AAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLakLVDQYKELVASERIVfQQELV---SIFPDIIPV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1421 SKESEKKLK--------SLEAEILQLQEELASS-ERARRHAEQERDELADEIANSASGKSALLDEKRRLEARiaqleeel 1491
Cdd:pfam09731 274 LKEDNLLSNddlnsliaHAHREIDQLSKKLAELkKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEA-------- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1492 eeeqsnmellndrfrkttlqvdTLNAELAAERSAAQKS--DNARQQLERQNKELKAKLQElegavkskfkatisaleaki 1569
Cdd:pfam09731 346 ----------------------QLRLEFEREREEIRESyeEKLRTELERQAEAHEEHLKD-------------------- 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1335178301 1570 gQLEEQlEQEakeraaankLVRRTEKKLKEifmQVEDERrhaDQYKEQMEKANARMKQLKRQL 1632
Cdd:pfam09731 384 -VLVEQ-EIE---------LQREFLQDIKE---KVEEER---AGRLLKLNELLANLKGLEKAT 429
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1427-1676 |
7.33e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1427 KLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFR 1506
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1507 KTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATisALEAKIGQLEEQLEqEAKERAAA 1586
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK--ELVEKIKELEKELE-KAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1587 NKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSRE 1666
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
250
....*....|
gi 1335178301 1667 VSTLKNRLRR 1676
Cdd:COG1340 239 LRELRKELKK 248
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1343-1480 |
7.49e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.57 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1343 QVRELEAELEDERKQRALAVASKKKMEIdlkdLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEAR---------AS 1413
Cdd:pfam00529 59 ALDSAEAQLAKAQAQVARLQAELDRLQA----LESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQidlarrrvlAP 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1335178301 1414 RDEIFAQSKESEKKL-KSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRL 1480
Cdd:pfam00529 135 IGGISRESLVTAGALvAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
895-1200 |
7.77e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 895 DETLHKNNALKVVRELQAQiaELQEDFESEKASRNKAEK-----QKRDLSEELEALKTELEDTLDTTAAQQELRFKAN-- 967
Cdd:pfam17380 272 NQLLHIVQHQKAVSERQQQ--EKFEKMEQERLRQEKEEKareveRRRKLEEAEKARQAEMDRQAAIYAEQERMAMEREre 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 968 -----LEKNKQGLE-TDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHA----KVSEGDRLRvelaeKANKLQNELDN 1037
Cdd:pfam17380 350 lerirQEERKRELErIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAarkvKILEEERQR-----KIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1038 VSSLLEEAEKKGIKfskdaaSLESQLQDTQELLQEETRQKLNLSSRIRQLEEE----KNSLQEQQEEEEEA----RKNLE 1109
Cdd:pfam17380 425 IRAEQEEARQREVR------RLEEERAREMERVRLEEQERQQQVERLRQQEEErkrkKLELEKEKRDRKRAeeqrRKILE 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1110 KQVLALQSQLTDTKKK---VDDDLGTIES--LEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRlQQELDDLMVDLDH 1184
Cdd:pfam17380 499 KELEERKQAMIEEERKrklLEKEMEERQKaiYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE-RSRLEAMEREREM 577
|
330
....*....|....*.
gi 1335178301 1185 QRQIVSNlEKKQKKFD 1200
Cdd:pfam17380 578 MRQIVES-EKARAEYE 592
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1282-1624 |
7.80e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1282 ALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLlIKQVRELEAELEDERKQRALA 1361
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL-NEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1362 VASKKKMEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEE 1441
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1442 LASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAA 1521
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1522 ERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIF 1601
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
330 340
....*....|....*....|...
gi 1335178301 1602 MQVEDERRHADQYKEQMEKANAR 1624
Cdd:COG4372 347 LVGLLDNDVLELLSKGAEAGVAD 369
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1512-1675 |
9.27e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1512 VDTLNAELAAERSAAqkSDNARQQLERQNKELKAKLQELEGAVkSKFKA---------TISALEAKIGQLEEQLEQEAKE 1582
Cdd:COG3206 158 AEAYLEQNLELRREE--ARKALEFLEEQLPELRKELEEAEAAL-EEFRQknglvdlseEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1583 RAAANKLVRRTEKKLKEIFMQVEDERRHAdqykeQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEA-NE 1661
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQSP-----VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQ 309
|
170
....*....|....
gi 1335178301 1662 GLSREVSTLKNRLR 1675
Cdd:COG3206 310 EAQRILASLEAELE 323
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1266-1441 |
1.05e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1266 KDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEdaklrlevnmqamkaQFERDLQTRDEQNEEKKRLLIkqvr 1345
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAE---------------KLKEELEEKKEKLQEEEDKLL---- 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1346 eleAELEDERKQRalavaskkkmeidlkdlesqIEAANKARDEVIKQLRKLQAQMKDYQ--RELEEARASRDEIfAQSKE 1423
Cdd:PRK00409 569 ---EEAEKEAQQA--------------------IKEAKKEADEIIKELRQLQKGGYASVkaHELIEARKRLNKA-NEKKE 624
|
170
....*....|....*...
gi 1335178301 1424 SEKKLKSLEAEILQLQEE 1441
Cdd:PRK00409 625 KKKKKQKEKQEELKVGDE 642
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
846-1373 |
1.23e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 846 QVTRQEEEL---QAKDEELLKVKEKQTKVEGELEEMERKHQQARATAeaggDDETLHKNNALKVVRELQAQIAELQEDFE 922
Cdd:pfam12128 455 QATATPELLlqlENFDERIERAREEQEAANAEVERLQSELRQARKRR----DQASEALRQASRRLEERQSALDELELQLF 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 923 SEKAS-----RNKA----EKQKRDLSEELeALKTELEDTLDTTAAQQELRFkanleknkQGLETDnkelacevkvLQQVK 993
Cdd:pfam12128 531 PQAGTllhflRKEApdweQSIGKVISPEL-LHRTDLDPEVWDGSVGGELNL--------YGVKLD----------LKRID 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 994 AESEHKRKKldaqvqelhakvsegdrlrvELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQee 1073
Cdd:pfam12128 592 VPEWAASEE--------------------ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALK-- 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1074 trqklNLSSRIRQLEEEKNSLQeqqeeeeearknlekqvLALQSQLTDTKKKVDDDlgtIESLEEAKKKLLKDGEALSQR 1153
Cdd:pfam12128 650 -----NARLDLRRLFDEKQSEK-----------------DKKNKALAERKDSANER---LNSLEAQLKQLDKKHQAWLEE 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1154 LEEkalaydklEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEE-------RDRAEAEARE 1226
Cdd:pfam12128 705 QKE--------QKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDlaslgvdPDVIAKLKRE 776
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1227 KETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSkraLEQQVEEMRTQLEELEDELQATED 1306
Cdd:pfam12128 777 IRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQ---LARLIADTKLRRAKLEMERKASEK 853
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1335178301 1307 AKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKqvrELEAELEDERKQRALAVASKKKMEIDLK 1373
Cdd:pfam12128 854 QQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIG---ERLAQLEDLKLKRDYLSESVKKYVEHFK 917
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1401-1599 |
1.24e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1401 KDYQRELEEARASRDEIFAQSK---ESEKKLKSLEAeilqlQEELassERARRHAEQERDELADEIAnsasgksalldek 1477
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKkeaEAIKKEALLEA-----KEEI---HKLRNEFEKELRERRNELQ------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1478 rRLEARIAQLEeeleeeqsnmELLNDRfrkttlqvdtlNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSK 1557
Cdd:PRK12704 86 -KLEKRLLQKE----------ENLDRK-----------LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1335178301 1558 FKAtISAL---EAKiGQLEEQLEQEAKERAAanKLVRRTEKKLKE 1599
Cdd:PRK12704 144 LER-ISGLtaeEAK-EILLEKVEEEARHEAA--VLIKEIEEEAKE 184
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1376-1477 |
1.26e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.93 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1376 ESQIEAANKARDEvikqlrkLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKslEAEILQLQEELAS-SERARRHAEQ 1454
Cdd:COG0711 37 ADGLAEAERAKEE-------AEAALAEYEEKLAEARAEAAEIIAEARKEAEAIA--EEAKAEAEAEAERiIAQAEAEIEQ 107
|
90 100
....*....|....*....|...
gi 1335178301 1455 ERDELADEIANSASGKSALLDEK 1477
Cdd:COG0711 108 ERAKALAELRAEVADLAVAIAEK 130
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
1192-1384 |
1.28e-03 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 43.15 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1192 LEKKQKKFDQLLAEEKNISARYAEERDRAEAeAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKD-DVG 1270
Cdd:COG5414 202 IEEVEKKVDDLLEKDMKAESVSVVLKDEKEL-ARQERVSSWENFKEEPGEPLSRPALKKEKQGAEEEGEEGMSEEDlDVG 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1271 KNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLrlevnmqamkaQFERDLQTRDEQNEEKKRLLIKQVRELEAE 1350
Cdd:COG5414 281 AAEIENKEVSEGDKEQQQEEVENAEAHKEEVQSDRPDEI-----------GEEKEEDDENEENERHTELLADELNELEKG 349
|
170 180 190
....*....|....*....|....*....|....*.
gi 1335178301 1351 LEDERKQ--RALAVASKKKMEIDLKDLESQIEAANK 1384
Cdd:COG5414 350 IEEKRRQmeSATNPILQKRFESQLNVLLKELELKRK 385
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1360-1614 |
1.39e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1360 LAVASKKKMEIDLKDLE--SQIEAANKARDEVIKQ--------LRKLQAQMKDYQRELEEARASRDEIFA--QSK--ESE 1425
Cdd:PHA02562 147 LSAPARRKLVEDLLDISvlSEMDKLNKDKIRELNQqiqtldmkIDHIQQQIKTYNKNIEEQRKKNGENIArkQNKydELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1426 KKLKSLEAEILQLQEELAsserarrhaeqerdELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSN-------- 1497
Cdd:PHA02562 227 EEAKTIKAEIEELTDELL--------------NLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGgvcptctq 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1498 -MELLNDRFRKTTLQVDTLNAELaaersaaQKSDNARQQLERQNKELKA---KLQELEGAVkSKFKATISALEAKIGQLE 1573
Cdd:PHA02562 293 qISEGPDRITKIKDKLKELQHSL-------EKLDTAIDELEEIMDEFNEqskKLLELKNKI-STNKQSLITLVDKAKKVK 364
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1335178301 1574 EQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQY 1614
Cdd:PHA02562 365 AAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1368-1530 |
1.47e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.80 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1368 MEIDLKDLESQIEAANKARDEVIKQLRKLQAQMKDYQ---RELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELAs 1444
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQaleSELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1445 seRARRHAEQE---RDELADEIANSASGKSALLDEKRRLEariAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAA 1521
Cdd:pfam00529 128 --RRRVLAPIGgisRESLVTAGALVAQAQANLLATVAQLD---QIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
....*....
gi 1335178301 1522 ERSAAQKSD 1530
Cdd:pfam00529 203 AKLDLERTE 211
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1372-1465 |
1.70e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.36 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1372 LKDLESQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKES--EKKLKSLEAEILQLQEELAsserar 1449
Cdd:cd22656 123 LDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAiaRKEIKDLQKELEKLNEEYA------ 196
|
90
....*....|....*.
gi 1335178301 1450 RHAEQERDELADEIAN 1465
Cdd:cd22656 197 AKLKAKIDELKALIAD 212
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1376-1477 |
1.77e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.11 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1376 ESQIEAANKARDEvikqlrkLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKslEAEILQLQEELASS-ERARRHAEQ 1454
Cdd:cd06503 36 AESLEEAEKAKEE-------AEELLAEYEEKLAEARAEAQEIIEEARKEAEKIK--EEILAEAKEEAERIlEQAKAEIEQ 106
|
90 100
....*....|....*....|...
gi 1335178301 1455 ERDELADEIANSASGKSALLDEK 1477
Cdd:cd06503 107 EKEKALAELRKEVADLAVEAAEK 129
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
852-1568 |
1.93e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.12 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 852 EELQAK-DEELLKVKEKQTK-VEGELEEMERKHQQARATAEAGGDDETLHKNNAL-KVVRELQAQIAELQEDFESEKASR 928
Cdd:TIGR01612 699 DDLKSKiDKEYDKIQNMETAtVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLnKILEDFKNKEKELSNKINDYAKEK 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 929 NKAEKQKRDLSEeleaLKTELEDTLDTTAAQQElRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQ 1008
Cdd:TIGR01612 779 DELNKYKSKISE----IKNHYNDQINIDNIKDE-DAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFIN 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1009 ELHAKVSEGDRLRVELAEKANKLQNEL--DNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKL--NLSSRI 1084
Cdd:TIGR01612 854 FENNCKEKIDSEHEQFAELTNKIKAEIsdDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKIceNTKESI 933
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1085 RQLEEEKNSLQEQQEEEEEARKN---LEKQVL-ALQSQLTDTKKKVDDDL--GTIESLEEAKKKLLKDGEALSQRL---E 1155
Cdd:TIGR01612 934 EKFHNKQNILKEILNKNIDTIKEsnlIEKSYKdKFDNTLIDKINELDKAFkdASLNDYEAKNNELIKYFNDLKANLgknK 1013
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1156 EKAL--AYDKLEKTKNRLQQELDDLMVDLDH-QRQIVSNLEKKQKKFDQLLAeeKNISARYAEERDRAEA------EARE 1226
Cdd:TIGR01612 1014 ENMLyhQFDEKEKATNDIEQKIEDANKNIPNiEIAIHTSIYNIIDEIEKEIG--KNIELLNKEILEEAEInitnfnEIKE 1091
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1227 KetkaLSLARALEEALEAKEEFERQNKQLRADMEDLmssKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQAT-- 1304
Cdd:TIGR01612 1092 K----LKHYNFDDFGKEENIKYADEINKIKDDIKNL---DQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAis 1164
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1305 -EDAKlRLEVNMQAMKAQFERDLQTRDEQNEekkrlLIKQVRELEAELEDERKQRALAVASKKKMEidlKDLESQIEAAN 1383
Cdd:TIGR01612 1165 nDDPE-EIEKKIENIVTKIDKKKNIYDEIKK-----LLNEIAEIEKDKTSLEEVKGINLSYGKNLG---KLFLEKIDEEK 1235
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1384 KARDEVIKQlrkLQAQMKDYqreleearasrDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRH--AEQERDELAD 1461
Cdd:TIGR01612 1236 KKSEHMIKA---MEAYIEDL-----------DEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHhiISKKHDENIS 1301
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1462 EIANSA-------SGKSALLDEKRRLEARIAQleeeleeEQSNMELLNDRFRKTTLQVDTLnaELAAERSAAQKSDNARQ 1534
Cdd:TIGR01612 1302 DIREKSlkiiedfSEESDINDIKKELQKNLLD-------AQKHNSDINLYLNEIANIYNIL--KLNKIKKIIDEVKEYTK 1372
|
730 740 750
....*....|....*....|....*....|....
gi 1335178301 1535 QLERQNKELKAKLQELEGAVKsKFKATISALEAK 1568
Cdd:TIGR01612 1373 EIEENNKNIKDELDKSEKLIK-KIKDDINLEECK 1405
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
909-1356 |
2.13e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 42.74 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 909 ELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELR--------FKANLEKNKQGLETDNK 980
Cdd:pfam13166 93 EIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDECWKKIKRKKNSalsealngFKYEANFKSRLLREIEK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 981 ELACEVKVLQQVKAESEHKRKKLDAQVQElhAKVSEGDRLRvELAEKANKLQNELDNVSSLLEEAEKKGI--KFSKDAAS 1058
Cdd:pfam13166 173 DNFNAGVLLSDEDRKAALATVFSDNKPEI--APLTFNVIDF-DALEKAEILIQKVIGKSSAIEELIKNPDlaDWVEQGLE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1059 LESQLQDTQELLQEETRQklnlsSRIRQLEEEKNslqeqqeeeeearknleKQVLALQSQLtdtKKKVDDDLGTIESLEE 1138
Cdd:pfam13166 250 LHKAHLDTCPFCGQPLPA-----ERKAALEAHFD-----------------DEFTEFQNRL---QKLIEKVESAISSLLA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1139 akkkLLKDGEALSQRLEEKALAYDKLEKTKNRLQQELDDLMvdldhqrqivsnlekkqkkfDQLLAEEKNISARYaeERD 1218
Cdd:pfam13166 305 ----QLPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLR--------------------RALEAKRKDPFKSI--ELD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1219 RAEAEArEKETKALSLAraleealeakeeferqNKQLRADMEdlmsskddvgkNVHELEKSKRALEQQVEemRTQLEELE 1298
Cdd:pfam13166 359 SVDAKI-ESINDLVASI----------------NELIAKHNE-----------ITDNFEEEKNKAKKKLR--LHLVEEFK 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1335178301 1299 DELQATEDAKLRLEvnmqamkAQFErDLQTRDEQNEEKKRLLIKQVRELEAELEDERK 1356
Cdd:pfam13166 409 SEIDEYKDKYAGLE-------KAIN-SLEKEIKNLEAEIKKLREEIKELEAQLRDHKP 458
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
963-1153 |
2.47e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 963 RFKANLEKNKQgLETDNKELACEVKVLQQVK-AESEHKRKKLDAQVQELHAKVsegdrlrVELAEKANKLQNELDNVSSL 1041
Cdd:pfam00038 12 RLASYIDKVRF-LEQQNKLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQL-------DTLTVERARLQLELDNLRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1042 LEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLqeqqeeeeeaRKNLEKQVLALQSQLTD 1121
Cdd:pfam00038 84 AEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFL----------KKNHEEEVRELQAQVSD 153
|
170 180 190
....*....|....*....|....*....|..
gi 1335178301 1122 TKKKVDDDLGTIESLEEAKKKLLKDGEALSQR 1153
Cdd:pfam00038 154 TQVNVEMDAARKLDLTSALAEIRAQYEEIAAK 185
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
885-1023 |
2.69e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 885 ARATAEAGGDDETLhkNNalkVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLdttaAQQELRF 964
Cdd:PRK00409 505 EEAKKLIGEDKEKL--NE---LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLL----EEAEKEA 575
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1335178301 965 KANLEKNKQGLETDNKELACEVKVLQ-QVKA-ESEHKRKKLDAQVQELHAKVS----------EGDRLRVE 1023
Cdd:PRK00409 576 QQAIKEAKKEADEIIKELRQLQKGGYaSVKAhELIEARKRLNKANEKKEKKKKkqkekqeelkVGDEVKYL 646
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1061-1320 |
2.72e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1061 SQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAK 1140
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1141 KKLLKDGEALSQRLEEKALAYDKLEKTK---NRLQQELDDL-------MVDLDHQRQIVSNLEKKQKKFDQLLAEE---- 1206
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLewrqqteVLSPEEEKELVEKIKELEKELEKAKKALekne 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1207 --KNISARYAEERDRAEAEAREKETkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALE 1284
Cdd:COG1340 161 klKELRAELKELRKEAEEIHKKIKE----LAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 1335178301 1285 QQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1320
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1422-1659 |
2.87e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1422 KESEKKLKSLEAE-ILQLQEELASS-ERARRHAEQERD---ELADEIANSASGKSALLDEKRRLEaRIAQLEEELEEEQS 1496
Cdd:pfam17380 287 RQQQEKFEKMEQErLRQEKEEKAREvERRRKLEEAEKArqaEMDRQAAIYAEQERMAMERERELE-RIRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1497 NMEllndrfrkttlqvdtlnaELAAERSAAQKSDnaRQQLERQNKELKAKlQELEGAVKSKF---------KATISALEA 1567
Cdd:pfam17380 366 RQE------------------EIAMEISRMRELE--RLQMERQQKNERVR-QELEAARKVKIleeerqrkiQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1568 KIGQLEEQLEQEAK----ERAAANKLVRRTEKKLK---EIFMQVEDERRHADQYKEQMEKANARMKQLKR-----QLEEA 1635
Cdd:pfam17380 425 IRAEQEEARQREVRrleeERAREMERVRLEEQERQqqvERLRQQEEERKRKKLELEKEKRDRKRAEEQRRkilekELEER 504
|
250 260
....*....|....*....|....
gi 1335178301 1636 EEEATRANASRRKLQRELDDATEA 1659
Cdd:pfam17380 505 KQAMIEEERKRKLLEKEMEERQKA 528
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1380-1486 |
2.90e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.52 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1380 EAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDEL 1459
Cdd:pfam20492 2 EEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQL 81
|
90 100
....*....|....*....|....*..
gi 1335178301 1460 ADEIANSASGKSALLDEKRRLEARIAQ 1486
Cdd:pfam20492 82 EAELAEAQEEIARLEEEVERKEEEARR 108
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
898-1090 |
3.01e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 898 LHKNNALKVVRELQAQIAELQEdfESEKASRNKAEKQKRDLSEELEALKTELEDTLdttaAQQELRFKANLEKNKQGLET 977
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKEL----RERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 978 DNKELAcevkvlqqvkaESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIkfskdaa 1057
Cdd:PRK12704 98 LDRKLE-----------LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEIL------- 159
|
170 180 190
....*....|....*....|....*....|...
gi 1335178301 1058 slesqLQDTQELLQEETrqklnlSSRIRQLEEE 1090
Cdd:PRK12704 160 -----LEKVEEEARHEA------AVLIKEIEEE 181
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1275-1486 |
3.02e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1275 ELEKSKRALEQQVEEMRTQLEELED-ELQATEDAKLRLEVNMQAMKAQFERDLQT------RDEQN-----EEKKRLLiK 1342
Cdd:COG0497 176 ELRADEAERARELDLLRFQLEELEAaALQPGEEEELEEERRRLSNAEKLREALQEalealsGGEGGaldllGQALRAL-E 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1343 QVRELEAELED--ERKQRALavaskkkmeIDLKDLESQIEA------ANKAR-DEVIKQLRKLQAQMKDYQRELEEARAS 1413
Cdd:COG0497 255 RLAEYDPSLAElaERLESAL---------IELEEAASELRRyldsleFDPERlEEVEERLALLRRLARKYGVTVEELLAY 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1335178301 1414 RDEIfaqskesEKKLKSLEAeilqLQEELASSERARRHAEQERDELADEIanSASGKSALldekRRLEARIAQ 1486
Cdd:COG0497 326 AEEL-------RAELAELEN----SDERLEELEAELAEAEAELLEAAEKL--SAARKKAA----KKLEKAVTA 381
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
1264-1419 |
3.18e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 41.48 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1264 SSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDaklrlEVN-----------MQAMK-AQFERDLQ-TRD 1330
Cdd:pfam15397 60 SNKKQLQQAKAELQEWEEKEESKLNKLEQQLEQLNAKIQKTQE-----ELNflstykdkeypVKAVQiANLVRQLQqLKD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1331 EQNEEKKRL--LIKQVRE-LEAELEDERKQRALAVASK---------KKMEIDLKDLESQIEAANKARDEVIKQLRKLQA 1398
Cdd:pfam15397 135 SQQDELDELeeMRRMVLEsLSRKIQKKKEKILSSLAEKtlspyqeslLQKTRDNQVMLKEIEQFREFIDELEEEIPKLKA 214
|
170 180
....*....|....*....|.
gi 1335178301 1399 QMKDYQRELEEArasRDEIFA 1419
Cdd:pfam15397 215 EVQQLQAQRQEP---REVIFA 232
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1257-1397 |
3.48e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1257 ADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDElqaTEDAKLRLEVNMQAMKAQFERDLQT-------- 1328
Cdd:cd22656 107 TDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQ---TEKDQTALETLEKALKDLLTDEGGAiarkeikd 183
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1335178301 1329 -RDEQNEEKKRLL------IKQVRELEAELEDERKQRALAVASKKKMEIDLKDLESQIEAAnkardevIKQLRKLQ 1397
Cdd:cd22656 184 lQKELEKLNEEYAaklkakIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPA-------IPALEKLQ 252
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
845-1077 |
3.58e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 845 LQVTRQE------EELQAKDEELLKVKEKQTKVEGELEEMErkhqQARATAEAGgddetlhknnalkvvRELQAQIAELQ 918
Cdd:pfam17380 383 LQMERQQknervrQELEAARKVKILEEERQRKIQQQKVEME----QIRAEQEEA---------------RQREVRRLEEE 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 919 EDFESEKASRNKAEKQkrdlsEELEALKTELEDTldttaAQQELRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEH 998
Cdd:pfam17380 444 RAREMERVRLEEQERQ-----QQVERLRQQEEER-----KRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEER 513
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1335178301 999 KRKKLDAQVQELHAKVSEGDRLRVelAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAAsLESQLQDTQELLQEETRQK 1077
Cdd:pfam17380 514 KRKLLEKEMEERQKAIYEEERRRE--AEEERRKQQEMEERRRIQEQMRKATEERSRLEA-MEREREMMRQIVESEKARA 589
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1527-1675 |
3.70e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1527 QKSDNARQQLERQNKELKAKLQELEGAVKsKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLkeifMQVED 1606
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELA-ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL----GNVRN 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1335178301 1607 ERrhadqykeQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLR 1675
Cdd:COG1579 88 NK--------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
911-1122 |
3.76e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 911 QAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTL-DTTAAQQEL-RFKANLEKNKQGLETDNKELACEVKV 988
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQaELEALQAEIdKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 989 LQQVKAESEHKRKKLDAQ-VQELHAKVSEGDRLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQ 1067
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSEsFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1335178301 1068 ELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDT 1122
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1385-1666 |
3.81e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1385 ARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASserarrhAEQERDELADEIA 1464
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQE-------LREKRDELNEKVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1465 NSASGKSALLDEKRRLEARIAQLEEeleeeqsnmelLNDRFRKTTLQVDTLNAELAAERSAAQKSD---NARQQLERQNK 1541
Cdd:COG1340 75 ELKEERDELNEKLNELREELDELRK-----------ELAELNKAGGSIDKLRKEIERLEWRQQTEVlspEEEKELVEKIK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1542 ELKAKLQELEGAVKskfkatisaLEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKA 1621
Cdd:COG1340 144 ELEKELEKAKKALE---------KNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1335178301 1622 NARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSRE 1666
Cdd:COG1340 215 HKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKRE 259
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1342-1449 |
3.91e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.16 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1342 KQVRELEAELEDERKQRALAVASKKKMEidlKDLESQIEAANKARD----------EVIKQLRKLQAQMKDYQRELEEAR 1411
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQ---EDLEKQAEIAREAQQnyerelvlhaEDIKALQALREELNELKAEIAELK 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 1335178301 1412 ASRDEIFAQSKESEkklKSLEAEILQLQEELASSERAR 1449
Cdd:pfam07926 78 AEAESAKAELEESE---ESWEEQKKELEKELSELEKRI 112
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1510-1676 |
4.24e-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: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1510 LQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKsKFKATISALEAKIGQLEEQL-------EQEA-- 1580
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK-RLELEIEEVEARIKKYEEQLgnvrnnkEYEAlq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1581 KERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEeaeeeaTRANASRRKLQRELDDATEAN 1660
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD------EELAELEAELEELEAEREELA 169
|
170
....*....|....*.
gi 1335178301 1661 EGLSREVSTLKNRLRR 1676
Cdd:COG1579 170 AKIPPELLALYERIRK 185
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1443-1669 |
4.28e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1443 ASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAE 1522
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1523 RSAAQKSDNARQQLER--QNKELKAKLQELE--GAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLK 1598
Cdd:COG3883 92 ARALYRSGGSVSYLDVllGSESFSDFLDRLSalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1335178301 1599 EIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVST 1669
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1363-1464 |
4.38e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1363 ASKKKMEID-----LKDLESQIEAANKARDEVIK-----------QLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK 1426
Cdd:COG0542 399 AARVRMEIDskpeeLDELERRLEQLEIEKEALKKeqdeasferlaELRDELAELEEELEALKARWEAEKELIEEIQELKE 478
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1335178301 1427 KLKSLEAEILQLQEELAS-SERARRHAEQERDEL-ADEIA 1464
Cdd:COG0542 479 ELEQRYGKIPELEKELAElEEELAELAPLLREEVtEEDIA 518
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1296-1586 |
4.44e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.86 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1296 ELEDELQATEDAKLRLEvnmqAMKAQFERDlqtrdeqneekkrlliKQVREleaeledERKQRAlAVASKKKMEIDLKDL 1375
Cdd:PRK05035 440 AIEQEKKKAEEAKARFE----ARQARLERE----------------KAARE-------ARHKKA-AEARAAKDKDAVAAA 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1376 ESQIEAANKARDEVIK----QLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKlKSLEAEIlqlqeelassERAR-R 1450
Cdd:PRK05035 492 LARVKAKKAAATQPIVikagARPDNSAVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAI----------ARAKaK 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1451 HAEQErdeladeiANSASGKSALLDEKRRLEARIAQLEEELEEEQSNmellNDRFRKTTLQVDTLNAELAAERSAAQKSD 1530
Cdd:PRK05035 561 KAAQQ--------AANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAA----SAEPEEQVAEVDPKKAAVAAAIARAKAKK 628
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1335178301 1531 NARQQLERQNKELKAKlqelegavKSKFKATISALEAKIGQLEEQL---EQEAKERAAA 1586
Cdd:PRK05035 629 AEQQANAEPEEPVDPR--------KAAVAAAIARAKARKAAQQQANaepEEAEDPKKAA 679
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1511-1592 |
4.67e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 40.80 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1511 QVDTLNAELAAERS-------------AAQKSDNARQQLERQNKELKAKLQELEGAVKSkfkATISALEAKIGQLEEQLE 1577
Cdd:COG4223 1 EIAALEAAVAELPAqltaleqrlaaleAAPAAAAATAALEARLAALRAALAAAREAVAA---AAAAALEARLAALEAKAA 77
|
90
....*....|....*
gi 1335178301 1578 QEAKERAAANKLVRR 1592
Cdd:COG4223 78 APEAEAAAAARAAAL 92
|
|
| Cytochrom_B562 |
pfam07361 |
Cytochrome b562; This family contains the bacterial cytochrome b562. This forms a four-helix ... |
1311-1429 |
5.44e-03 |
|
Cytochrome b562; This family contains the bacterial cytochrome b562. This forms a four-helix bundle that non-covalently binds a single heme prosthetic group..
Pssm-ID: 429427 Cd Length: 101 Bit Score: 38.03 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1311 LEVNMQAMKAQFERDLQTRDeqneekkrllikqVRELEAELEDerkQRALAVASKKKMEIDLKDLESQIEAANKARDEVI 1390
Cdd:pfam07361 1 LKEDMKQMKLAYKQAAKADD-------------AAELKQALAK---LRAAAEDAKEATPPKLEGDSEEFKDYQEGMDKLI 64
|
90 100 110
....*....|....*....|....*....|....*....
gi 1335178301 1391 KQLRKLQAQMKdyQRELEEARASRDEIFAQSKESEKKLK 1429
Cdd:pfam07361 65 AQLDKADALAD--AGKLDEAKAALKKLKDLRKEYHKKFK 101
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
898-1077 |
5.79e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 898 LHKNNaLKVVRELQAQ-IAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTldtTAAQQELRFKANLEKNKqgLE 976
Cdd:PHA02562 199 TYNKN-IEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDP---SAALNKLNTAAAKIKSK--IE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 977 TDNKEL----------AC------EVKVLQQVK---AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQN---- 1033
Cdd:PHA02562 273 QFQKVIkmyekggvcpTCtqqiseGPDRITKIKdklKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTnkqs 352
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1034 ------ELDNVSSLLEEAEKKGIKFSKDAASLESQLQDTQELLQEETRQK 1077
Cdd:PHA02562 353 litlvdKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
846-1002 |
5.94e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 846 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQARATAEAGGDDET----LHKNNALKVVR----------ELQ 911
Cdd:COG4942 70 RIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlallLSPEDFLDAVRrlqylkylapARR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 912 AQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRfkANLEKNKQGLETDNKELACEVKVLQQ 991
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL--ARLEKELAELAAELAELQQEAEELEA 227
|
170
....*....|.
gi 1335178301 992 VKAESEHKRKK 1002
Cdd:COG4942 228 LIARLEAEAAA 238
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1506-1676 |
6.27e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.87 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1506 RKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAvkskfKATISALEAKIGQLEEQLEQEAKERAa 1585
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGA-----TAQLRAAQAAVKAAQAQLAQAQIDLA- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1586 anklvrRTEKKLKEIFMQvedeRRHADQYKEQMEKANARMKQLKRQLEEAEEEAT-RANASRRKLQRELDDATEANEGLS 1664
Cdd:pfam00529 128 ------RRRVLAPIGGIS----RESLVTAGALVAQAQANLLATVAQLDQIYVQITqSAAENQAEVRSELSGAQLQIAEAE 197
|
170
....*....|..
gi 1335178301 1665 REVSTLKNRLRR 1676
Cdd:pfam00529 198 AELKLAKLDLER 209
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1053-1312 |
6.42e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.56 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1053 SKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLTDTKKKVDDDLGT 1132
Cdd:pfam15905 44 SKDASTPATARKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSAS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1133 IESLEEAKKKLLKDGEALSQRLEE----KALAYDKLE--KTKNRLQQELDDLMV--------------DLDHQRQIVSNL 1192
Cdd:pfam15905 124 VASLEKQLLELTRVNELLKAKFSEdgtqKKMSSLSMElmKLRNKLEAKMKEVMAkqegmegklqvtqkNLEHSKGKVAQL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1193 EKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKN 1272
Cdd:pfam15905 204 EEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEK 283
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1335178301 1273 VHELEKSKralEQQVEEMRTQLEELEDELQATEDaKLRLE 1312
Cdd:pfam15905 284 CKLLESEK---EELLREYEEKEQTLNAELEELKE-KLTLE 319
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
854-953 |
6.51e-03 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 39.57 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 854 LQAKDEELLKVKEKQTKVEGELEEMERKhqQARATAEAGGDDETLHKNNalKVVRELQAQIAELQEDFESEKASRNKAEK 933
Cdd:pfam05266 90 PQSRINKLLSLKDRQTKLLEELKKLEKK--IAEEESEKRKLEEEIDELE--KKILELERQLALAKEKKEAADKEIARLKS 165
|
90 100
....*....|....*....|
gi 1335178301 934 QKRDLSEELEALKTELEDTL 953
Cdd:pfam05266 166 EAEKLEQEIQDVELEFEATA 185
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1377-1480 |
6.97e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.48 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1377 SQIEAANKARDEVIKQLRKLQAQMKD-YQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRhaeQE 1455
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAqSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK---QK 217
|
90 100
....*....|....*....|....*..
gi 1335178301 1456 RDELADEIAnsasgKSALLDEK--RRL 1480
Cdd:PRK11448 218 RKEITDQAA-----KRLELSEEetRIL 239
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1250-1356 |
7.02e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.64 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1250 RQNKQLRAD--MEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQ 1327
Cdd:cd16269 161 VPRKGVKAEevLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240
|
90 100 110
....*....|....*....|....*....|
gi 1335178301 1328 TRDEQNEEKKRLLIK-QVRELEAELEDERK 1356
Cdd:cd16269 241 QLKEKMEEERENLLKeQERALESKLKEQEA 270
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1258-1676 |
7.06e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.83 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1258 DMEDLMSSKDDVGKNVHELEKS-------KRALEQQVEEMRTQLEELED-----------------ELQATEDAKLRLEV 1313
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQvsllqeeKNSLQQENKKLQERLDQLESgddsgtpggkkylllqkQLEQLQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1314 NMQAMK---AQFERDLQTRDEQNEE------KKRLLIKQVRELEAELEDERKQRALAVASKKKMEiDLKDLESQIEAANK 1384
Cdd:pfam05622 81 ARDDYRikcEELEKEVLELQHRNEEltslaeEAQALKDEMDILRESSDKVKKLEATVETYKKKLE-DLGDLRRQVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1385 ARDEVIKQ-------LRK---LQAQMKDYQRELEEARASRDEifaQSKESEKklksLEAEILQLQEELASSERARRHAEQ 1454
Cdd:pfam05622 160 RNAEYMQRtlqleeeLKKanaLRGQLETYKRQVQELHGKLSE---ESKKADK----LEFEYKKLEEKLEALQKEKERLII 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1455 ERDELADeiANSasgksalldekrrlEARIAQLEEELEEEQSNMEllndrfRKTTLQVDTLNAELAaerSAAQKSDNARq 1534
Cdd:pfam05622 233 ERDTLRE--TNE--------------ELRCAQLQQAELSQADALL------SPSSDPGDNLAAEIM---PAEIREKLIR- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1535 qLERQNKELKAKLQELEgavkskfkatisalEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHAdqy 1614
Cdd:pfam05622 287 -LQHENKMLRLGQEGSY--------------RERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKAL--- 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1335178301 1615 KEQMEKANARMkQLKRQLEEAEEEATRANASRRKLQRELDD-ATEANEGLSREVSTLKNRLRR 1676
Cdd:pfam05622 349 QEQGSKAEDSS-LLKQKLEEHLEKLHEAQSELQKKKEQIEElEPKQDSNLAQKIDELQEALRK 410
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1425-1589 |
7.28e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1425 EKKLKSLEAEILQLQEELaSSERARRHaeqerdELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSnmellndr 1504
Cdd:PRK09039 52 DSALDRLNSQIAELADLL-SLERQGNQ------DLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG-------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1505 frkttlQVDTLNAELAAERsaaQKSDNARQQLERQNKElkaklqelegavkskfkatISALEAKIGQLEEQLE-QEAKER 1583
Cdd:PRK09039 117 ------RAGELAQELDSEK---QVSARALAQVELLNQQ-------------------IAALRRQLAALEAALDaSEKRDR 168
|
....*.
gi 1335178301 1584 AAANKL 1589
Cdd:PRK09039 169 ESQAKI 174
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1276-1480 |
7.29e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1276 LEKSK-RALEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDE 1354
Cdd:PHA02562 171 LNKDKiRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR----KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1355 RKQRALAVASKKKMEIDLKDLESQIEAANK----------------ARDEVIKQLRKLQAQMKDYQRELEEARASRDE-- 1416
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEle 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1335178301 1417 -IFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRL 1480
Cdd:PHA02562 327 eIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
910-1434 |
7.89e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.83 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 910 LQAQIAELQE---DFESEKASRNKAEKQKRDLSEELEALKTELedtLDTTAAQQELRFKANLeknkqgLETDNKELACEV 986
Cdd:pfam05622 33 LQQENKKLQErldQLESGDDSGTPGGKKYLLLQKQLEQLQEEN---FRLETARDDYRIKCEE------LEKEVLELQHRN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 987 KVLQQVKAESEHKRKKLDAqvqelhakvsegdrLRvELAEKANKLQNELDNVSSLLEeaekkgikfskDAASLESQLqdt 1066
Cdd:pfam05622 104 EELTSLAEEAQALKDEMDI--------------LR-ESSDKVKKLEATVETYKKKLE-----------DLGDLRRQV--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1067 qELLQEETRQKLNlssRIRQLEEEknslqeqqeeeeeARK--NLEKQVLALQSQLTDTKKKVDDDLGTIESLEEAKKKLl 1144
Cdd:pfam05622 155 -KLLEERNAEYMQ---RTLQLEEE-------------LKKanALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKL- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1145 kdgealsqrlEEKalaYDKLEKTKNRLQQELDDL----------MVDLDHQRQIVSNLEKKQKKFDQLLAEEknISARYA 1214
Cdd:pfam05622 217 ----------EEK---LEALQKEKERLIIERDTLretneelrcaQLQQAELSQADALLSPSSDPGDNLAAEI--MPAEIR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1215 EERDRAEAEarekeTKALSLaraleealeakeefeRQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQL 1294
Cdd:pfam05622 282 EKLIRLQHE-----NKMLRL---------------GQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1295 EELedelqatedaklrlevnmqaMKAQFERDLQTRDEQNEEKK-RLLIKQVRELEAELEDERKQ---RALAVASKKKMEI 1370
Cdd:pfam05622 342 EEL--------------------QKALQEQGSKAEDSSLLKQKlEEHLEKLHEAQSELQKKKEQieeLEPKQDSNLAQKI 401
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1335178301 1371 DlkdlesQIEAANKARDEvikqlrKLQAQMKDYQRELEEAR------------ASRDEIFA---QSKESEKKLKSLEAE 1434
Cdd:pfam05622 402 D------ELQEALRKKDE------DMKAMEERYKKYVEKAKsviktldpkqnpASPPEIQAlknQLLEKDKKIEHLERD 468
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1029-1419 |
7.98e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1029 NKLQNELDNVSSLLEEAEKKGIKFSKDAASLEsqlqdTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNL 1108
Cdd:COG5185 171 ELNQNLKKLEIFGLTLGLLKGISELKKAEPSG-----TVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1109 EK---QVLALQSQLTDTKKKVDDDLG----TIESLEEAKKKLLKDGEALSQRLEEKALAYDKLEKTKNRLQQelddlmvd 1181
Cdd:COG5185 246 EDlaqTSDKLEKLVEQNTDLRLEKLGenaeSSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQ-------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1182 lDHQRQIVSNLEKKQKKFDQLLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMED 1261
Cdd:COG5185 318 -LAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1262 LMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQtrdEQNEEKKRLLI 1341
Cdd:COG5185 397 PQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQ---SRLEEAYDEIN 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1342 KQVRELEAELEDERKQRALAVAS-KKKMEIDLKDLESQIEAANKARDEVI----------KQLRKLQAQMKDYQRELEEA 1410
Cdd:COG5185 474 RSVRSKKEDLNEELTQIESRVSTlKATLEKLRAKLERQLEGVRSKLDQVAeslkdfmrarGYAHILALENLIPASELIQA 553
|
....*....
gi 1335178301 1411 RASRDEIFA 1419
Cdd:COG5185 554 SNAKTDGQA 562
|
|
| Mei5 |
pfam10376 |
Double-strand recombination repair protein; Mei5 is one of a pair of meiosis-specific proteins ... |
1325-1402 |
8.34e-03 |
|
Double-strand recombination repair protein; Mei5 is one of a pair of meiosis-specific proteins which facilitate the loading of Dmc1 on to Rad51 on DNA at double-strand breaks during recombination. Recombination is carried out by a large protein complex based around the two RecA homologs, Rad51 and Dmc1. This complex may play both a catalytic and a structural role in the interaction between homologous chromosomes during meiosis. Mei5 is seen to contain a coiled-coli region.
Pssm-ID: 431242 [Multi-domain] Cd Length: 207 Bit Score: 39.75 E-value: 8.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1335178301 1325 DLQTRDEQNEEKKRLLIKQVRELEAELederkqRALAVASKKKMEIDLKDLESQIeaaNKARDEVIKQLRKLQAQMKD 1402
Cdd:pfam10376 114 PEKIPKKELEAEKRKLEKQVDEKEELL------RRLKLVKMYRSKNDLSELQSLI---KKWRNCSQLLLEELQSAMSE 182
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1387-1543 |
8.72e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.60 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1387 DEVIKQL--RKLQAQMKDYQRELEEA----RASRDEIFA-QSKES----EKKLKSLEAEILQLQEELASserarrhAEQE 1455
Cdd:COG3524 164 EELVNQLseRAREDAVRFAEEEVERAeerlRDAREALLAfRNRNGildpEATAEALLQLIATLEGQLAE-------LEAE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1456 RDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMEL--LNDRFRktTLQVDTLNAELAAErSAAQKSDNAR 1533
Cdd:COG3524 237 LAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLasLLAEYE--RLELEREFAEKAYT-SALAALEQAR 313
|
170
....*....|
gi 1335178301 1534 QQLERQNKEL 1543
Cdd:COG3524 314 IEAARQQRYL 323
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1291-1632 |
8.80e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.59 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1291 RTQLEELEDELQATEDaklrlevNMQAMKAQFErDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVaskKKMEI 1370
Cdd:PRK04778 104 KHEINEIESLLDLIEE-------DIEQILEELQ-ELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPAL---DELEK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1371 DLKDLESQIEAANKARDEvikqlrklqaqmKDYqrelEEARasrdEIFAQSKESEKKLKSLEAEILQLQEELAsserarr 1450
Cdd:PRK04778 173 QLENLEEEFSQFVELTES------------GDY----VEAR----EILDQLEEELAALEQIMEEIPELLKELQ------- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1451 haeqerDELADEIANSASGKSALLDEKRRL-----EARIAQLEEELEEEQSNMELLN-DRFRKTTLQV--------DTLN 1516
Cdd:PRK04778 226 ------TELPDQLQELKAGYRELVEEGYHLdhldiEKEIQDLKEQIDENLALLEELDlDEAEEKNEEIqeridqlyDILE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1517 AELAAERSAAQKSDNARQQLER---QNKELKAKLQEL---------EGAVKSKFKATISALEAKIGQLEEQLEQEAKERA 1584
Cdd:PRK04778 300 REVKARKYVEKNSDTLPDFLEHakeQNKELKEEIDRVkqsytlnesELESVRQLEKQLESLEKQYDEITERIAEQEIAYS 379
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1335178301 1585 AANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQL 1632
Cdd:PRK04778 380 ELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1000-1230 |
9.23e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1000 RKKLDAQVQELH----------AKVSEGDRLRvELAEKANKLQNELDNVSSLLEEAEKKGIKFSKdaasleSQLQDTQEL 1069
Cdd:PRK05771 15 KSYKDEVLEALHelgvvhiedlKEELSNERLR-KLRSLLTKLSEALDKLRSYLPKLNPLREEKKK------VSVKSLEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1070 LQEETRQKLNLSSRIRQLEEEKNSLQEQqeeeeeaRKNLEKQVLALQS--------QLTDTKKKVDDDLGTIesleeaKK 1141
Cdd:PRK05771 88 IKDVEEELEKIEKEIKELEEEISELENE-------IKELEQEIERLEPwgnfdldlSLLLGFKYVSVFVGTV------PE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335178301 1142 KLLKDGEALSQRLEEKALAYDKLEK-----TKNRLQQELDDLMVDLDHQR--------------QIVSNLEKKQKKFDQL 1202
Cdd:PRK05771 155 DKLEELKLESDVENVEYISTDKGYVyvvvvVLKELSDEVEEELKKLGFERleleeegtpselirEIKEELEEIEKERESL 234
|
250 260 270
....*....|....*....|....*....|....*....
gi 1335178301 1203 LAEEKNISARYAE-----------ERDRAEAEAREKETK 1230
Cdd:PRK05771 235 LEELKELAKKYLEellalyeyleiELERAEALSKFLKTD 273
|
|
| |
