|
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 ... |
109-789 |
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: 1457.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGrkkeAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTMDSMA 348
Cdd:cd14920 157 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 349 IMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTK 428
Cdd:cd14920 237 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 429 EQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 508
Cdd:cd14920 317 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 509 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEAD 588
Cdd:cd14920 397 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 589 FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSSGessaPVTFGAAGLKTKKGMF 668
Cdd:cd14920 477 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGM----TETAFGSAYKTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 669 RTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEI 748
Cdd:cd14920 553 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1988774931 749 LTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14920 633 LTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
109-789 |
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: 1307.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKeavQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKK---KGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLL-GTADQYRFLSGGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLtGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 348 AIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQT 427
Cdd:cd01377 238 DILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 428 KEQADFAVEALAKATYERLFRWLVHRINRALDRrQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFI 507
Cdd:cd01377 318 KEQVVFSVGALAKALYERLFLWLVKRINKTLDT-KSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 508 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFF-KSKQPRGE 586
Cdd:cd01377 397 LEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFkKPKPKKSE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 587 ADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGldqvssgessapvtfGAAGLKTKKG 666
Cdd:cd01377 475 AHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGG---------------GGGKKKKKGG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 667 MFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 746
Cdd:cd01377 540 SFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRY 619
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1988774931 747 EILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd01377 620 SILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
109-789 |
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: 1167.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTMDSMA 348
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 349 IMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTK 428
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 429 EQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 508
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 509 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEAD 588
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 589 FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSSGESSAPVTFgaaglKTKKGMF 668
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHGAF-----KTRKGMF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 669 RTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEI 748
Cdd:cd14932 556 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1988774931 749 LTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14932 636 LTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
109-789 |
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: 1157.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQ-----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 263
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVNpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 264 FDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQT 343
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 344 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQ 423
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 424 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 503
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 504 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQp 583
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDF- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 584 RGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDrIVGLDQVSSGESsapvTFGAaglKT 663
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQALTDT----QFGA---RT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 664 KKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 743
Cdd:cd14911 549 RKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1988774931 744 QRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14911 629 QRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
109-789 |
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: 1126.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVASSHKGgtlgrKKEavQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKS-----KKD--QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTMDSMA 348
Cdd:cd14919 154 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 349 IMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTK 428
Cdd:cd14919 234 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 429 EQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 508
Cdd:cd14919 314 EQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 509 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEAD 588
Cdd:cd14919 394 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKAD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 589 FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSS-GESSAPVTFgaaglKTKKGM 667
Cdd:cd14919 474 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGmSETALPGAF-----KTRKGM 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 668 FRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 747
Cdd:cd14919 549 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 628
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1988774931 748 ILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14919 629 ILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
109-789 |
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: 1125.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVASSHKGgtlgRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKG----KKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTMDSMA 348
Cdd:cd14921 157 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 349 IMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTK 428
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 429 EQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 508
Cdd:cd14921 317 EQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 509 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEAD 588
Cdd:cd14921 397 EQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 589 FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSS-GESSAPvtfgaAGLKTKKGM 667
Cdd:cd14921 477 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKmTESSLP-----SASKTKKGM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 668 FRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 747
Cdd:cd14921 552 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1988774931 748 ILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14921 632 ILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
866-1946 |
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: 1122.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 866 TRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGEL 945
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 946 ETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEER 1025
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1026 LNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQ 1105
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1106 KEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQE 1185
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1186 LRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASR 1265
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1266 SESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDE 1345
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1346 SRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQR 1425
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1426 ERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLA 1505
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1506 LSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEV 1585
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1586 TLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQL 1665
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1666 RRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVL 1745
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1746 SEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGA 1825
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1826 VRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLE 1905
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1988774931 1906 EVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQL 1946
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
109-789 |
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: 1116.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTMDSMA 348
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 349 IMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTK 428
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 429 EQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 508
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 509 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEAD 588
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 589 FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVsSGESSAPVTFgaaglKTKKGMF 668
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKV-SGMSEMPGAF-----KTRKGMF 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 669 RTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEI 748
Cdd:cd15896 555 RTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 634
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1988774931 749 LTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd15896 635 LTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
97-789 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1104.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 97 VEDMADLTCLNEASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSML 176
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 177 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRkkeavqgeLERQLLQANPILEAFGNAKTVKNDNSSRF 256
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVGR--------LEEQILQSNPILEAFGNAKTVRNNNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 257 GKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQS 335
Cdd:pfam00063 153 GKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSqSGCYTIDGID 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 336 DSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRI 415
Cdd:pfam00063 233 DSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 416 KVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNE 495
Cdd:pfam00063 313 KTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 496 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHP 575
Cdd:pfam00063 393 KLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 576 KFFKSKQpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSSGESSAPvt 655
Cdd:pfam00063 470 HFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTPK-- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 656 fgaaglKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPN 735
Cdd:pfam00063 547 ------RTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPN 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1988774931 736 RIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:pfam00063 621 RITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
109-789 |
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: 1103.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVASSHKGgtlgRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKG----RKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQsDSENFTQTMDSMA 348
Cdd:cd14930 157 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ-ERELFQETLESLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 349 IMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTK 428
Cdd:cd14930 236 VLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 429 EQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 508
Cdd:cd14930 316 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 509 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEAD 588
Cdd:cd14930 396 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQAD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 589 FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSSGESSAPvtfgaaGLKTKKGMF 668
Cdd:cd14930 476 FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPP------GGRPRRGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 669 RTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEI 748
Cdd:cd14930 550 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1988774931 749 LTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14930 630 LTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
90-801 |
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: 1018.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 90 NPPRFSKVEDMADLTCLNEASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISE 169
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 170 AAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGtlgrkkeavqGELERQLLQANPILEAFGNAKTVK 249
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV----------GSVEDQILESNPILEAFGNAKTLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 250 NDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGS 328
Cdd:smart00242 151 NNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNqGGC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 329 IPVPGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFT 407
Cdd:smart00242 231 LTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 408 RAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQgASFIGILDIAGFEIFQLNSFEQ 487
Cdd:smart00242 311 KALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 488 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATDRSFVEKL 567
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 568 SGEQGSHPKFFKSKQpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdrivgldqvss 647
Cdd:smart00242 467 NQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG----------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 648 gessapvtfgaAGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIR 727
Cdd:smart00242 535 -----------VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIR 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774931 728 ICRQGFPNRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFRAGVLAHLEEERD 801
Cdd:smart00242 604 IRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
46-1261 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 902.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 46 VWVPSEKQGFESASIREERGDEVEVELTDSQRRVTLSREEVQ-----RMNPPRFSKVEDMADLTCLNEASVLHNLRERYY 120
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEGKKEDGESVSVKKKvlgndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 121 SGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGESGAGKTENTKK 200
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 201 VIQYLAHVASSHkggtlgrkkEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLL 280
Cdd:COG5022 172 IMQYLASVTSSS---------TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 281 EKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSMAIMGFTPEELMS 359
Cdd:COG5022 243 EKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSqGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 360 MLKVISAVLQFGNISFMKEKNhDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALA 439
Cdd:COG5022 323 IFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 440 KATYERLFRWLVHRINRALDRRQRQGaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE 519
Cdd:COG5022 402 KALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 520 WNFIDFgLDLQPCIDLIERpANPPGVLALLDEECWFPRATDRSFVEKLSG--EQGSHPKFFKSKQprGEADFSIIHYAGK 597
Cdd:COG5022 481 WSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRF--RDNKFVVKHYAGD 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 598 VDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVgldqvssgessapvtfgaaglktKKGMFRTVGQLYKE 677
Cdd:COG5022 557 VEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-----------------------SKGRFPTLGSRFKE 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 678 SLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPNAIPRT 757
Cdd:COG5022 614 SLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTG 693
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 758 ----FMDGKQASELMISALELDKNLFRVGQSKVFFRAGVLAHLEEERDLKITDTIIRFQSAARGFLSRKAFLKKQQQLSA 833
Cdd:COG5022 694 eytwKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKK 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 834 LRVMQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQDEEIQTREAALQKAKEQLTR---AEQDYTELDRKHAQLLEEKAVL 910
Cdd:COG5022 774 IQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKRekkLRETEEVEFSLKAEVLIQKFGR 853
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 911 ADQLQAEAELFAEAEEMRarlasrkqeleevlgeletrleeeeergVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLE 990
Cdd:COG5022 854 SLKAKKRFSLLKKETIYL----------------------------QSAQRVELAERQLQELKIDVKSISSLKLVNLELE 905
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 991 KVTLEtKVKSLETDLATAVE-QRERLGKEKKQLEERlnEVTDQLTEEEEKTKSLNKL---KNKQEAVIADLEERLKREEQ 1066
Cdd:COG5022 906 SEIIE-LKKSLSSDLIENLEfKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLhevESKLKETSEEYEDLLKKSTI 982
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1067 GRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRgSLAQKEKEITSLQgrleeegarraEAQRSLREALSQVSELKEEVE 1146
Cdd:COG5022 983 LVREGNKANSELKNFKKELAELSKQYGALQESTK-QLKELPVEVAELQ-----------SASKIISSESTELSILKPLQK 1050
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1147 NERGMreraEKQRRDLSEELEALRTELEDTLDSTaAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAAldsl 1226
Cdd:COG5022 1051 LKGLL----LLENNQLQARYKALKLRRENSLLDD-KQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQ---- 1121
|
1210 1220 1230
....*....|....*....|....*....|....*
gi 1988774931 1227 QEQLDNSKRARQSLEKAKATLEEERQNLTSELKSL 1261
Cdd:COG5022 1122 MIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLEL 1156
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
109-789 |
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: 873.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRH-EMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 188 GESGAGKTENTKKVIQYLAHVASSHKGgtlgrKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 267
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSS-----KSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 268 GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFL-----SGGSIPVPGQSDSENFTQ 342
Cdd:cd00124 156 GRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 343 TMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKN--HDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGRE 420
Cdd:cd00124 236 LLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEdeDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 421 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALD-RRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 499
Cdd:cd00124 316 TITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSpTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 500 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFK 579
Cdd:cd00124 396 FFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 580 SKQPRGEAdFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDhfvselwkevdrivgldqvssgessapvtfgaa 659
Cdd:cd00124 473 KKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ--------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 660 glktkkgmfrtvgqlYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPF 739
Cdd:cd00124 519 ---------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPF 583
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1988774931 740 QEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd00124 584 DEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
109-789 |
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: 792.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVASshKGGTLGRKKEAVQ----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 264
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAA--LGDGPGKKAQFLAtktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 265 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRaDLLLGTAD--QYRFLSGGSIPVPGQSDSENFTQ 342
Cdd:cd14927 159 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEELMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 343 TMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 422
Cdd:cd14927 238 TDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 423 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRR-QRQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 501
Cdd:cd14927 318 TKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKlPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 502 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFK- 579
Cdd:cd14927 396 NHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKp 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 580 --SKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivglDQVSSGESSAPVTFG 657
Cdd:cd14927 473 rpDKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---------ENYVGSDSTEDPKSG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 658 AAGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRI 737
Cdd:cd14927 544 VKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRI 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1988774931 738 PFQEFRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14927 624 LYADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
110-789 |
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: 773.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 190 SGAGKTENTKKVIQYLAHVASShkgGTLGRKKEA-VQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAAT---GDLAKKKDSkMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETrADLLLGTADQYR--FLSGGSIPVPGQSDSENFTQTMDS 346
Cdd:cd14913 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEILVASIDDAEELLATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 347 MAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKA 425
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKF-KQKQREEQAEPDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 426 QTKEQADFAVEALAKATYERLFRWLVHRINRALDRR-QRQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 504
Cdd:cd14913 317 QTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKlPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 505 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKSKQP 583
Cdd:cd14913 395 MFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKVV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 584 RG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivgldqVSSGESSAPVTFGaAGL 661
Cdd:cd14913 472 KGraEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY-----------ATFATADADSGKK-KVA 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 662 KTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 741
Cdd:cd14913 540 KKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGD 619
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1988774931 742 FRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14913 620 FKQRYRVLNASAIPEgQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
109-789 |
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: 758.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKeavqGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSK----GSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGT-ADQYRFLSGGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd14909 157 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDnIYDYYIVSQGKVTVPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 348 AIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQT 427
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 428 KEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFI 507
Cdd:cd14909 317 VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKR-QHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 508 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKSKQPRG- 585
Cdd:cd14909 396 LEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKPg 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 586 --EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEvdrivgldqvSSGESSAPVtfGAAGLKT 663
Cdd:cd14909 473 qqAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD----------HAGQSGGGE--QAKGGRG 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 664 KKGM-FRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEF 742
Cdd:cd14909 541 KKGGgFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDF 620
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1988774931 743 RQRYEILTPNAIpRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14909 621 KMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
109-789 |
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 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGrkkeavQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDG------KGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLL-GTADQYRFLSGGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd14934 155 KLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQGVTVVDNMDDGEELQITDVAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 348 AIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQT 427
Cdd:cd14934 235 DVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 428 KEQADFAVEALAKATYERLFRWLVHRINRALDRR-QRQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 506
Cdd:cd14934 315 MEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKmQRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 507 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKSKQPRG 585
Cdd:cd14934 393 VLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 586 ---EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSdHFVSELWKEvdrivgldqvssgESSAPvtfgAAGLK 662
Cdd:cd14934 470 kgpEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS-LGLLALLFK-------------EEEAP----AGSKK 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 663 TKKGM-FRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 741
Cdd:cd14934 532 QKRGSsFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPE 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1988774931 742 FRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14934 612 FKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
110-789 |
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: 727.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSG-LIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVASSHKGGTlgrkkeavqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET----------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd01380 152 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNqGGSPVIDGVDDAAEFEETRKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 348 AIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQT 427
Cdd:cd01380 232 TLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 428 KEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 506
Cdd:cd01380 312 LQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 507 ILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPRATDRSFVEKLSGE-QGSHPKFFKSkqPR- 584
Cdd:cd01380 392 KLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQhLKKPNKHFKK--PRf 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 585 GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHfvselwkevdrivgldqvssgessapvtfgaaglktK 664
Cdd:cd01380 466 SNTAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR------------------------------------K 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 665 KgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 744
Cdd:cd01380 510 K----TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFS 585
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1988774931 745 RYEILTPNAiPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd01380 586 RYRVLLPSK-EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
109-789 |
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: 713.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVASShkggTLGRKKeavQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAM----IESKKK---LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEetRADLLLGTAD--QYRFLSGGSIPVPGQSDSENFTQTMDS 346
Cdd:cd14929 154 MLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEELLATEQA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 347 MAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQ 426
Cdd:cd14929 232 MDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 427 TKEQADFAVEALAKATYERLFRWLVHRINRALDRR-QRQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 505
Cdd:cd14929 312 NIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKlSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHM 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 506 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKSKQPR 584
Cdd:cd14929 390 FVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 585 G--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKevdrivglDQVSSGESSapvTFGAAglK 662
Cdd:cd14929 467 KkfEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFE--------NYISTDSAI---QFGEK--K 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 663 TKKGM-FRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 741
Cdd:cd14929 534 RKKGAsFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYAD 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1988774931 742 FRQRYEILTPNAIPRT-FMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14929 614 FKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
110-789 |
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: 704.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 190 SGAGKTENTKKVIQYLAHVASShkGGTLGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 269
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAI--GDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 270 IVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETrADLLLGTAD--QYRFLSGGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 348 AIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASmPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQ 426
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 427 TKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 505
Cdd:cd14917 318 NVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQpRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 506 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKL-SGEQGSHPKFFKSKQPR 584
Cdd:cd14917 396 FVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLfDNHLGKSNNFQKPRNIK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 585 G--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivgldqVSSGESSAPVTFGAAglK 662
Cdd:cd14917 473 GkpEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLF-----------ANYAGADAPIEKGKG--K 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 663 TKKG-MFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 741
Cdd:cd14917 540 AKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGD 619
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1988774931 742 FRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14917 620 FRQRYRILNPAAIPEgQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
111-789 |
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: 697.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 111 VLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGES 190
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 191 GAGKTENTKKVIQYLAHVASShkggtlGRKKE----AVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 266
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVT------GEKKKeesgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 267 AGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTAD-QYRFLSGGSIPVPGQSDSENFTQTMD 345
Cdd:cd14918 157 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMATDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 346 SMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQK 424
Cdd:cd14918 237 AIDILGFTPEEKVSIYKLTGAVMHYGNMKF-KQKQREEQAEPDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 425 AQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 503
Cdd:cd14918 316 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 504 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKSKQ 582
Cdd:cd14918 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 583 PRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKevdrivgldQVSSGESSAPVTFGAag 660
Cdd:cd14918 471 VKGkaEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFS---------TYASAEADSGAKKGA-- 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 661 lKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 740
Cdd:cd14918 540 -KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYG 618
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1988774931 741 EFRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14918 619 DFKQRYKVLNASAIPEgQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
110-789 |
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: 692.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 190 SGAGKTENTKKVIQYLAHVASshkggTLGRKKEAV-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 264
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAV-----TGEKKKEEAtsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 265 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTAD-QYRFLSGGSIPVPGQSDSENFTQT 343
Cdd:cd14910 157 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 344 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 422
Cdd:cd14910 237 DSAIEILGFTSDERVSIYKLTGAVMHYGNMKF-KQKQREEQAEPDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 423 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 501
Cdd:cd14910 316 TKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 502 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKS 580
Cdd:cd14910 394 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 581 KQPRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivgldqvsSGESSAPVTFGA 658
Cdd:cd14910 471 KPAKGkvEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF-------------SGAAAAEAEEGG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 659 A--GLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNR 736
Cdd:cd14910 538 GkkGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1988774931 737 IPFQEFRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14910 618 ILYADFKQRYKVLNASAIPEgQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
110-789 |
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: 691.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 190 SGAGKTENTKKVIQYLAHVASSHKggtlgRKKEA----VQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 265
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGD-----KKKEQqpgkMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 266 VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETrADLLLGTADQYR--FLSGGSIPVPGQSDSENFTQT 343
Cdd:cd14923 157 ATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELLAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 344 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 422
Cdd:cd14923 236 DNAIDILGFSSEEKVGIYKLTGAVMHYGNMKF-KQKQREEQAEPDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 423 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 501
Cdd:cd14923 315 TKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 502 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSK 581
Cdd:cd14923 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 582 QP---RGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdriVGLDQVSSGESSapvtfga 658
Cdd:cd14923 470 KPakgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSK------- 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 659 AGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIP 738
Cdd:cd14923 540 KGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRIL 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 739 FQEFRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14923 620 YADFKQRYRILNASAIPEgQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
110-789 |
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: 687.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 190 SGAGKTENTKKVIQYLAHVASShkgGTLGRKKEA--VQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 267
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAI---GDRSKKENPnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 268 GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETrADLLLGTAD--QYRFLSGGSIPVPGQSDSENFTQTMD 345
Cdd:cd14916 159 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPEL-LDMLLVTNNpyDYAFVSQGEVSVASIDDSEELLATDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 346 SMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNTA-AQKLCHLLGVNVLEFTRAILTPRIKVGREYVQK 424
Cdd:cd14916 238 AFDVLGFTAEEKAGVYKLTGAIMHYGNMKF-KQKQREEQAEPDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 425 AQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 503
Cdd:cd14916 317 GQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQpRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 504 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKL-SGEQGSHPKFFKSKQ 582
Cdd:cd14916 395 HMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLyDNHLGKSNNFQKPRN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 583 PRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdriVGLDQVSSGESSapvtfgaaG 660
Cdd:cd14916 472 VKGkqEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY---ASADTGDSGKGK--------G 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 661 LKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 740
Cdd:cd14916 541 GKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1988774931 741 EFRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14916 621 DFRQRYRILNPAAIPEgQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
110-789 |
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: 686.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 190 SGAGKTENTKKVIQYLAHVASSHKggtlgRKKE-----AVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 264
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGE-----KKKEeitsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 265 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTAD-QYRFLSGGSIPVPGQSDSENFTQT 343
Cdd:cd14912 157 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPyDYPFVSQGEISVASIDDQEELMAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 344 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 422
Cdd:cd14912 237 DSAIDILGFTNEEKVSIYKLTGAVMHYGNLKF-KQKQREEQAEPDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 423 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 501
Cdd:cd14912 316 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 502 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKS 580
Cdd:cd14912 394 NHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 581 KQPRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdrivgldQVSSGESSApvtfGA 658
Cdd:cd14912 471 KVVKGkaEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGA-------QTAEGASAG----GG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 659 A--GLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNR 736
Cdd:cd14912 540 AkkGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSR 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1988774931 737 IPFQEFRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14912 620 ILYADFKQRYKVLNASAIPEgQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
110-789 |
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: 679.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 190 SGAGKTENTKKVIQYLAHVASSHKggtlGRKKEA----VQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 265
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGE----KKKEEAasgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 266 VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETrADLLLGTADQYRF--LSGGSIPVPGQSDSENFTQT 343
Cdd:cd14915 158 ATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 344 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 422
Cdd:cd14915 237 DSAVDILGFSADEKVAIYKLTGAVMHYGNMKF-KQKQREEQAEPDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 423 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 501
Cdd:cd14915 316 TKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 502 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKS 580
Cdd:cd14915 394 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 581 KQPRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSdhfvselWKEVDRIVGLDQVSSGESSApvtfGA 658
Cdd:cd14915 471 KPAKGkaEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSG-------MKTLAFLFSGGQTAEAEGGG----GK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 659 AGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIP 738
Cdd:cd14915 540 KGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 739 FQEFRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14915 620 YADFKQRYKVLNASAIPEgQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
110-789 |
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: 674.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 190 SGAGKTENTKKVIQYLAHVASSHKggtlgrkkeavqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 269
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 270 IVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGA--SEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDS 346
Cdd:cd14883 149 IKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAkhSKELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 347 MAIMGFTPEELMSMLKVISAVLQFGNISFMK-EKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKA 425
Cdd:cd14883 229 MNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 426 QTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 505
Cdd:cd14883 309 LKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 506 FILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRG 585
Cdd:cd14883 388 FKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRW 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 586 EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVD--RIVGLDQVSSGESSApvtfgaagLKT 663
Cdd:cd14883 465 KTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDllALTGLSISLGGDTTS--------RGT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 664 KKGMfRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 743
Cdd:cd14883 537 SKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFV 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1988774931 744 QRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14883 616 DRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
110-789 |
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: 663.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 190 SGAGKTENTKKVIQYLAHVASSHkggtlgrkkeavQGELER---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 266
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGS------------ESEVERvkdMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 267 AGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMD 345
Cdd:cd01378 150 KGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSkSGCFDVDGIDDAADFKEVLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 346 SMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREY---V 422
Cdd:cd01378 230 AMKVIGFTEEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 423 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFn 502
Cdd:cd01378 309 EVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 503 hTMFIL--EQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-RATDRSFVEKLSGEQGSHPKFFK 579
Cdd:cd01378 388 -IELTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFEC 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 580 SKQPR--GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDrivgldqvssgessapvtfg 657
Cdd:cd01378 464 PSGHFelRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGV-------------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 658 aagLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRI 737
Cdd:cd01378 524 ---DLDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQ 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 738 PFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd01378 601 TYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
110-789 |
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: 644.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRgkKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 190 SGAGKTENTKKVIQYLAHVAsshkGGTLGrkkeavqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 269
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALG----GGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 270 IVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSG-GSIPVPGQSDSENFTQTMDSMA 348
Cdd:cd01383 147 ICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQsNCLTIDGVDDAKKFHELKEALD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 349 IMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTK 428
Cdd:cd01383 227 TVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 429 EQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 508
Cdd:cd01383 307 QQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 509 EQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRgead 588
Cdd:cd01383 387 EQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGERGGA---- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 589 FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLhQSSDHFVSELWKEVDRIVGLDQVSSgessapvtfgaAGLKTKKGMF 668
Cdd:cd01383 460 FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQLFASKMLDASRKALPL-----------TKASGSDSQK 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 669 RTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEI 748
Cdd:cd01383 528 QSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGF 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1988774931 749 LTPNAiprtfMDGKQaSELMISALELDKN-----LFRVGQSKVFFR 789
Cdd:cd01383 608 LLPED-----VSASQ-DPLSTSVAILQQFnilpeMYQVGYTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
109-789 |
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: 629.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 188 GESGAGKTENTKKVIQYLAHVASshKGGTLGRKkeavqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 267
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGG--RAVTEGRS-------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 268 GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDS 346
Cdd:cd01384 152 GRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNqSKCFELDGVDDAEEYRATRRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 347 MAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKL---CHLLGVNVLEFTRAILTPRIKVGREYVQ 423
Cdd:cd01384 232 MDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDALCKRVIVTPDGIIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 424 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 503
Cdd:cd01384 312 KPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 504 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQP 583
Cdd:cd01384 391 HVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPKLS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 584 RgeADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRivgldqvsSGESSApvtfgaaglkT 663
Cdd:cd01384 468 R--TDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR--------EGTSSS----------S 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 664 KkgmFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 743
Cdd:cd01384 528 K---FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1988774931 744 QRYEILTPNAIPRTFmDGKQASELMISALELDKnlFRVGQSKVFFR 789
Cdd:cd01384 605 DRFGLLAPEVLKGSD-DEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
109-789 |
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: 628.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVASSHKggtlgrkkeavqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS-------------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd01381 148 VIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTqGNCLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 348 AIMGFTPEELMSMLKVISAVLQFGNISFMK--EKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKA 425
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 426 QTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAS--FIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 503
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 504 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQ 582
Cdd:cd01381 388 HIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 583 pRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFvselwkeVDRIVGLDQVSSGESSApvtfgaaglK 662
Cdd:cd01381 464 -DLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKF-------LKQLFNEDISMGSETRK---------K 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 663 TKkgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEF 742
Cdd:cd01381 527 SP-----TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEF 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1988774931 743 RQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd01381 602 VERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
109-789 |
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: 579.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVASSHKGgtlgrkkeavqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLllGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd14872 148 RICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGW--GSSAAYGYLSlSGCIEVEGVDDVADFEEVVLAM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 348 AIMGFTPEELMSMLKVISAVLQFGNISF---MKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKV-GREYVQ 423
Cdd:cd14872 226 EQLGFDDADINNVMSLIAAILKLGNIEFasgGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 424 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 503
Cdd:cd14872 306 IPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 504 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQP 583
Cdd:cd14872 386 YTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 584 RGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivgldqvssgessaPVTFGAAglKT 663
Cdd:cd14872 463 TSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF-------------------PPSEGDQ--KT 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 664 KKGmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 743
Cdd:cd14872 522 SKV---TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFL 598
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1988774931 744 QRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14872 599 KRYRFLVKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
109-789 |
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: 572.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 188 GESGAGKTENTKKVIQYLAHVasshkGGTLGrkkeavqGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 267
Cdd:cd01382 81 GESGAGKTESTKYILRYLTES-----WGSGA-------GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 268 GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGtadqyrflsggsipvPGQSDSENFTQTMDSM 347
Cdd:cd01382 149 SSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKD---------------PLLDDVGDFIRMDKAM 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 348 AIMGFTPEELMSMLKVISAVLQFGNISFmkEKNHDQA---SMPDNTAAQKL---CHLLGVNVLEF-----TRAILTPRIK 416
Cdd:cd01382 214 KKIGLSDEEKLDIFRVVAAVLHLGNIEF--EENGSDSgggCNVKPKSEQSLeyaAELLGLDQDELrvsltTRVMQTTRGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 417 VGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRrqRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 496
Cdd:cd01382 292 AKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPF--ETSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 497 LQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPRATDRSFVEKLSGEQGSH-- 574
Cdd:cd01382 370 LQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHfr 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 575 ---PKFFKSKQPRGEAD---FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKevdrivglDQVSSG 648
Cdd:cd01382 447 lsiPRKSKLKIHRNLRDdegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFE--------SSTNNN 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 649 ESSAPvtfgaaglKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRI 728
Cdd:cd01382 519 KDSKQ--------KAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDL 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774931 729 CRQGFPNRIPFQEFRQRYEILTPNAI----PRTFmdgkqaSELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd01382 591 MQGGFPSRTSFHDLYNMYKKYLPPKLarldPRLF------CKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
109-789 |
1.57e-180 |
|
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: 563.24 E-value: 1.57e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQ----DREDQS 183
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 184 ILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQ------GELERQLLQANPILEAFGNAKTVKNDNSSRFG 257
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 258 KFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDS 337
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 338 ENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFmkEKNHDQASMPDNTAAQKLCH---LLGVNVLEFTRAILTPR 414
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDF--ESENDTTVLEDATTLQSLKLaaeLLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 415 IKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQgASFIGILDIAGFEIFQLNSFEQLCINYTN 494
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 495 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPRAT--DRSFVEKL---- 567
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLhasf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 568 ---------SGEQGSHPKFFkskQPRGEAD--FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDhfvselwkev 636
Cdd:cd14890 476 grksgsggtRRGSSQHPHFV---HPKFDADkqFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRR---------- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 637 drivGLDQVSsgessapvtfgaaglktkkgmfrtVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQ 716
Cdd:cd14890 543 ----SIREVS------------------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQ 594
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774931 717 LRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPNAiprtfMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14890 595 LKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
109-789 |
1.58e-176 |
|
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: 552.44 E-value: 1.58e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVAsshkggtlgRKKEAVQGElerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvAG 268
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN---------QRRNNLVTE---QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd01387 148 VIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNqGGNCEIAGKSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 348 AIMGFTPEELMSMLKVISAVLQFGNISFMK---EKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQK 424
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNVYFHKrqlRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 425 AQTKEQADFAVEALAKATYERLFRWLVHRINrALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 504
Cdd:cd01387 308 PLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKH 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 505 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKskqPR 584
Cdd:cd01387 387 VFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSK---PR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 585 -GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKevdrivgldQVSSGESSAPVTFGAAGLKT 663
Cdd:cd01387 461 mPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFS---------SHRAQTDKAPPRLGKGRFVT 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 664 KKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 743
Cdd:cd01387 532 MKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFI 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1988774931 744 QRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd01387 612 DRYRCLVALKLPRPAPGDMCVSLLSRLCTVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
109-789 |
2.14e-175 |
|
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: 550.44 E-value: 2.14e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLahVASSHKGGTLGrkkeavqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKGYGSG---------VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd01385 150 MVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFERLKQAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 348 AIMGFTPEELMSMLKVISAVLQFGNISFMKEK-NHDQASMPDNTAAQKL-CHLLGVNVLEFTRAILTPRIKVGREYVQKA 425
Cdd:cd01385 230 EMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVGETLILP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 426 QTKEQADFAVEALAKATYERLFRWLVHRINRAL----DRRQRQGASfIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 501
Cdd:cd01385 310 YKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 502 NHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPkfFKSK 581
Cdd:cd01385 389 NQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNK--YYEK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 582 QPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELwkevdriVGLDQV---------------- 645
Cdd:cd01385 464 PQVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVavfrwavlrafframa 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 646 ---------------SSGESSAPVTFGAAGL-KTKKGMfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLS 709
Cdd:cd01385 537 afreagrrraqrtagHSLTLHDRTTKSLLHLhKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFD 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 710 PHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMisalELDKNLFRVGQSKVFFR 789
Cdd:cd01385 615 DELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKL----NLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
109-789 |
1.57e-173 |
|
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: 544.35 E-value: 1.57e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEM---PPHIYAISEAAYRSMLQDR----ED 181
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 182 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 261
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 262 INFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGS-IPVPGQSDSENF 340
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 341 TQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFmkEKNHDQ----ASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIK 416
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 417 VGR-EYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQ---------GASFIGILDIAGFEIFQLNSFE 486
Cdd:cd14892 319 TARgSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 487 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPR-ATDRSFVE 565
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKRkTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 566 KLSGEQGSHPKFFksKQPRGEAD-FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDhfvselwkevdrivgldq 644
Cdd:cd14892 476 IYHQTHLDKHPHY--AKPRFECDeFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 645 vssgessapvtfgaaglktkkgmFRTvgqlykeSLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLE 724
Cdd:cd14892 536 -----------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLE 585
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774931 725 GIRICRQGFPNRIPFQEFRQRYEILTPN-AIPRTFMDGKQASELM-----ISALELDKNLFRVGQSKVFFR 789
Cdd:cd14892 586 VVRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
109-787 |
2.54e-172 |
|
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: 540.92 E-value: 2.54e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMY------RGKKRHEMPPHIYAISEAAYRSMLQDRE-- 180
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 181 --DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQgeleRQLLQANPILEAFGNAKTVKNDNSSRFGK 258
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVR----DRVLESNPILEAFGNARTNRNNNSSRFGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 259 FIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFL--SGGSIPVPGQSD 336
Cdd:cd14901 157 FIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 337 SENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFM-KEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRI 415
Cdd:cd14901 237 SVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVkKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 416 KVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAS-FIGILDIAGFEIFQLNSFEQLCINYTN 494
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 495 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSH 574
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 575 PKFFKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSElwkevdrivgldqvssgessapv 654
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 655 tfgaaglktkkgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFP 734
Cdd:cd14901 531 ---------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYP 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774931 735 NRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNL-----FRVGQSKVF 787
Cdd:cd14901 596 VRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIehlppFQVGKTKVF 653
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
109-789 |
9.21e-171 |
|
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: 536.67 E-value: 9.21e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 188 GESGAGKTENTKKVIQYLAHVASSHKGGTLgrkkeavqgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 267
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLNDSTI------------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 268 GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRadLLLGTADQYRFL-SGGSIPVPGQSDSENFTQTMDS 346
Cdd:cd14903 149 GTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEER--LFLDSANECAYTgANKTIKIEGMSDRKHFARTKEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 347 MAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASM--PDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQK 424
Cdd:cd14903 227 LSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 425 AQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 504
Cdd:cd14903 307 PLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 505 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPRATDRSFVEKLSG---EQGSHPKFfksk 581
Cdd:cd14903 386 VFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLSSihkDEQDVIEF---- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 582 qPR-GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSSGESSAPVTFGAAG 660
Cdd:cd14903 458 -PRtSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 661 LKtkkgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 740
Cdd:cd14903 537 TT-------TVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHE 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1988774931 741 EFRQRYEILTPNAiPRTFMDGKQASELMISALELDK-NLFRVGQSKVFFR 789
Cdd:cd14903 610 EFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
110-789 |
9.40e-171 |
|
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: 535.70 E-value: 9.40e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 190 SGAGKTENTKKVIQYLAHvasshkggtLGRkkeAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 269
Cdd:cd01379 82 SGAGKTESANLLVQQLTV---------LGK---ANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 270 IVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETR-ADLLLGTADQYRFLSGGSIPVPG----QSDSENFTQTM 344
Cdd:cd01379 150 VTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDivnnSGNREKFEEIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 345 DSMAIMGFTPEELMSMLKVISAVLQFGNISF----MKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAiLTPRIKVGR- 419
Cdd:cd01379 230 QCFKVIGFTKEEVDSVYSILAAILHIGDIEFteveSNHQTDKSSRISNPEALNNVAKLLGIEADELQEA-LTSHSVVTRg 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 420 EYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL--DRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKL 497
Cdd:cd01379 309 ETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 498 QQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPRATDRSFVEKLsgEQGSHPK 576
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKF--HNNIKSK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 577 FFkSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSElwkevdrivgldqvssgessapvtf 656
Cdd:cd01379 463 YY-WRPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 657 gaaglktkkgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNR 736
Cdd:cd01379 517 -------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHR 583
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1988774931 737 IPFQEFRQRYEILTPNAIPRTFMDgKQASELMISALELDKnlFRVGQSKVFFR 789
Cdd:cd01379 584 ILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
109-789 |
2.40e-170 |
|
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: 534.65 E-value: 2.40e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKK-RHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 188 GESGAGKTENTKKVIQYLAHVASShkggtlgrkkeaVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 267
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS------------DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTEN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 268 GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSEN-------F 340
Cdd:cd14897 149 GQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDSEEleyyrqmF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 341 TQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGRE 420
Cdd:cd14897 229 HDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 421 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL----DRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 496
Cdd:cd14897 309 RIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNER 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 497 LQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPK 576
Cdd:cd14897 389 LQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 577 FfkSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKevdrivgldqvssgessapvtf 656
Cdd:cd14897 466 Y--VASPGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT---------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 657 gaaglktkkgmfrtvgQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNR 736
Cdd:cd14897 522 ----------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIR 585
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1988774931 737 IPFQEFRQRYEILTPNaiPRTFMDGKQASELMISALELDKNlFRVGQSKVFFR 789
Cdd:cd14897 586 IKYEDFVKRYKEICDF--SNKVRSDDLGKCQKILKTAGIKG-YQFGKTKVFLK 635
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
109-789 |
4.81e-167 |
|
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: 526.29 E-value: 4.81e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 188 GESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVqgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 267
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCV----EQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 268 GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDS 346
Cdd:cd14873 157 GNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 347 MAIMGFTPEELMSMLKVISAVLQFGNISFMkekNHDQASMPDNTAAQKLCHLLGVNVLEFTRAiLTPRIKVGR-EYVQKA 425
Cdd:cd14873 237 MEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQRSMFLRgEEILTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 426 QTKEQADFAVEALAKATYERLFRWLVHRINRALdrRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 505
Cdd:cd14873 313 LNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 506 FILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKskqPR- 584
Cdd:cd14873 391 FSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVK---PRv 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 585 GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDrivgldqvSSGESSAPVTfgaaGLKTK 664
Cdd:cd14873 464 AVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVS--------SRNNQDTLKC----GSKHR 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 665 KgmfRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 744
Cdd:cd14873 532 R---PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYK 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1988774931 745 RYEILTPNAIPRTFMDGKQASelMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14873 609 RYKVLMRNLALPEDVRGKCTS--LLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
109-751 |
1.39e-163 |
|
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: 517.71 E-value: 1.39e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRgKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 188 GESGAGKTENTKKVIQYLAHVASSHKggtlgRKKEAVqgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-- 265
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDI-----KKRSLV----EAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSkl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 266 -------VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLlCGASEETR-ADLLLGTADQYRFLSGGSIPV------ 331
Cdd:cd14888 151 kskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQL-CAAAREAKnTGLSYEENDEKLAKGADAKPIsidmss 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 332 ------------------PGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQ 393
Cdd:cd14888 230 fephlkfryltksschelPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 394 KL---CHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIG 470
Cdd:cd14888 310 DLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 471 ILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLD 550
Cdd:cd14888 390 VLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 551 EECWFPRATDRSFVEKLSGEQGSHPKF--FKSKQprgeADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHF 628
Cdd:cd14888 467 EECFVPGGKDQGLCNKLCQKHKGHKRFdvVKTDP----NSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPF 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 629 VSELWKE-VDRIVgldqvssgessapvtfgaaGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGK 707
Cdd:cd14888 543 ISNLFSAyLRRGT-------------------DGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDL 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1988774931 708 LSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTP 751
Cdd:cd14888 604 FDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
109-789 |
1.51e-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: 473.36 E-value: 1.51e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRH--------EMPPHIYAISEAAYRSMLQDR 179
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 180 EDQSILCTGESGAGKTENTKKVIQYL----AHVASSHKGGTLGRKKEA---VQGELERQLLQANPILEAFGNAKTVKNDN 252
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLtqlsQQEQNSEEVLTLTSSIRAtskSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 253 SSRFGKFIRINFD-VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLL---GTADQYRFLS-GG 327
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLknqLSGDRYDYLKkSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 328 SIPVPGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEK-NHDQASMPDNTAA-QKLCHLLGVNVLE 405
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTlDDNSPCCVKNKETlQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 406 FTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL------DRRQRQGASF-IGILDIAGFE 478
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYLsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 479 IFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFP 556
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 557 RATDRSFVEKLSGEQGSHPKFFKSKQPRGEAdFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkev 636
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF--- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 637 driVGLDQVSSGESSAPVtfgaaglKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQ 716
Cdd:cd14907 554 ---SGEDGSQQQNQSKQK-------KSQKKD-KFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQ 622
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774931 717 LRCNGVLEGIRICRQGFPNRIPFQEFRQRYEiltpnaiprtfmdgkqaselmisalELDKNLFrVGQSKVFFR 789
Cdd:cd14907 623 IRYLGVLESIRVRKQGYPYRKSYEDFYKQYS-------------------------LLKKNVL-FGKTKIFMK 669
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
110-756 |
3.91e-147 |
|
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: 470.56 E-value: 3.91e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMY-----------RGKKRHEMPPHIYAISEAAYRSM-- 175
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 176 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQgeLERQLLQANPILEAFGNAKTVKNDNS 253
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSG--IAAKVLQTNILLESFGNARTLRNDNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 254 SRFGKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRAdlllgtadqyrflsggsipvpg 333
Cdd:cd14900 160 SRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK---------------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 334 qsdSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISF-MKEKNHDQASMPDNTAAQKL------CHLLGVNVLEF 406
Cdd:cd14900 218 ---RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFeHDENSDRLGQLKSDLAPSSIwsrdaaATLLSVDATKL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 407 TRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL---DRRQRQGAS-FIGILDIAGFEIFQL 482
Cdd:cd14900 295 EKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVFPK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 483 NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATDRS 562
Cdd:cd14900 375 NSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSDTT 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 563 FVEKLSGEQGSHPKFFKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDplndnvasLLHQSSdhfvselwkeVDrivgl 642
Cdd:cd14900 452 LASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------VD----- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 643 dqvssgessapvtfgaaglktkkgMFRTVGQlYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGV 722
Cdd:cd14900 509 ------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGV 563
|
650 660 670
....*....|....*....|....*....|....
gi 1988774931 723 LEGIRICRQGFPNRIPFQEFRQRYEILTPNAIPR 756
Cdd:cd14900 564 MEAVRVARAGFPIRLLHDEFVARYFSLARAKNRL 597
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
111-789 |
2.13e-145 |
|
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: 467.08 E-value: 2.13e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 111 VLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSML----QDREDQSILC 186
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 187 TGESGAGKTENTKKVIQYLAHVAsshKGGTlgrkkeavqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDv 266
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---RGNS----------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 267 AGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSipvpGQSDS-----ENFT 341
Cdd:cd14889 149 NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGA----GCKREvqywkKKYD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 342 QTMDSMAIMGFTPEELMSMLKVISAVLQFGNISF-MKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAiLTPRIKVGR- 419
Cdd:cd14889 225 EVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFeMDDDEALKVENDSNGWLKAAAGQFGVSEEDLLKT-LTCTVTFTRg 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 420 EYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQG--ASFIGILDIAGFEIFQLNSFEQLCINYTNEKL 497
Cdd:cd14889 304 EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 498 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIerPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKF 577
Cdd:cd14889 384 QYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 578 FKSKqpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEvdRIVGLDQVSSGESSAPVTFG 657
Cdd:cd14889 461 GKSR--SKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTA--TRSRTGTLMPRAKLPQAGSD 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 658 AAGLKTKKgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRI 737
Cdd:cd14889 537 NFNSTRKQ----SVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRP 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1988774931 738 PFQEFRQRYEIL--TPNaIPRTfmdgKQASELMISALELDKnlFRVGQSKVFFR 789
Cdd:cd14889 613 SFAEFAERYKILlcEPA-LPGT----KQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
109-789 |
1.80e-139 |
|
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: 451.28 E-value: 1.80e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYR--GKKRHE-------MPPHIYAISEAAYRSMLQD- 178
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 179 REDQSILCTGESGAGKTENTKKVIQYLAHVASShKGGTLGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGK 258
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNG-EEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 259 FIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRA-----DLLLGT---ADQYRFLSGGSIP 330
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyefhDGITGGlqlPNEFHYTGQGGAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 331 VPGQ-SDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNTAAQK----LCHLLGVNVLE 405
Cdd:cd14908 240 DLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEF-ESKEEDGAAEIAEEGNEKclarVAKLLGVDVDK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 406 FTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL--DRRQRQGASfIGILDIAGFEIFQLN 483
Cdd:cd14908 319 LLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFECFAHN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 484 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP-RATDRS 562
Cdd:cd14908 398 SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGSDAN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 563 FVEKL--------SGEQGSHPKFFKSKQPRGEADFSIIHYAGKVDYKA-NDWLVKNMDPLNdnvasllhqssdhfvselw 633
Cdd:cd14908 475 YASRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIP------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 634 kevdrivgldqvssgessapvtfgaaglKTKKGMFRTvGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLV 713
Cdd:cd14908 536 ----------------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRV 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 714 LDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPnAIPRT----FMDGKQASEL-----------------MISAL 772
Cdd:cd14908 587 TEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVvlswSMERLDPQKLcvkkmckdlvkgvlspaMVSMK 665
|
730
....*....|....*..
gi 1988774931 773 ELDKNLFRVGQSKVFFR 789
Cdd:cd14908 666 NIPEDTMQLGKSKVFMR 682
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
109-789 |
1.58e-137 |
|
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: 444.77 E-value: 1.58e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 188 GESGAGKTENTKKVIQYLAHVASSHKGGTLGRkkeavqgelerqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 267
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTIAK------------VIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 268 GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGG--SIPVPGQSDSENFTQTMD 345
Cdd:cd14904 149 GKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSlaQMQIPGLDDAKLFASTQK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 346 SMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMpDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKA 425
Cdd:cd14904 229 SLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRIS-NGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 426 QTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 505
Cdd:cd14904 308 LAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 506 FILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPRATDRSFVEKL---SGEQGSHP--KFFKS 580
Cdd:cd14904 388 FKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNEsiDFPKV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 581 KQPRgeadFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivgldqvSSGESSAPVTFGAAG 660
Cdd:cd14904 464 KRTQ----FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF------------GSSEAPSETKEGKSG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 661 LKTKKGmfRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 740
Cdd:cd14904 528 KGTKAP--KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPK 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1988774931 741 EFRQRYEILTPNAIPRTfmDGKQASELMISALELDKNL-FRVGQSKVFFR 789
Cdd:cd14904 606 ELATRYAIMFPPSMHSK--DVRRTCSVFMTAIGRKSPLeYQIGKSLIYFK 653
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
109-789 |
1.38e-135 |
|
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: 439.09 E-value: 1.38e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERyySGLI----YTYSGLFCVVVNPYKNLPiytESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDRE---D 181
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 182 QSILCTGESGAGKTENTKKVIQYLAH--VASSHKGGT----LGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSR 255
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTraVGGKKASGQdieqSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 256 FGKFIRINFDVAGY-IVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPG 333
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 334 QSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEK----NHDQASMPDNTAAQKLCHLLGVNVLEFTRA 409
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDtsegEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 410 ILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrRQRQGASFIGILDIAGFEIFQL-NSFEQL 488
Cdd:cd14891 316 ITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLG-HDPDPLPYIGVLDIFGFESFETkNDFEQL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 489 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATDRSFVEKLS 568
Cdd:cd14891 395 LINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNETLH 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 569 GEQGSHPKFFKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSsdhfvselwkevdrivgldqvssg 648
Cdd:cd14891 472 KTHKRHPCFPRPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS------------------------ 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 649 essapvtfgaaglktkkgmfrtvgQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRI 728
Cdd:cd14891 528 ------------------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEV 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 729 CRQGFPNRIPFQEFRQRYEILTPNAIPRTFMDGKQA-SELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14891 584 LKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
110-789 |
1.19e-133 |
|
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: 435.92 E-value: 1.19e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPiytesivEMYRGKKRHE-------MPPHIYAISEAAYRSMLQ----- 177
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 178 --DREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQGElerQLLQANPILEAFGNAKTVKNDNSSR 255
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISGS---ELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 256 FGKFIRINF-----DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEE--TRADLLLGTADQYRFLSGGS 328
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmkLELQLELLSAQEFQYISGGQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 329 IPV--PGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHD---------------QASMPDNTA 391
Cdd:cd14895 232 CYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 392 AQKL---CHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ------ 462
Cdd:cd14895 312 QQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpn 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 463 ----RQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIEr 538
Cdd:cd14895 392 kaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 539 pANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVA 618
Cdd:cd14895 470 -QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELF 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 619 SLLHQSSDHFVSELWKEVDRIVgldqvssgesSAPVTFGAAGLKTKKGMFRTV--GQLYKESLTKLMATLRNTNPNFLRC 696
Cdd:cd14895 549 SVLGKTSDAHLRELFEFFKASE----------SAELSLGQPKLRRRSSVLSSVgiGSQFKQQLASLLDVVQQTQTHYIRC 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 697 IIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELdk 776
Cdd:cd14895 619 IKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL-- 696
|
730
....*....|...
gi 1988774931 777 nlfrvGQSKVFFR 789
Cdd:cd14895 697 -----GKTRVFLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
109-789 |
1.79e-133 |
|
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: 433.05 E-value: 1.79e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAhvasshkggTLGRKKEAVQGeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvAG 268
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLS---------SLYQDQTEDRL---RQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd14896 148 VIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNqGGACRLQGKEDAQDFEGLLKAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 348 AIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQ--ASMPDNTAAQKLCHLLGVNVlEFTRAILTPRIKV---GReyV 422
Cdd:cd14896 228 QGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPP-ERLEGAVTHRVTEtpyGR--V 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 423 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALD-RRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 501
Cdd:cd14896 305 SRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLApPGEAESDATIGVVDAYGFEALRVNGLEQLCINLASERLQLFS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 502 NHTMFILEQEEYQREGIEWNFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSK 581
Cdd:cd14896 385 SQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQ 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 582 QPRgeADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQvssgessapvtfGAAGL 661
Cdd:cd14896 462 LPL--PVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQ------------GKPTL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 662 KTKkgmfrtvgqlYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 741
Cdd:cd14896 528 ASR----------FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQA 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1988774931 742 FRQRYEILTPNAIPrTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14896 598 FLARFGALGSERQE-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
99-800 |
4.86e-129 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 426.75 E-value: 4.86e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 99 DMADLTCLNEASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHE-MPPHIYAISEAAYRSMLQ 177
Cdd:PTZ00014 100 DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 178 DREDQSILCTGESGAGKTENTKKVIQYLAhvasSHKGGTLGRKkeavqgeLERQLLQANPILEAFGNAKTVKNDNSSRFG 257
Cdd:PTZ00014 180 VKKSQTIIVSGESGAGKTEATKQIMRYFA----SSKSGNMDLK-------IQNAIMAANPVLEAFGNAKTIRNNNSSRFG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 258 KFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDS 337
Cdd:PTZ00014 249 RFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 338 ENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFM-KEKN-HDQASM--PDNTAA-QKLCHLLGVNVLEFTRAILT 412
Cdd:PTZ00014 329 KDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEgKEEGgLTDAAAisDESLEVfNEACELLFLDYESLKKELTV 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 413 PRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAsFIGILDIAGFEIFQLNSFEQLCINY 492
Cdd:PTZ00014 409 KVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINI 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 493 TNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPRATDRSFVEKLSGEQG 572
Cdd:PTZ00014 488 TNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLK 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 573 SHPKFFKSKQpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdrivgldQVSSGessa 652
Cdd:PTZ00014 565 NNPKYKPAKV-DSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGV-------EVEKG---- 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 653 pvtfgaaglKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQG 732
Cdd:PTZ00014 633 ---------KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLG 701
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774931 733 FPNRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR---AGVLAHLEEER 800
Cdd:PTZ00014 702 FSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREK 772
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
109-751 |
1.14e-127 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 419.30 E-value: 1.14e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYR--------GKKRHEMPPHIYAISEAAYRSMLQ-D 178
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 179 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHkggTLGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGK 258
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQ---SSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 259 FIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFL-----SGGSIPVPG 333
Cdd:cd14902 158 FIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLnsygpSFARKRAVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 334 QSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDqasmpDNTAAQKLC--------HLLGVNVLE 405
Cdd:cd14902 238 DKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQE-----DATAVTAASrfhlakcaELMGVDVDK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 406 FTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALD--------RRQRQGASFIGILDIAGF 477
Cdd:cd14902 313 LETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 478 EIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPR 557
Cdd:cd14902 393 ESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 558 ATDRSFVEklsgeqgshpKFFKSKQPRGEadFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELwkevd 637
Cdd:cd14902 470 GSNQALST----------KFYRYHGGLGQ--FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAI----- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 638 rivGLDqvssGESSAPVTFGAAGLKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLD 715
Cdd:cd14902 533 ---GAD----ENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVE 605
|
650 660 670
....*....|....*....|....*....|....*.
gi 1988774931 716 QLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTP 751
Cdd:cd14902 606 QMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
109-789 |
1.48e-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: 412.47 E-value: 1.48e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAvqgelerqllqANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNA-----------ALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLG--TADQYRFLSGGSIPVPGQSDSENFTQTMDS 346
Cdd:cd01386 150 QLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNqlAESNSFGIVPLQKPEDKQKAAAAFSKLQAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 347 MAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAI------------LTPR 414
Cdd:cd01386 230 MKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 415 IKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASfIGILDIAGfeiFQLN---------SF 485
Cdd:cd01386 310 GQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPG---FQNPahsgsqrgaTF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 486 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERP---ANPP---------GVLALLDEEC 553
Cdd:cd01386 386 EDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLLDEEA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 554 WFPRATDRSFVEKLS---GEQGS---HPKFFKSKQPRgeaDFSIIHYAGK--VDYKANDWLVK-NMDPLNDNVASLLHQS 624
Cdd:cd01386 466 LYPGSSDDTFLERLFshyGDKEGgkgHSLLRRSEGPL---QFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQES 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 625 SDHFvselwkevdrivgldqvssgessapvtfgaAGLKtKKGMFRTVgqlyKESLTKLMATLRNTNPNFLRCIIPNHE-- 702
Cdd:cd01386 543 QKET------------------------------AAVK-RKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHNag 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 703 ----KRAGKLSPHLVLD------QLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTP-----NAIPRTFMDGKQASEL 767
Cdd:cd01386 588 kderSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkkLGLNSEVADERKAVEE 667
|
730 740
....*....|....*....|..
gi 1988774931 768 MISALELDKNLFRVGQSKVFFR 789
Cdd:cd01386 668 LLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
109-787 |
3.35e-124 |
|
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: 407.07 E-value: 3.35e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRH-EMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 188 GESGAGKTENTKKVIQYLAhvaSSHKGGTLGRKKEAVqgelerqlLQANPILEAFGNAKTVKNDNSSRFGKFIRInfDVA 267
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRIQTAI--------MAANPVLEAFGNAKTIRNNNSSRFGRFMQL--DVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 268 --GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTMD 345
Cdd:cd14876 148 seGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 346 SMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKnhdQASMPDntAA----------QKLCHLLGVNVLEFTRAILTPRI 415
Cdd:cd14876 228 SLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKT---EQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 416 KVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAsFIGILDIAGFEIFQLNSFEQLCINYTNE 495
Cdd:cd14876 303 KAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINITNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 496 KLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPRATDRSFVEKLSGEQGSHP 575
Cdd:cd14876 382 MLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 576 KFFKSKQpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdrivgldqvssgessaPVT 655
Cdd:cd14876 459 KFKPAKV-DSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGV----------------VVE 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 656 FGaaglKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPN 735
Cdd:cd14876 522 KG----KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSY 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 736 RIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVF 787
Cdd:cd14876 596 RRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
109-787 |
6.16e-123 |
|
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: 405.90 E-value: 6.16e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKR-HEMPPHIYAISEAAYRSMLQDREDQSILC 186
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 187 TGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEavQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 266
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNNNNN--NNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 267 AGYIV-GANIETYLLEKSRAT-RQAKDERTFHIFYQLLCGASEETRADLLLGT-ADQYRFL--------------SGGSI 329
Cdd:cd14906 159 SDGKIdGASIETYLLEKSRIShRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqsSNKNS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 330 PVPGQSDS-ENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQAS--MPDNTAA-QKLCHLLGVNVLE 405
Cdd:cd14906 239 NHNNKTESiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 406 FTRAILTPRIKVGREYVQKAQTKE--QADFAVEALAKATYERLFRWLVHRINRALDR----RQRQGAS------FIGILD 473
Cdd:cd14906 319 FKQALLNRNLKAGGRGSVYCRPMEvaQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsNDLAGGSnkknnlFIGVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 474 IAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEEC 553
Cdd:cd14906 399 IFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDEC 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 554 WFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEadFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELW 633
Cdd:cd14906 476 IMPKGSEQSLLEKYNKQYHNTNQYYQRTLAKGT--LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 634 kevdrivgldqvSSGESSAPVTfgaaglKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLV 713
Cdd:cd14906 554 ------------QQQITSTTNT------TKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHV 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 714 LDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALEL------------------- 774
Cdd:cd14906 616 LSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSklktmgisnnkkknnsnsn 695
|
730
....*....|....*...
gi 1988774931 775 -----DKNLFRVGQSKVF 787
Cdd:cd14906 696 snttnDKPLFQIGKTKIF 713
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
109-751 |
4.48e-121 |
|
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: 398.45 E-value: 4.48e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKR-HEMPPHIYAISEAAYRSMLQDRE--DQSI 184
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 185 LCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEavqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 264
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAE----RIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 265 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLsggsiPVPGQS-DSENFTQT 343
Cdd:cd14880 157 NRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL-----PNPERNlEEDCFEVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 344 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTA---AQKLCHLLGVNVLEFTRAILTPRIKVGRE 420
Cdd:cd14880 232 REAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRAGKQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 421 YV--QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 498
Cdd:cd14880 312 QQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 499 QLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATD----RSFVEK-LSGEQG- 572
Cdd:cd14880 392 QHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSaaqlQTRIESaLAGNPCl 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 573 SHPKFfkSKQPrgeaDFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVsSGESSA 652
Cdd:cd14880 469 GHNKL--SREP----SFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEP-SGQSRA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 653 PVTfgaaglktkkgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQG 732
Cdd:cd14880 542 PVL--------------TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAG 607
|
650
....*....|....*....
gi 1988774931 733 FPNRIPFQEFRQRYEILTP 751
Cdd:cd14880 608 FPIRVSHQNFVERYKLLRR 626
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
109-789 |
2.24e-117 |
|
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: 388.01 E-value: 2.24e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYS-GLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRG-KKRHEMPPHIYAISEAAYRSM-LQDREDQSIL 185
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 186 CTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKkeaVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 265
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRS---IADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 266 -VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADL-LLGTADQYRFLSGGSI----PVPGQ--SDS 337
Cdd:cd14875 158 pTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDGKtlDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 338 ENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILtprIKV 417
Cdd:cd14875 238 HEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEF-ESDQNDKAQIADETPFLTACRLLQLDPAKLRECFL---VKS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 418 GREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQR-QGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 496
Cdd:cd14875 314 KTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDcSGCKYIGLLDIFGFENFTRNSFEQLCINYANES 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 497 LQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPK 576
Cdd:cd14875 394 LQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 577 FF---KSKQPRgeaDFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELwkevdrivgldqvssgessap 653
Cdd:cd14875 471 YFvlpKSTIPN---QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL--------------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 654 vtfgaagLKTKKGMFR---TVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICR 730
Cdd:cd14875 527 -------LSTEKGLARrkqTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKR 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774931 731 QGFPNRIPFQEFRQRYEILTPNAIPRTFMDGKqASELMISALELDKNLFR-------VGQSKVFFR 789
Cdd:cd14875 600 QGYPVRRPIEQFCRYFYLIMPRSTASLFKQEK-YSEAAKDFLAYYQRLYGwakpnyaVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
109-789 |
2.95e-113 |
|
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: 375.76 E-value: 2.95e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRH-----EMPPHIYAISEAAYRSMLQDREDQ 182
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 183 SILCTGESGAGKTENTKKVIQYLAHVASSHkggtlgrkkeavQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 262
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTS------------STDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 263 NFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSI-PVPGQSDSENFT 341
Cdd:cd14886 149 LVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGIDDQKEFA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 342 QTMDSMAIMgFTPEELMSMLKVISAVLQFGNISFMKEKNH---DQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVG 418
Cdd:cd14886 229 PVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMgviNAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVIN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 419 REYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALdRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 498
Cdd:cd14886 308 NETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 499 QLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPRATDRSFVEKLSgeqgSHPK-- 576
Cdd:cd14886 387 QYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSSCK----SKIKnn 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 577 -FFKSKQprGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLdqvssgessapvt 655
Cdd:cd14886 460 sFIPGKG--SQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 656 fgaaglktKKGMFrtVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPN 735
Cdd:cd14886 525 --------MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAY 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774931 736 RIPFQEFRQRYEILT--PNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14886 595 NDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
109-746 |
1.96e-106 |
|
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: 358.25 E-value: 1.96e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMY----------RGKKRHEMPPHIYAISEAAYRSMLQ 177
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 178 DREDQSILCTGESGAGKTENTKKVIQYLAhvASSHKGGTLGRKKEAVQGE-------LERQLLQANPILEAFGNAKTVKN 250
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFA--VHCGTGNNNLTNSESISPPaspsrttIEEQVLQSNPILEAFGNARTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 251 DNSSRFGKFIRINF-DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLL-----CGASEETRADLLLGTADQYRFL 324
Cdd:cd14899 159 DNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLsadnnCVSKEQKQVLALSGGPQSFRLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 325 SGG--SIPVPGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISF--MKEKNHDQASMPDNTAAQ------- 393
Cdd:cd14899 239 NQSlcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqIPHKGDDTVFADEARVMSsttgafd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 394 ---KLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRR--------- 461
Cdd:cd14899 319 hftKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 462 -----QRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLI 536
Cdd:cd14899 399 sdvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 537 ERpaNPPGVLALLDEECWFPRATDRSFVEKLSGE---QGSHPKFFKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPL 613
Cdd:cd14899 478 EH--RPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 614 NDNVASLLHQSSDHFVSELWKEvdrivGLDQVSSGESSAPVTFGAAGLKTKKGMFR-TVGQLYKESLTKLMATLRNTNPN 692
Cdd:cd14899 556 CESAAQLLAGSSNPLIQALAAG-----SNDEDANGDSELDGFGGRTRRRAKSAIAAvSVGTQFKIQLNELLSTVRATTPR 630
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1988774931 693 FLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 746
Cdd:cd14899 631 YVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
109-789 |
1.21e-98 |
|
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: 335.85 E-value: 1.21e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYS--------GLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDRE 180
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 181 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGgtlgrkkeAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFI 260
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHG--------ADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKML 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 261 RINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFlsggsipvpgqsDSENF 340
Cdd:cd14887 153 LLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST------------DLRRI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 341 TQTMDSMAIMGFTPEELmsmLKVISAVLQFGNISFMKEKNHDQASMPDNTA--------AQKLCHLL------------- 399
Cdd:cd14887 221 TAAMKTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssglkvte 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 400 -----------------GVNVLEFTRAILTprIKVGREyVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDR-- 460
Cdd:cd14887 298 asrkhlktvarllglppGVEGEEMLRLALV--SRSVRE-TRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRsa 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 461 -----------RQRQGASFIGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI--D 524
Cdd:cd14887 375 kpsesdsdedtPSTTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsA 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 525 FGLDLQPCIDLIERPAN---------------------PPGVLALLDE------ECWFPRATDRSFVEKLSGEQGSHPKF 577
Cdd:cd14887 455 FPFSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSAKY 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 578 FKSKQ--PRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLhQSSDHFVSElwkevdriVGLDQVSsgessapvt 655
Cdd:cd14887 535 KNITPalSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRL--------VGSKKNS--------- 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 656 fgaaGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPN 735
Cdd:cd14887 597 ----GVRAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPC 672
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1988774931 736 RIPFQEFRQRYEILTPNAIpRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14887 673 RLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
110-753 |
6.31e-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: 328.78 E-value: 6.31e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNlpIYTESIVEMYRGKKRHeMPPHIYAISEAAYRSMLQdREDQSILCTGE 189
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 190 SGAGKTENTKKVIQYLAHvasshkgGTLGRKKeavqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvaGY 269
Cdd:cd14898 78 SGSGKTENAKLVIKYLVE-------RTASTTS------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 270 IVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLlgtadQYRFLSGGSIPVPgqSDSENFTQTMDSMAI 349
Cdd:cd14898 143 ITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI-----DTSSTAGNKESIV--QLSEKYKMTCSAMKS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 350 MGFTpeELMSMLKVISAVLQFGNISFMkekNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKE 429
Cdd:cd14898 216 LGIA--NFKSIEDCLLGILYLGSIQFV---NDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 430 QADFAVEALAKATYERLFRWLVHRINRALdrrQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILE 509
Cdd:cd14898 291 QARTIRNSMARLLYSNVFNYITASINNCL---EGSGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAK 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 510 QEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLsgeqgshpKFFKSKQPRGEADF 589
Cdd:cd14898 368 QGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI--------KKYLNGFINTKARD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 590 SII--HYAGKVDYKANDWLVKNMdplndnvasllhqssdhfvselwkevdrivgldqvssgESSAPVTFGAAGLKTkKGM 667
Cdd:cd14898 436 KIKvsHYAGDVEYDLRDFLDKNR--------------------------------------EKGQLLIFKNLLIND-EGS 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 668 FRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 747
Cdd:cd14898 477 KEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYR 556
|
....*.
gi 1988774931 748 ILTPNA 753
Cdd:cd14898 557 ILGITL 562
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
106-788 |
2.43e-96 |
|
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: 326.43 E-value: 2.43e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 106 LNEASVLHNLRERYYSGLIYTY---SGLfcVVVNPYKNLPIYTESIVEMYR-------GKKRHEMPPHIYAISEAAYRSM 175
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 176 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTlgrkkeavqgELERQLLQANPILEAFGNAKTVKNDNSSR 255
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGT----------KLSSQISAAEFVLDSFGNAKTLTNPNASR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 256 FGKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFL-SGGSIPV--- 331
Cdd:cd14879 149 FGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLaSYGCHPLplg 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 332 PGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFM--KEKNHDQASMpDNTAA-QKLCHLLGV--NVLEf 406
Cdd:cd14879 229 PGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTydHEGGEESAVV-KNTDVlDIVAAFLGVspEDLE- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 407 trAILTPRIK-VGRE----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEifQ 481
Cdd:cd14879 307 --TSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQ--N 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 482 L-----NSFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIERPanPPGVLALLDE 551
Cdd:cd14879 379 RsstggNSLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGK--PGGLLGILDD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 552 EC-WFPRATDRSFVEKLSGEQGSHPKF---FKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLndnvasllhqSSDh 627
Cdd:cd14879 451 QTrRMPKKTDEQMLEALRKRFGNHSSFiavGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVL----------SPD- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 628 FVSelwkevdrivgldqvssgessapvtfgaaglktkkgMFRTVGQLyKESLTKLMATLRNTNPNFLRCIIPNHEKRAGK 707
Cdd:cd14879 520 FVN------------------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNS 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 708 LSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPnaiprtFMDGKQASELMISALELDKNLFRVGQSKVF 787
Cdd:cd14879 563 FDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVF 636
|
.
gi 1988774931 788 F 788
Cdd:cd14879 637 L 637
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
109-789 |
2.18e-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: 314.65 E-value: 2.18e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLpiytESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHvasshkggtlGRKKEavqGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14937 77 ESGSGKTEASKLVIKYYLS----------GVKED---NEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTMDSMA 348
Cdd:cd14937 144 NIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 349 IMGftpeelMSMLK-----VISAVLQFGNISFM---KEKNHDQASMPDNT--AAQKLCHLLGVNVLEFTRAILTPRIKVG 418
Cdd:cd14937 224 KMN------MHDMKddlflTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 419 REYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 498
Cdd:cd14937 298 NQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLN-NNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIH 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 499 QLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFF 578
Cdd:cd14937 377 SIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 579 KSKQPRGEaDFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdrivgldQVSSgessapvTFGA 658
Cdd:cd14937 453 STKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDV-------EVSE-------SLGR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 659 AGLKTKKgmfrtvgqlYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRIcRQGFPNRIP 738
Cdd:cd14937 518 KNLITFK---------YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYT 587
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1988774931 739 FQEFRQRYEILTPNAIPRTFMDGKQASELMISAlELDKNLFRVGQSKVFFR 789
Cdd:cd14937 588 FDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
109-749 |
2.84e-92 |
|
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: 314.83 E-value: 2.84e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYR---GKKRHEMPPHIYAISEAAYRSMLQDREDQSIL 185
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 186 CTGESGAGKTENTKKVIQYLAHVASSHKGgtlgrkkeavqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF- 264
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT------------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFc 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 265 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGG----SIPVPGQSDSENF 340
Cdd:cd14878 149 ERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmredVSTAERSLNREKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 341 TQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGRE 420
Cdd:cd14878 229 AVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 421 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAS---FIGILDIAGFEIFQLNSFEQLCINYTNEKL 497
Cdd:cd14878 309 MIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtlDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 498 QQLFNHTMFILEQEEYQREGIewnfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECWFPRATDRSFVEK 566
Cdd:cd14878 389 HHYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVEPNLPKK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 567 LSG---EQGSHPKFFKSKQPRGE-------ADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEv 636
Cdd:cd14878 456 LQSlleSSNTNAVYSPMKDGNGNvalkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 637 drivgldqvssgessapvtfgaaglktkkgMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQ 716
Cdd:cd14878 535 ------------------------------KLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQ 584
|
650 660 670
....*....|....*....|....*....|...
gi 1988774931 717 LRCNGVLEGIRICRQGFPNRIPFQEFRQRYEIL 749
Cdd:cd14878 585 LQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL 617
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
109-741 |
3.41e-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: 3.41e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHE-------MPPHIYAISEAAYRSMLQDRE 180
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 181 DQSILCTGESGAGKTENTKKVIQYLAHVASshkggtlgrkkEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFI 260
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQT-----------DSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRIN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 261 RINFD---------VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRAD-----------LLLGTADQ 320
Cdd:cd14884 150 LLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARrnlvrncgvygLLNPDESH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 321 YRFLSGGSIPVPG----------QSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFmkeknhdqasmpdnt 390
Cdd:cd14884 230 QKRSVKGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAY--------------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 391 aaQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGA---- 466
Cdd:cd14884 295 --KAAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdne 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 467 -------SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERp 539
Cdd:cd14884 373 diysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 540 anppgVLALLDE-----ECWFPRATDRSFVEKLSGE-----QGSHPKFFKS---------KQPRGEADFSIIHYAGKVDY 600
Cdd:cd14884 451 -----IFRRLDDitklkNQGQKKTDDHFFRYLLNNErqqqlEGKVSYGFVLnhdadgtakKQNIKKNIFFIRHYAGLVTY 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 601 KANDWLVKNMDPLNDNVASLLHQSSDHFVSElwkevdrivgldqvssgessapvtfgaAGLKTKKGMFRTVGQLYKESLT 680
Cdd:cd14884 526 RINNWIDKNSDKIETSIETLISCSSNRFLRE---------------------------ANNGGNKGNFLSVSKKYIKELD 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774931 681 KLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 741
Cdd:cd14884 579 NLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
110-756 |
1.94e-77 |
|
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: 270.83 E-value: 1.94e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYknlpiytesiveMYRGKKRH-------EMPPHIYAISEAAYRSMLQDREDQ 182
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 183 SILCTGESGAGKTENTKKVIQYLAHVAsshkGGtlGRKKEAVqgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 262
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVA----GG--GPETDAF-----KHLAAAFTVLRSLGSAKTATNSESSRIGHFIEV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 263 NFdVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLG--TADQYRFLSGGSIPVPGQSDSENF 340
Cdd:cd14881 139 QV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYLSHGDTRQNEAEDAARF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 341 TQTMDSMAIMGFtpeELMSMLKVISAVLQFGNISFMkEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAiLTPRIK-VGR 419
Cdd:cd14881 218 QAWKACLGILGI---PFLDVVRVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRG-LTTRTHnARG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 420 EYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALdrrqRQGAS--------FIGILDIAGFEIFQLNSFEQLCIN 491
Cdd:cd14881 293 QLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSLK----RLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCIN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 492 YTNEKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPRATDRSFVEKLSGE 570
Cdd:cd14881 369 LCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQ 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 571 QGSHPKFFKSKQPRGEAdFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSdhfvselwkevdrivgldqvssges 650
Cdd:cd14881 445 HRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN------------------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 651 sapVTFGaaglktkkgmFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICR 730
Cdd:cd14881 499 ---CNFG----------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMA 565
|
650 660
....*....|....*....|....*.
gi 1988774931 731 QGFPNRIPFQEFRQRYEILTPNAIPR 756
Cdd:cd14881 566 GGYPHRMRFKAFNARYRLLAPFRLLR 591
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
110-789 |
9.51e-77 |
|
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: 270.04 E-value: 9.51e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYrgKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAHVasshkggTLGRKKEavqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTT-------DLSRSKY-----LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd14905 148 EIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNqGGSISVESIDDNRVFDRLKMSF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 348 AIMGFTPEELMSMLKVISAVLQFGNISFMKEKNhdQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAqt 427
Cdd:cd14905 228 VFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 428 keqadfavEALAKATYERLFRWLVHRINRALdrRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFI 507
Cdd:cd14905 304 --------DSLARSLYSALFHWIIDFLNSKL--KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 508 LEQEEYQREGIEW-NFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFfkSKQPRge 586
Cdd:cd14905 374 QEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLF--GKKPN-- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 587 aDFSIIHYAGKVDYKANDWLVKNMDPLNDNvASLLHQSS--DHFVSE--LWKEVDRIVGLDQVSSGESSA---PVTF--- 656
Cdd:cd14905 443 -KFGIEHYFGQFYYDVRGFIIKNRDEILQR-TNVLHKNSitKYLFSRdgVFNINATVAELNQMFDAKNTAkksPLSIvkv 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 657 --------------------GAAGLKTKKGMFRTVGQLYKE-SLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLD 715
Cdd:cd14905 521 llscgsnnpnnvnnpnnnsgGGGGGGNSGGGSGSGGSTYTTySSTNKAINNSNCDFHFIRCIKPNSKKTHLTFDVKSVNE 600
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774931 716 QLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPNAipRTFMDgkQASELMISALELDKNL---FRVGQSKVFFR 789
Cdd:cd14905 601 QIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQN--LFEKLKENDINIDSILpppIQVGNTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
109-789 |
6.89e-70 |
|
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: 248.63 E-value: 6.89e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYrgkkrhemppHIYAISEAAYRSMLQDRED-QSILCT 187
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 188 GESGAGKTENTKKVIQYLAhvaSSHKGGTLGRKKEAVQGelerqllqanpILEAFGNAKTVKNDNSSRFGKFIRINFDvA 267
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPKSKVTTKHSSAIES-----------VFKSFGCAKTLKNDEATRFGCSIDLLYK-R 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 268 GYIVGANIE-TYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTMDS 346
Cdd:cd14874 136 NVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 347 MAIMGFTPEELMSMLKVISAVLQFGNISFMKEKN----HDQASMPDNTAAQKLCHLLGVNVLEFTrAILTPRIKVGREYv 422
Cdd:cd14874 216 LHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnveQDVVEIGNMSEVKWVAFLLEVDFDQLV-NFLLPKSEDGTTI- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 423 qkaqTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAsfIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 502
Cdd:cd14874 294 ----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 503 HTMFILEQEEYQREGIEWNF-IDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSK 581
Cdd:cd14874 368 KHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKAR 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 582 QpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELwkevdrivgldqVSSGESSApvtfgaagl 661
Cdd:cd14874 446 N-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLL------------FESYSSNT--------- 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 662 ktkKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 741
Cdd:cd14874 504 ---SDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTT 580
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 742 FRQRYEILTPNAIPRTfmdgKQASELMISALELD----KNLFRVGQSKVFFR 789
Cdd:cd14874 581 FARQYRCLLPGDIAMC----QNEKEIIQDILQGQgvkyENDFKIGTEYVFLR 628
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
112-788 |
2.01e-67 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 244.11 E-value: 2.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 112 LHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKR----------HEMPPHIYAISEAAYRSMLQDRED 181
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 182 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 261
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 262 INFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEET--RADLLLG-TADQYRFLSGGSIPVPGQS-DS 337
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPtlRDSLEMNkCVNEFVMLKQADPLATNFAlDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 338 ENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFM------KEKN-------HDQASMPDNTAAQKL--CHLLGVN 402
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVpdpeggKSVGgansttvSDAQSCALKDPAQILlaAKLLEVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 403 --VLE---FTRAILTpriKVGREYVQ--KAQTKEQADFAVEALAKATYERLFRWLVHRINRAL----DRR-------QRQ 464
Cdd:cd14893 324 pvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYeksniviNSQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 465 GasfIGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQPCIDL 535
Cdd:cd14893 401 G---VHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 536 IERPanPPGVLALLDEECWFPRATDRSFVEKL-SGEQGSHpkffKSKQPRGEAD---------------FSIIHYAGKVD 599
Cdd:cd14893 478 FEDK--PFGIFDLLTENCKVRLPNDEDFVNKLfSGNEAVG----GLSRPNMGADttneylapskdwrllFIVQHHCGKVT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 600 YKANDWLVKNMDPLNDNVASLLHQSSDhfvselwkEVDRIVGLDQVSSGESSAPVTfGAAGLKTKKGMFRTVGQLYKESL 679
Cdd:cd14893 552 YNGKGLSSKNMLSISSTCAAIMQSSKN--------AVLHAVGAAQMAAASSEKAAK-QTEERGSTSSKFRKSASSARESK 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 680 T--------------KLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQR 745
Cdd:cd14893 623 NitdsaatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRR 702
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1988774931 746 YEILTPNaipRTFMDGKQASELMISALELDKnlFRVGQSKVFF 788
Cdd:cd14893 703 YKNVCGH---RGTLESLLRSLSAIGVLEEEK--FVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
110-749 |
5.80e-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: 237.33 E-value: 5.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 190 SGAGKTENTKKVIQYLAHvasshkggtLGRKKEAVQGELERqllqANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 269
Cdd:cd14882 82 SYSGKTTNARLLIKHLCY---------LGDGNRGATGRVES----SIKAILALVNAGTPLNADSTRCILQYQLTFGSTGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 270 IVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETR-ADLLLGTADQYRFLsggSIP--VPG----------QSD 336
Cdd:cd14882 149 MSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRlKEYNLKAGRNYRYL---RIPpeVPPsklkyrrddpEGN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 337 SENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMkeKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIK 416
Cdd:cd14882 226 VERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFR--QNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 417 VGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALD-RRQRQGASF-IGILDIAGFEIFQLNSFEQLCINYTN 494
Cdd:cd14882 304 KGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfPRAVFGDKYsISIHDMFGFECFHRNRLEQLMVNTLN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 495 EKLQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQPCIdlierpANPPGVLALLDEECWfPRATDRSFVEKLSGEQ 571
Cdd:cd14882 384 EQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVDQLM------TKPDGLFYIIDDASR-SCQDQNYIMDRIKEKH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 572 GSHPKffkskqPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEvdrivglDQVSSgess 651
Cdd:cd14882 457 SQFVK------KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRN---- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 652 apvtfgaagLKTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRI 728
Cdd:cd14882 520 ---------MRTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKA 584
|
650 660
....*....|....*....|.
gi 1988774931 729 CRQGFPNRIPFQEFRQRYEIL 749
Cdd:cd14882 585 RQKGFSYRIPFQEFLRRYQFL 605
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
131-287 |
1.09e-61 |
|
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: 208.74 E-value: 1.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 131 FCVVVNPYKNLPIYTESIV-EMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 209
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 210 SSHKGGT---LGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAT 286
Cdd:cd01363 81 FNGINKGeteGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGFEIINESLNTLMNVLRAT 160
|
.
gi 1988774931 287 R 287
Cdd:cd01363 161 R 161
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
110-787 |
2.63e-55 |
|
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: 207.00 E-value: 2.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYR-GKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 189 ESGAGKTENTKKVIQYLAH-VASSHKGGTLGRKKEAV----------QGELERQLLQANPILEAFGNAKTVKNDNSSRFG 257
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYqVKGSRRLPTNLNDQEEDnihneentdyQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 258 KFIRINFDvAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDS 337
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 338 ENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKE--------------------------KNHDQASMPDNTA 391
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAfrkksllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 392 AQKL-CHLLGVNVLEFTRAILTPRIkVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQR--QGASF 468
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 469 IGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANppGVLAL 548
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 549 LDEECWFPRATDRSFVEKLSGEQGSH-PKFFKSKQPRG-EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSD 626
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSIIRKFSRnSKYIKKDDITGnKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 627 HFVSEL-----WKEVDRIVGLDQVSSGESSapvtfgaagLKTKKGMFRTVGQ----LYKESLTKLMATLRNTNPNFLRCI 697
Cdd:cd14938 558 EYMRQFcmfynYDNSGNIVEEKRRYSIQSA---------LKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCM 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 698 IPNHEKRA-GKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEIltPNAiprtfmDGKQASELMISALELDK 776
Cdd:cd14938 629 KPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI--KNE------DLKEKVEALIKSYQISN 700
|
730
....*....|.
gi 1988774931 777 NLFRVGQSKVF 787
Cdd:cd14938 701 YEWMIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
987-1731 |
1.15e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 129.41 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 987 LLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKreeq 1066
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ---- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1067 grlEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVE 1146
Cdd:TIGR02168 306 ---ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1147 NERGMRERAEKQRRDLSEELEALRTELEdtlDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSL 1226
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1227 QEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRsESERGRKRADNQLQELSARLAQADREREDREERMHKLQCE 1306
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ-ENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1307 IES-LSGNLSSSDSKSLRLAKE-ISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQI 1384
Cdd:TIGR02168 539 IEAaLGGRLQAVVVENLNAAKKaIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1385 QTHSQQL---------TELRKQSEEVNSAV-EAGDEIRRK--LQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTI 1452
Cdd:TIGR02168 619 SYLLGGVlvvddldnaLELAKKLRPGYRIVtLDGDLVRPGgvITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEK 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1453 ALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRL--- 1529
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEela 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1530 ----EMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEReISTNEEKG 1605
Cdd:TIGR02168 779 eaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE-LSEDIESL 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1606 EEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVT 1685
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1988774931 1686 RDDVISQ-SKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEI 1731
Cdd:TIGR02168 938 IDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1122-1942 |
2.52e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 128.25 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1122 ARRAEAQRSLREA---LSQV----SELKEEVENERGMRERAEKQRrDLSEELEALRTELEdTLDSTAAQQELRsRREAEL 1194
Cdd:TIGR02168 172 ERRKETERKLERTrenLDRLedilNELERQLKSLERQAEKAERYK-ELKAELRELELALL-VLRLEELREELE-ELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1195 SELQRCVEEETRR---HETQLSELRVKHS---AALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSES 1268
Cdd:TIGR02168 249 KEAEEELEELTAElqeLEEKLEELRLEVSeleEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1269 ERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQ 1348
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1349 KMALASRVRALEEEKNGLmeRLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAiqrerq 1428
Cdd:TIGR02168 409 LERLEDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA------ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1429 keeekERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKF---DQCLAE--------EKAVSARLAEERDRAEADSR 1497
Cdd:TIGR02168 481 -----ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgiLGVLSElisvdegyEAAIEAALGGRLQAVVVENL 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1498 EKETRCLAlsrALQEAQDQK-----EELERANKQLRLEMEQLVNQQDDVGKN---VHELERARRTLETEAQNLRIQTQEL 1569
Cdd:TIGR02168 556 NAAKKAIA---FLKQNELGRvtflpLDSIKGTEIQGNDREILKNIEGFLGVAkdlVKFDPKLRKALSYLLGGVLVVDDLD 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1570 EEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEA 1649
Cdd:TIGR02168 633 NALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1650 QVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERD 1729
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1730 EIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNEL-------LTERLRKTALQVETLTVQLQGERTLAQKAE 1802
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAterrledLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1803 AA-------REQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQ 1875
Cdd:TIGR02168 873 SEleallneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT 952
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1876 AEDERRHADQYREQLDKSMVRLKQLKRQL-----------EEVEEENSRS---SAQKRKLQRELEELTDSSQTMNREISS 1941
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnlaaiEEYEELKERYdflTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
.
gi 1988774931 1942 L 1942
Cdd:TIGR02168 1033 R 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1122-1715 |
6.64e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 116.96 E-value: 6.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1122 ARRAEAQRSLREA---LSQVSELKEEVENERG----MRERAEK------------------QRRDLSEELEALRTELEDT 1176
Cdd:COG1196 172 ERKEEAERKLEATeenLERLEDILGELERQLEplerQAEKAERyrelkeelkeleaellllKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1177 LDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRvKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTS 1256
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEY-ELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1257 ELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLH 1336
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1337 DARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQ 1416
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1417 RELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRErqnctaLEKRQKKFDQCLAEEKAVSARLAEERDRAEADS 1496
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG------VEAAYEAALEAALAAALQNIVVEDDEVAAAAIE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1497 REKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDvgknVHELERARRTLETEAQNLRIQTQELEEELSEA 1576
Cdd:COG1196 565 YLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDL----READARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1577 ENSRLRLEVTLQAlkAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANR 1656
Cdd:COG1196 641 TLAGRLREVTLEG--EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774931 1657 GKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELA 1715
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1678 |
7.52e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 117.08 E-value: 7.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 847 LRNWQWWRLftkvkpLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEE 926
Cdd:TIGR02168 222 LRELELALL------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 927 MRARLASRKQeleevlgeletrleeeeergvQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLA 1006
Cdd:TIGR02168 296 EISRLEQQKQ---------------------ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1007 TAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQgrlEQEKFKRRMESEAMEAQ 1086
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED---RRERLQQEIEELLKKLE 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1087 E-QLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEE 1165
Cdd:TIGR02168 432 EaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1166 LE----------------------------ALRTELEDTLDSTAAQQ------------------ELRSRREAELSELQR 1199
Cdd:TIGR02168 512 LKnqsglsgilgvlselisvdegyeaaieaALGGRLQAVVVENLNAAkkaiaflkqnelgrvtflPLDSIKGTEIQGNDR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1200 CVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRA---RQSLEKAKATLEEERqnLTSELKSLQASRSESERGRKRAD 1276
Cdd:TIGR02168 592 EILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVddlDNALELAKKLRPGYR--IVTLDGDLVRPGGVITGGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1277 NQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRV 1356
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1357 RALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDsaiqrerqkeeekerv 1436
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT---------------- 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1437 erqrerlreeieDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQ 1516
Cdd:TIGR02168 814 ------------LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1517 KEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQeleeelseaensrlRLEVTLQALKAQF-- 1594
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE--------------GLEVRIDNLQERLse 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1595 -----EREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQ 1669
Cdd:TIGR02168 948 eysltLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
....*....
gi 1988774931 1670 GQMKEVLRE 1678
Cdd:TIGR02168 1028 REARERFKD 1036
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
115-730 |
8.94e-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: 116.38 E-value: 8.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 115 LRERYYSGLIYTYSGLFCV-VVNPYKNL------PIYTESIVEMYRGKKRHE--MPPHIYAISE---------------- 169
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 170 ----AAYRSMLQDReDQSILCTGESGAGKTENTKKVIQYLAHVA---------------------------SSHKGGTLG 218
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetckvsgstrqpkiklftSSTKSTIQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 219 RKKEA------------------------------------------VQG------------ELERQL------------ 232
Cdd:cd14894 166 RTEEArtialleakgvekyeivlldlhperwdemtsvsrskrlpqvhVDGlffgfyeklehlEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 233 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVAGY---IVGANIETYLLEKSRATRQA------KDERTFHI 297
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 298 FYQLLCGASEETRADLL----------------LGTADqYRFLSGGSIPVPGQSDSENFTQTMDSMAIMGFTPEELMSML 361
Cdd:cd14894 326 LYAMVAGVNAFPFMRLLakelhldgidcsaltyLGRSD-HKLAGFVSKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 362 KVISAVLQFGNISFMKEKNHDQASMPDN---TAAQKLCHLLGVNVLE-FTRAILTPRIKV--GREYVQKAQTKEQADFAV 435
Cdd:cd14894 405 KVLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEkLERMLMTKSVSLqsTSETFEVTLEKGQVNHVR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 436 EALAKATYERLFRWLVHRINRAL-------DRRQRQ---------GASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQq 499
Cdd:cd14894 485 DTLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY- 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 500 lfnhtmfileQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATD--------------RSFVE 565
Cdd:cd14894 564 ----------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENmnaqqeekrnklfvRNIYD 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 566 KLSGEQGSHPKFFKSKQPRGEA-----DFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRI- 639
Cdd:cd14894 634 RNSSRLPEPPRVLSNAKRHTPVllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQLg 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 640 ----VGLDQVSSGESSapvtfgAAGLKTKKGMFRTVGQLYKESLTKLMatlrntnPNFLRCIIPNHEKRAGKLSPHLVLD 715
Cdd:cd14894 714 wspnTNRSMLGSAESR------LSGTKSFVGQFRSHVNVLTSQDDKNM-------PFYFHCIRPNAKKQPSLVNNDLVEQ 780
|
810
....*....|....*
gi 1988774931 716 QLRCNGVLEGIRICR 730
Cdd:cd14894 781 QCRSQRLIRQMEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
985-1563 |
5.00e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.80 E-value: 5.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 985 QRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKRE 1064
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1065 EQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEE 1144
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1145 VENERGMRERAEKQRRDLSEELEALRTELEdtldstAAQQELRSRREAELSELQRcvEEETRRHETQLSELRVKHSAALD 1224
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLE------RLEEELEELEEALAELEEE--EEEEEEALEEAAEEEAELEEEEE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1225 SLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASrsesergrkRADNQLQELSARLAQADREREDREERMHKLQ 1304
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA---------EADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1305 ceieslsgnlssSDSKSLRLAKEISSLESQLHDARELLQDESRQ----KMALASRVRALEEEKnglmeRLEEEEERGKEL 1380
Cdd:COG1196 531 ------------GVEAAYEAALEAALAAALQNIVVEDDEVAAAAieylKAAKAGRATFLPLDK-----IRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1381 SRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEdmtIALQRERQN 1460
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS---LTGGSRREL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1461 CTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDD 1540
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
570 580
....*....|....*....|...
gi 1988774931 1541 VGKNVHELERARRTLETEAQNLR 1563
Cdd:COG1196 751 EALEELPEPPDLEELERELERLE 773
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
993-1749 |
2.92e-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: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 993 TLETKVKSLETDLATAVEQRERLGKEKKQLEErlnevTDQLTEEEEKTKSLNKLKNKQEAViADLEERLKREEQGRLEQE 1072
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRREREKAER-----YQALLKEKREYEGYELLKEKEALE-RQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1073 KFKRRMESEAMEAQEQLSDLGMLSSELRgslAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENergmr 1152
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIK---DLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK----- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1153 erAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEEtrrhETQLSELRVKHSA---ALDSLQEQ 1229
Cdd:TIGR02169 327 --LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV----DKEFAETRDELKDyreKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1230 LDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIES 1309
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1310 LSGNLSSsdskslrLAKEISSLESQLHDARELLQDESRQKMALASRVR------------------ALEEEKNGLMERLE 1371
Cdd:TIGR02169 481 VEKELSK-------LQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryatAIEVAAGNRLNNVV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1372 EEEERGKELSRQIQTHSQ-------QLTELRKQSEEVNSAVEAG------------DEIRRKLQRELDSAIQRERQKEEE 1432
Cdd:TIGR02169 554 VEDDAVAKEAIELLKRRKagratflPLNKMRDERRDLSILSEDGvigfavdlvefdPKYEPAFKYVFGDTLVVEDIEAAR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1433 KERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFdqcLAEEKAVSARLAE---ERDRAEADSREKETRCLALSRA 1509
Cdd:TIGR02169 634 RLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSE---PAELQRLRERLEGlkrELSSLQSELRRIENRLDELSQE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1510 LQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRiqtQELEEELSEAENSRLRLEVTLQA 1589
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE---ARIEELEEDLHKLEEALNDLEAR 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1590 LKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQ-------VETANRGKEEAM 1662
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQiksiekeIENLNGKKEELE 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1663 KQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVS-SSSG 1741
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdEEIP 947
|
....*...
gi 1988774931 1742 KNVLSEEK 1749
Cdd:TIGR02169 948 EEELSLED 955
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
864-1402 |
2.78e-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: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 864 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLG 943
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 944 ELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLE 1023
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1024 ERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSL 1103
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1104 AQKEKEITSLQGRLEEEGARR-AEAQRSLREALSQVSELKEEVENERGMRERAEKQR--RDLSEELEALRTELEDTLDST 1180
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALlLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNivVEDDEVAAAAIEYLKAAKAGR 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1181 AAQQEL---RSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQnLTSE 1257
Cdd:COG1196 574 ATFLPLdkiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE-VTLE 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1258 LKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIEslsgnlsssdskslRLAKEISSLESQLHD 1337
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE--------------EEERELAEAEEERLE 718
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774931 1338 ARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVN 1402
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVN 783
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
962-1816 |
2.78e-20 |
|
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: 98.51 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 962 EKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTK 1041
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1042 SLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLgmlsselrgslaqkEKEITSLQGRLEEEG 1121
Cdd:pfam02463 255 SSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL--------------ERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1122 ARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCV 1201
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1202 EEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQE 1281
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1282 LSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDAREL-LQDESRQKMALASRVRALE 1360
Cdd:pfam02463 481 KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENyKVAISTAVIVEVSATADEV 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1361 EEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQR 1440
Cdd:pfam02463 561 EERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKES 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1441 ERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEEL 1520
Cdd:pfam02463 641 AKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1521 ERANKQLRLEM----EQLVNQQDDVGKNVHELERARRTLETEaQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFER 1596
Cdd:pfam02463 721 ELLADRVQEAQdkinEELKLLKQKIDEEEEEEEKSRLKKEEK-EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1597 EISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVL 1676
Cdd:pfam02463 800 EEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEEL 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1677 RELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVL-SEEKRRLDAR 1755
Cdd:pfam02463 880 EEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKeKEENNKEEEE 959
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774931 1756 VNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELK 1816
Cdd:pfam02463 960 ERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
871-1422 |
5.03e-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: 5.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 871 EIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGELETRLE 950
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 951 EEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVT 1030
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1031 DQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEI 1110
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1111 TSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGM-----RERAEKQRRDLSEELEALRT--ELEDTLDSTAAQ 1183
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFlegvkAALLLAGLRGLAGAVAVLIGveAAYEAALEAALA 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1184 QELRSRREAELSELQRCVEEETRRHETQLSELrvkhsAALDSLQEQLDNSKRARQSLEKAKATLEEERQnltsELKSLQA 1263
Cdd:COG1196 546 AALQNIVVEDDEVAAAAIEYLKAAKAGRATFL-----PLDKIRARAALAAALARGAIGAAVDLVASDLR----EADARYY 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1264 SRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQ 1343
Cdd:COG1196 617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE 696
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774931 1344 DesrQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSA 1422
Cdd:COG1196 697 E---ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
990-1550 |
3.12e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 95.11 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 990 EKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLknkqEAVIADLEERLKREEQgrl 1069
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETL----EAEIEDLRETIAETER--- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1070 EQEKFKRRMEseamEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENER 1149
Cdd:PRK02224 273 EREELAEEVR----DLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1150 GMRERAEKQRRDLSEELEALRTELEDTldstaaqQELRSRREAELSELqrcvEEETRRHETQLSELRVKHSAALDSLQEQ 1229
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEA-------REAVEDRREEIEEL----EEEIEELRERFGDAPVDLGNAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1230 LDNSKRARQSLEKAKATLEEERQNLTSELKSLQASR----------SESERGRKRADNQLQELSARLAQADREREDREER 1299
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1300 MHKLQcEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKE 1379
Cdd:PRK02224 498 LERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1380 LSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQ 1459
Cdd:PRK02224 577 LNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKE 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1460 NC-TALEKRQKKFDQCLAEEKAVSARL-AEERDRAEADS-REKETRCLALSRALQEAQDQKEELERANKQLRLEMEQlvn 1536
Cdd:PRK02224 657 RAeEYLEQVEEKLDELREERDDLQAEIgAVENELEELEElRERREALENRVEALEALYDEAEELESMYGDLRAELRQ--- 733
|
570
....*....|....
gi 1988774931 1537 qqddvgKNVHELER 1550
Cdd:PRK02224 734 ------RNVETLER 741
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1324-1939 |
3.69e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.00 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1324 LAKEISSLESQ---LHDARELLQD-ESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSE 1399
Cdd:COG1196 198 LERQLEPLERQaekAERYRELKEElKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1400 EVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEK 1479
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1480 AVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEA 1559
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1560 QNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREistnEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQ 1639
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL----EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1640 LEAELQEAEAQVETANRGKEEAMKQLR--RLQGQMKEVLRELDDskvTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVS 1717
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALeaALAAALQNIVVEDDE---VAAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1718 ERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTL 1797
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1798 AQKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKE--VMMQ 1875
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEeeLLEE 750
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774931 1876 AEDERRHADQYREQLDKsmvRLKQLKRQL--------------EEVEEENSRSSAQKRKLQRELEELTDSSQTMNREI 1939
Cdd:COG1196 751 EALEELPEPPDLEELER---ELERLEREIealgpvnllaieeyEELEERYDFLSEQREDLEEARETLEEAIEEIDRET 825
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1241-1844 |
1.38e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.08 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1241 EKAKATLEEERQNLT----------SELKSL--QASRSE-----SERGRKRadnQLQELSARLAQADREREDREERMHKL 1303
Cdd:COG1196 175 EEAERKLEATEENLErledilgeleRQLEPLerQAEKAEryrelKEELKEL---EAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1304 QCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQ 1383
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1384 IQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERqrerlreeiedmtiALQRERQNCTA 1463
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE--------------ELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1464 LEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGK 1543
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1544 nvhELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRRALSkQVRELEIQL 1623
Cdd:COG1196 478 ---ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL-AAALQNIVV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1624 EEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQG---------QMKEVLRELDDSKVTRDDVISQSK 1694
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAvdlvasdlrEADARYYVLGDTLLGRTLVAARLE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1695 DSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEmvssssgknVLSEEKRRLDARVNQLEEELEEEQTNNELLT 1774
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA---------LLEAEAELEELAERLAEEELELEEALLAEEE 704
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774931 1775 ERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARL-----GEMEGAVRGKHRMSVAALEAKIETM 1844
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEeealeELPEPPDLEELERELERLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1203-1947 |
1.61e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 92.81 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1203 EETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQ------SLEKAKATLEEERQNltSELKSLQASRSESERGRKRAD 1276
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAERYKElkaelrELELALLVLRLEELR--EELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1277 NQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRV 1356
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1357 RALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVeagdeirRKLQRELDSAiqrerqkeeekerv 1436
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV-------AQLELQIASL-------------- 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1437 ERQRERLREEIEDMTIALQRERQNCTALEKRQKKfdqclAEEKAVSARLAEERDRAEadsrEKETRCLALSRALQEAQDQ 1516
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEE-----AELKELQAELEELEEELE----ELQEELERLEEALEELREE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1517 KEELERANKQLRLEMEQLVNQQDdvgknvhELERARRTLETEAQNLRIQTQELEEELSEA----------ENSRLRLEVT 1586
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLD-------SLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisvdEGYEAAIEAA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1587 LQAL--------KAQFEREISTNEEKGEEKR--------RALSKQVRELEIQLEEERSQRSQSVSSK--KQLEAELQEAE 1648
Cdd:TIGR02168 543 LGGRlqavvvenLNAAKKAIAFLKQNELGRVtflpldsiKGTEIQGNDREILKNIEGFLGVAKDLVKfdPKLRKALSYLL 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1649 AQVETANRGkEEAMKQLRRLQGQMKEVlrELDDSKVTRDDVIS-QSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQE 1727
Cdd:TIGR02168 623 GGVLVVDDL-DNALELAKKLRPGYRIV--TLDGDLVRPGGVITgGSAKTNSSILERRREIEELEEKIEELEEKIAELEKA 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1728 RDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQ 1807
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1808 LEKQNKELKARLGEMEGAVrGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYR 1887
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEEL-KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1888 EQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLS 1947
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1389-1946 |
7.76e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 7.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1389 QQLTELRKQSEEVNSAVEAGDEIR-----------RKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRE 1457
Cdd:COG1196 200 RQLEPLERQAEKAERYRELKEELKeleaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1458 RQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQ 1537
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1538 QDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFER------EISTNEEKGEEKRRA 1611
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERleeeleELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1612 LSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETAnRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVIS 1691
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL-LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1692 QSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDA----RVNQLEEELEEEQ 1767
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKirarAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1768 TNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGA------VRGKHRMSVAALEAKI 1841
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGsaggslTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1842 ETMEEQLEQerqeraiANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKL 1921
Cdd:COG1196 679 AELEELAER-------LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570 580
....*....|....*....|....*
gi 1988774931 1922 QRELEELTDSSQTMNREISSLRNQL 1946
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1036-1939 |
1.14e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 90.13 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1036 EEEKTKSLNKLK------NKQEAVIADLEERLKREEQGRLEQEKFK----RRMESEAMEAQEQLSDLGMLSSELRGSLAQ 1105
Cdd:TIGR02169 169 DRKKEKALEELEeveeniERLDLIIDEKRQQLERLRREREKAERYQallkEKREYEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1106 KEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENE-RGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQ 1184
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1185 ELRSRREAELSELQRCVEEETRRhetqlselRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQAS 1264
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKR--------RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1265 RSESERGRKRADNQLQELSARLAQadreredreermhkLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQD 1344
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELAD--------------LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1345 ESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAiq 1424
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVA-- 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1425 rerqkeeekerverqrerlreeiedmtiALQRERQNCTALEKRQKKFDQCLAEEKAVSAR---LAEERDRAEADSREKET 1501
Cdd:TIGR02169 545 ----------------------------AGNRLNNVVVEDDAVAKEAIELLKRRKAGRATflpLNKMRDERRDLSILSED 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1502 RCLALSRALQEAQDQKEELERANKQLRLEMEqlvnqqddvgknvhELERARRTLeteaqnlriqtqeleeelseaenSRL 1581
Cdd:TIGR02169 597 GVIGFAVDLVEFDPKYEPAFKYVFGDTLVVE--------------DIEAARRLM-----------------------GKY 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1582 RLeVTLQAL----------KAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQV 1651
Cdd:TIGR02169 640 RM-VTLEGElfeksgamtgGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI 718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1652 ETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSER-----QKRQAQQ 1726
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsRIPEIQA 798
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1727 ERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAARE 1806
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1807 QLEKQNKELKARLGEMEGAVRgKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEvMMQAEDERRHADQY 1886
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLR-ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE-DEEIPEEELSLEDV 956
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774931 1887 REQLDKSMVRLKQLK-------RQLEEVEEENSRSSAQKRKLQRELEEL---TDSSQTMNREI 1939
Cdd:TIGR02169 957 QAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAIlerIEEYEKKKREV 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1009-1728 |
1.65e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.82 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1009 VEQRERLGKEKKQLE--ERLNEVTDQLTEEEEKtkslnklknkqeaviadLEERLKREEQGRLEQEkfkrrmeSEAMEAQ 1086
Cdd:PTZ00121 1066 VGQDEGLKPSYKDFDfdAKEDNRADEATEEAFG-----------------KAEEAKKTETGKAEEA-------RKAEEAK 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1087 EQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREalSQVSELKEEVENERGMRE--RAEKQRR--DL 1162
Cdd:PTZ00121 1122 KKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEE--ARKAEDAKKAEAARKAEEvrKAEELRKaeDA 1199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1163 SEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHE--------TQLSELRVKHSAALDSLQ------- 1227
Cdd:PTZ00121 1200 RKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEeernneeiRKFEEARMAHFARRQAAIkaeeark 1279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1228 -------EQLDNSKRARQSLEKAKAtleEERQNLTSELKSLQASRSESERGRKRAD------------NQLQELSARLAQ 1288
Cdd:PTZ00121 1280 adelkkaEEKKKADEAKKAEEKKKA---DEAKKKAEEAKKADEAKKKAEEAKKKADaakkkaeeakkaAEAAKAEAEAAA 1356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1289 ADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEI-SSLESQLHDARELLQDESRQKMALASRVRAlEEEKNGLM 1367
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkKKAEEDKKKADELKKAAAAKKKADEAKKKA-EEKKKADE 1435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1368 ERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEA---------GDEIRRKLQRELDSAIQRERQKEEEKERVER 1438
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAkkkaeeakkADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1439 QRERLREEIEDMTIALQRERQNCTALEKRQKKFDQClaeEKAVSARLAEERDRAEADSREKETRCLALSRAlQEAqdQKE 1518
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL---KKAEELKKAEEKKKAEEAKKAEEDKNMALRKA-EEA--KKA 1589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1519 ELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREI 1598
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1599 STNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEaQVETANRGKEEAMKQLRRLQGQMKEVLRE 1678
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE-ELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1679 LDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQER 1728
Cdd:PTZ00121 1749 AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1125-1942 |
5.37e-16 |
|
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: 84.73 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1125 AEAQRSLREALSQVSELKEEVENERGMRERAEKQR-------RDLSEELEALRTELEDTLDSTAAQQELRSRREAELSEL 1197
Cdd:TIGR02169 152 PVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIerldliiDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1198 QRCVEEETRRHETQLSELRvKHSAALDSLQEQL-DNSKRARQSLE----KAKATLEEERQNLTSELKSLQASRSESERGR 1272
Cdd:TIGR02169 232 KEALERQKEAIERQLASLE-EELEKLTEEISELeKRLEEIEQLLEelnkKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1273 KRADNQLQELSARLAQADREredreerMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDES----RQ 1348
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAE-------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDkefaET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1349 KMALASRVRALE---EEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQR 1425
Cdd:TIGR02169 384 RDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1426 ERQKEEEkerverqrerlreeiedmtiaLQRERQNCTALEKRQKKFDQCLAEEKAvSARLAEERDRAEADSREketrclA 1505
Cdd:TIGR02169 464 LSKYEQE---------------------LYDLKEEYDRVEKELSKLQRELAEAEA-QARASEERVRGGRAVEE------V 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1506 LSRALQEAQDQKEELERANKQLRLEME--------QLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAE 1577
Cdd:TIGR02169 516 LKASIQGVHGTVAQLGSVGERYATAIEvaagnrlnNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSE 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1578 NSRLRLEVTLQALKAQFEREI-----STNEEKGEEKRRALSKQVR--ELEIQLEEE-------RSQRSQSVSSKKQLEAE 1643
Cdd:TIGR02169 596 DGVIGFAVDLVEFDPKYEPAFkyvfgDTLVVEDIEAARRLMGKYRmvTLEGELFEKsgamtggSRAPRGGILFSRSEPAE 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1644 LQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKvtrddviSQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQ 1723
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS-------RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1724 AQQERDEIADEMVSSSSGKNVLSEEKRRLDARV-----NQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLA 1798
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1799 QKAEAAREQLEKQNKELKARLGEMEGAvrgkhrmsVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAED 1878
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKE--------IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1879 ERRHADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKLQRE------LEELTDSSQTMNREISSL 1942
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRAL 970
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1115-1722 |
3.96e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.62 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1115 GRLEEEGARRAEAQRSLREALSQVSELKEEVENERgmrerAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAEL 1194
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQI-----EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETR 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1195 SELQRCVEEetrrHETQLSELRVKhSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKR 1274
Cdd:PRK02224 237 DEADEVLEE----HEERREELETL-EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1275 ADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALAS 1354
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1355 RVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGdeirrklQRELDSAIQRERQKEEEKE 1434
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA-------EALLEAGKCPECGQPVEGS 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1435 RVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSaRLAEERDRAEADSREKETRCLALSRALQEAQ 1514
Cdd:PRK02224 465 PHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE-RLEERREDLEELIAERRETIEEKRERAEELR 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1515 DQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRiqtqeleeelseaensRLRlevTLQALKAQF 1594
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE----------------RIR---TLLAAIADA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1595 EREIstneEKGEEKRRALSKQVRELEIQLEEersqrsqSVSSKKQLEAELQeaEAQVETANRGKEEAMKQLRRLQGQmke 1674
Cdd:PRK02224 605 EDEI----ERLREKREALAELNDERRERLAE-------KRERKRELEAEFD--EARIEEAREDKERAEEYLEQVEEK--- 668
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1988774931 1675 vLRELDDSkvtRDDVISQSKDSEKKIQTLEAevlhLTEEL-AVSERQKR 1722
Cdd:PRK02224 669 -LDELREE---RDDLQAEIGAVENELEELEE----LRERReALENRVEA 709
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
862-1289 |
1.58e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 862 LLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEV 941
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 942 LGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQ 1021
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1022 LEERLNEV--TDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRL--EQEKFKRRMESEAMEAQEQLSDLGMLSS 1097
Cdd:COG1196 503 YEGFLEGVkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVveDDEVAAAAIEYLKAAKAGRATFLPLDKI 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1098 ELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSE--LKEEVENERGMRERAEKQRRDLSEELEALRTELED 1175
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRtlVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1176 TLDSTAAQQELRSRREAELSELqrcvEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLT 1255
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEEL----AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
410 420 430
....*....|....*....|....*....|....
gi 1988774931 1256 SELKSLQASRSESERGRKRADNQLQELSARLAQA 1289
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
863-1310 |
1.89e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 863 LQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVL 942
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 943 GELETRLEeeeergvQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQL 1022
Cdd:COG1196 403 EELEEAEE-------ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1023 EERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGS 1102
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1103 LAQKEKEITSLQ----GRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRD----LSEELEALRTELE 1174
Cdd:COG1196 556 DEVAAAAIEYLKaakaGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLgdtlLGRTLVAARLEAA 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1175 DTLDSTAAQQELRSRREAE-LSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQN 1253
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEgGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774931 1254 LTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESL 1310
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
982-1563 |
2.65e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.95 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 982 SARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEaviaDLEERL 1061
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1062 KREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRgSLAQKEKEITSLQGrLEEEGARRAEAQRSLREALSQVSEL 1141
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-ELEEKVKELKELKE-KAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1142 KEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQElrsrrEAELSELQRCVEEETRRHETQLSELrvkhsa 1221
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-----RHELYEEAKAKKEELERLKKRLTGL------ 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1222 aldslqeQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSEsergRKRADNQLQELSAR--LAQADREREDREER 1299
Cdd:PRK03918 385 -------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE----LKKAIEELKKAKGKcpVCGRELTEEHRKEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1300 MHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESrqkmaLASRVRALEEEKNGLMERLEEEEERGKE 1379
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE-----LAEQLKELEEKLKKYNLEELEKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1380 LSRQ-----------IQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELD----SAIQRERQKEEEKERVERQRERLR 1444
Cdd:PRK03918 529 KLKEkliklkgeiksLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfESVEELEERLKELEPFYNEYLELK 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1445 EEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAE-ERDRAEADSREKETRCLALSRALQEAQDQKEELERA 1523
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElEKKYSEEEYEELREEYLELSRELAGLRAELEELEKR 688
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1988774931 1524 NKQLRLEMEQLVNQQDDVGKNVHELERARRTLEtEAQNLR 1563
Cdd:PRK03918 689 REEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELR 727
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
958-1261 |
2.80e-14 |
|
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: 78.96 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 958 QLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEE 1037
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1038 EKTKSLNKLKNKQEAVIADLEERLKREEQgRLEQEKFKrrmeseamEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRL 1117
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEA-RLSHSRIP--------EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1118 EEEGARRAEAQRSLREALSQVSELKEEVENERGmreraekQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSEL 1197
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG-------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774931 1198 QRCVEE---ETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKA--TLEEERQNLTSELKSL 1261
Cdd:TIGR02169 902 ERKIEEleaQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRAL 970
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
860-1707 |
5.85e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 78.09 E-value: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 860 KPLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLAdQLQAEAELFAEAEEMRARLASRKQELE 939
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL-YLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 940 EVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEK 1019
Cdd:pfam02463 255 SSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1020 KQLEERLNE---VTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLS 1096
Cdd:pfam02463 335 EEIEELEKElkeLEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELA 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1097 SELRGSLAQKEKEITSLQGRLEEEGaRRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDT 1176
Cdd:pfam02463 415 RQLEDLLKEEKKEELEILEEEEESI-ELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1177 LDSTAAQQELRSRREAELSELQRCVEEETR---------RHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATL 1247
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLALIKDGVGGRiisahgrlgDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1248 EEERQNLTSELKSLQASRS-----ESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSL 1322
Cdd:pfam02463 574 PLGARKLRLLIPKLKLPLKsiavlEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVS 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1323 RLAKEissLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTEL---RKQSE 1399
Cdd:pfam02463 654 LEEGL---AEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELladRVQEA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1400 EVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEK 1479
Cdd:pfam02463 731 QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1480 AVSARLAEERDRAEADSrEKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQddvgknvhELERARRTLETEA 1559
Cdd:pfam02463 811 KEEAELLEEEQLLIEQE-EKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL--------LQELLLKEEELEE 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1560 QNLRIQTQELEEELSEAENSRLRLEVTLQALkaqfEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQ 1639
Cdd:pfam02463 882 QKLKDELESKEEKEKEEKKELEEESQKLNLL----EEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEE 957
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1640 LEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVI--SQSKDSEKKIQTLEAEV 1707
Cdd:pfam02463 958 EEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIraIIEETCQRLKEFLELFV 1027
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
994-1541 |
2.84e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 75.54 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 994 LETKVKSLETDLATAVEQRE-RLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEER-----LKREEQG 1067
Cdd:pfam15921 322 LESTVSQLRSELREAKRMYEdKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRekelsLEKEQNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1068 RLEQ---------EKFKRRMESEAMEAQEQLSDLGMLSSELRGslaQKEKEITSLQGRLEE-EGARRAEAQ-RSLREALS 1136
Cdd:pfam15921 402 RLWDrdtgnsitiDHLRRELDDRNMEVQRLEALLKAMKSECQG---QMERQMAAIQGKNESlEKVSSLTAQlESTKEMLR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1137 QVSElkeEVENERGMRERAEKQRRDLSEELEalrtELEDTLDSTAAQ-QELRSRREAELSELQRCVEEET--RRHETQLS 1213
Cdd:pfam15921 479 KVVE---ELTAKKMTLESSERTVSDLTASLQ----EKERAIEATNAEiTKLRSRVDLKLQELQHLKNEGDhlRNVQTECE 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1214 ELRVKHSA---ALDSLQEQLDNSK-------RARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELS 1283
Cdd:pfam15921 552 ALKLQMAEkdkVIEILRQQIENMTqlvgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1284 ARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQ-KMALASRVRALEEE 1362
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQT 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1363 KNGLMERLEE---EEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGD-------EIRRKLQRELDSAIQRERQKEEE 1432
Cdd:pfam15921 712 RNTLKSMEGSdghAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANkekhflkEEKNKLSQELSTVATEKNKMAGE 791
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1433 KERVERQRERLREEIEDMTIAL--------------QRERQNCTALeKRQKKFD------QCLAEEKAVSARLAEERDRA 1492
Cdd:pfam15921 792 LEVLRSQERRLKEKVANMEVALdkaslqfaecqdiiQRQEQESVRL-KLQHTLDvkelqgPGYTSNSSMKPRLLQPASFT 870
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1988774931 1493 EADSREKETRCLA--LSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDV 1541
Cdd:pfam15921 871 RTHSNVPSSQSTAsfLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTV 921
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1076-1266 |
2.46e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.64 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1076 RRMESEAMEAQEQLSDLGMLSsELRGSLAQKEKEITSLqgRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERA 1155
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIR-ELAERYAAARERLAEL--EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1156 EKQRRDLSEELEALR-----------TELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALD 1224
Cdd:COG4913 315 EARLDALREELDELEaqirgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1988774931 1225 SLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRS 1266
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
924-1731 |
3.09e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.48 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 924 AEEMRARLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQ--DLEEQLEEEESARQRLLLEKVTLETKVKSL 1001
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkaEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1002 ETDLATAVEQRERLGK--EKKQLEERlnEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRME 1079
Cdd:PTZ00121 1276 EARKADELKKAEEKKKadEAKKAEEK--KKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1080 SEAMEAQEqlsdlgmlsselrgslAQKEKEITSLQgrlEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQR 1159
Cdd:PTZ00121 1354 AAADEAEA----------------AEEKAEAAEKK---KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1160 RDlSEELEALRTELEDTLDSTAAQQELRSRREAElsELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQS 1239
Cdd:PTZ00121 1415 AA-KKKADEAKKKAEEKKKADEAKKKAEEAKKAD--EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1240 LEKAKATLEEERQNLTSELKSLQASRSESergRKRADNQLQELSARLAqadreredreermhklqceiESLSGNLSSSDS 1319
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEE---AKKADEAKKAEEAKKA--------------------DEAKKAEEKKKA 1548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1320 KSLRLAKEISSLEsQLHDARELLQDESRQKMAL--ASRVRALEEEK-NGLMERLEEEEERGKELSRQIQTHSQQLTELRK 1396
Cdd:PTZ00121 1549 DELKKAEELKKAE-EKKKAEEAKKAEEDKNMALrkAEEAKKAEEARiEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1397 QsEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQclA 1476
Cdd:PTZ00121 1628 A-EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK--A 1704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1477 EEkaVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKqlrlemeqlvnqqDDVGKNvhELERARRTLE 1556
Cdd:PTZ00121 1705 EE--LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK-------------DEEEKK--KIAHLKKEEE 1767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1557 TEAQNLRIQTQELEEELSEAENSRLRLEV--TLQALKAQFEreistNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSV 1634
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVdkKIKDIFDNFA-----NIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQ 1842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1635 SSKKQlEAELQEAEAQVETANRGKEEA--MKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAevlhLTE 1712
Cdd:PTZ00121 1843 LEEAD-AFEKHKFNKNNENGEDGNKEAdfNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDI----IDD 1917
|
810
....*....|....*....
gi 1988774931 1713 ELAVSERQKRQAQQERDEI 1731
Cdd:PTZ00121 1918 KLDKDEYIKRDAEETREEI 1936
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1465-1943 |
3.28e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.48 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1465 EKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANkQLRLEMEQLVNQQDDVGKN 1544
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKKK 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1545 VHELERARRTLETEAqnlriqtqeleeelseaensrlrlEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLE 1624
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEA------------------------EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA 1393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1625 EERSQRSQSVSSKKQleaELQEAEAQVETANRGKEEAMKQLRRLQGQMK-EVLRELDDSKVTRDDVISQSKDSEKKIQTL 1703
Cdd:PTZ00121 1394 DEAKKKAEEDKKKAD---ELKKAAAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1704 EAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQ 1783
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1784 VETLTVQLQGERTlaQKAEAAREQLEKQNKELkaRLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMR 1863
Cdd:PTZ00121 1551 LKKAEELKKAEEK--KKAEEAKKAEEDKNMAL--RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1864 KTE---KKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVE---EENSRSSAQKRK----LQRELEELTDSSQ 1933
Cdd:PTZ00121 1627 KAEeekKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKkkaEEAKKAEEDEKKaaeaLKKEAEEAKKAEE 1706
|
490
....*....|
gi 1988774931 1934 TMNREISSLR 1943
Cdd:PTZ00121 1707 LKKKEAEEKK 1716
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
864-1422 |
6.14e-12 |
|
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: 71.36 E-value: 6.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 864 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELfaeaeemRARLASRKQELEEVLG 943
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEA-------KRNVERQLSTLQAQLS 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 944 ELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDL------------------ 1005
Cdd:pfam01576 528 DMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLdhqrqlvsnlekkqkkfd 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1006 ----------ATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFK 1075
Cdd:pfam01576 608 qmlaeekaisARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSK 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1076 RRMESEAMEAQEQLSDlgmLSSELRGSLAQK---EKEITSLQGRLEEEGARRAEAQRSLREALS-QVSELKEEVENERGM 1151
Cdd:pfam01576 688 RALEQQVEEMKTQLEE---LEDELQATEDAKlrlEVNMQALKAQFERDLQARDEQGEEKRRQLVkQVRELEAELEDERKQ 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1152 RERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQL-----SELRVKH-SAALDS 1225
Cdd:pfam01576 765 RAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILaqskeSEKKLKNlEAELLQ 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1226 LQEQLDNSKRARQslekakaTLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQC 1305
Cdd:pfam01576 845 LQEDLAASERARR-------QAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTL 917
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1306 EIESLSGNLSSSDSKS------------------LRLAKE-----------ISSLESQLHDARELLQDESRQKMALASRV 1356
Cdd:pfam01576 918 QVEQLTTELAAERSTSqksesarqqlerqnkelkAKLQEMegtvkskfkssIAALEAKIAQLEEQLEQESRERQAANKLV 997
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774931 1357 RALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSA 1422
Cdd:pfam01576 998 RRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDA 1063
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
928-1254 |
7.78e-12 |
|
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: 70.87 E-value: 7.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 928 RARLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLAt 1007
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE- 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1008 avEQRERLGKEKKQLEERLNEVTDQLTEE-EEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQ 1086
Cdd:TIGR02169 769 --ELEEDLHKLEEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1087 EQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEEL 1166
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1167 EALRTELEDTLDSTAAQQELrsrREAELSElqRCVEEETRRHETQLSELRVKHSAALdslqEQLDNSKRARQSLEKAKAT 1246
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEI---PEEELSL--EDVQAELQRVEEEIRALEPVNMLAI----QEYEEVLKRLDELKEKRAK 997
|
....*...
gi 1988774931 1247 LEEERQNL 1254
Cdd:TIGR02169 998 LEEERKAI 1005
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
995-1681 |
8.40e-12 |
|
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: 70.87 E-value: 8.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 995 ETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVT---DQLTEE-EEKTKSLNKLKNKQEAVIADLEERLKREEQGRLE 1070
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkrrDKLTEEyAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1071 QEKFKRRMES---EAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVEN 1147
Cdd:TIGR02169 394 LEKLKREINElkrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1148 ERGMRERAEKQRRDLSEELEALRTEL----EDTLDSTAAQQELRSRRE------AELSEL-------------------- 1197
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQAraseERVRGGRAVEEVLKASIQgvhgtvAQLGSVgeryataievaagnrlnnvv 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1198 -------QRCVEEETRRHETQ-----LSELRVKHS--------AALDSLQEQLDNSKRAR-------------QSLEKAK 1244
Cdd:TIGR02169 554 veddavaKEAIELLKRRKAGRatflpLNKMRDERRdlsilsedGVIGFAVDLVEFDPKYEpafkyvfgdtlvvEDIEAAR 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1245 ATLEEERQ-NLTSELKSLQASRSESERGRKRADNQLQELSARLAQadreredreermhkLQCEIESLSGNLSSsdskslr 1323
Cdd:TIGR02169 634 RLMGKYRMvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQR--------------LRERLEGLKRELSS------- 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1324 LAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNglmerleEEEERGKELSRQIQTHSQQLTELRKQSEEVNS 1403
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE-------KLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1404 AVEAGDEIRRKLQRELDSaiqrerqkeEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDqcLAEEKAVSA 1483
Cdd:TIGR02169 766 RIEELEEDLHKLEEALND---------LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT--LEKEYLEKE 834
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1484 RLAEERDRAEADSREKETRclalsRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLR 1563
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIE-----KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1564 IQTQELEEELSeaensrlRLEVTLQALK---AQFEREISTNEE---------KGEEKRRALSKQVRELE------IQLEE 1625
Cdd:TIGR02169 910 AQIEKKRKRLS-------ELKAKLEALEeelSEIEDPKGEDEEipeeelsleDVQAELQRVEEEIRALEpvnmlaIQEYE 982
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774931 1626 ERSQRSQSVSSKKQ-LEAELQEAEAQVETANRGKEEA-MKQLRRLQGQMKEVLRELDD 1681
Cdd:TIGR02169 983 EVLKRLDELKEKRAkLEEERKAILERIEEYEKKKREVfMEAFEAINENFNEIFAELSG 1040
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
867-1211 |
2.07e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.78 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 867 RQDEEIQTREAALQKAKEQLTRAEQDYTELDRkhAQLLEEKAVLADQLQAEAELFAEAEEMRARLAsRKQELEEVLGELE 946
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADE--AKKAAEAKKKADEAKKAEEAKKADEAKKAEEA-KKADEAKKAEEKK 1546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 947 TRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQrerlgkEKKQLEERL 1026
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE------AKKAEEAKI 1620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1027 NevTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQE--QLSDLGMLSSELRGSLA 1104
Cdd:PTZ00121 1621 K--AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEakKAEEDEKKAAEALKKEA 1698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1105 QKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENErgmRERAEKQRRDLSEELEALRTELEDTLDSTAAQQ 1184
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED---KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
330 340
....*....|....*....|....*..
gi 1988774931 1185 ELRSRREAELSElqrcvEEETRRHETQ 1211
Cdd:PTZ00121 1776 EKEAVIEEELDE-----EDEKRRMEVD 1797
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
867-1416 |
2.45e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 867 RQDEEIQTREAAlqKAKEQLTRAEQDYTELDRKHAQLL---------EEKAVLADQLQAEAELFAEAEEMRARLASR--- 934
Cdd:PTZ00121 1194 RKAEDARKAEAA--RKAEEERKAEEARKAEDAKKAEAVkkaeeakkdAEEAKKAEEERNNEEIRKFEEARMAHFARRqaa 1271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 935 -KQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRE 1013
Cdd:PTZ00121 1272 iKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1014 RLGKEKKQLEERLNEVTDQLTEEEEKTKSlNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLG 1093
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKA-DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK 1430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1094 MLSSELRGSlAQKEKEITSLQGRLEE-----------EGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDL 1162
Cdd:PTZ00121 1431 KKADEAKKK-AEEAKKADEAKKKAEEakkaeeakkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1163 SEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEK 1242
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1243 AKATLEEERQNLTSE--LKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESL---SGNLSSS 1317
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEkkMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENkikAAEEAKK 1669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1318 DSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNG---LMERLEEEEERGKELSRQIQTHSQQLTEL 1394
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
570 580
....*....|....*....|..
gi 1988774931 1395 RKQSEEVNSAVEAGDEIRRKLQ 1416
Cdd:PTZ00121 1750 KKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
982-1750 |
2.80e-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: 69.23 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 982 SARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEErlnevtdqltEEEEKTKSLNKLKNKQEaviadleerl 1061
Cdd:TIGR00618 191 SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE----------ALQQTQQSHAYLTQKRE---------- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1062 KREEQGRLEQEKFKRRMESEAMEAQEQlsdlgmlsselRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSEL 1141
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELRAQEA-----------VLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1142 KEEVENERGMRERAEKQRRDLSEELEALRT---ELEDTLDSTAAQQELRSRREAELSELQRCVE-EETRRHETQLSELRV 1217
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsQEIHIRDAHEVATSIREISCQQHTLTQHIHTlQQQKTTLTQKLQSLC 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1218 KHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQnLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDRE 1297
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE-LQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1298 ERMHKLQCEIESLSGNLSSSDSKSLRLAKeisslESQLHDARELLQdeSRQKMALASRVRALEEEKNGLMERLEEEEERG 1377
Cdd:TIGR00618 479 EQIHLQETRKKAVVLARLLELQEEPCPLC-----GSCIHPNPARQD--IDNPGPLTRRMQRGEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1378 KELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSaIQRERQKEEEKERVERQRERLREEIEDMTIALQRE 1457
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR-LQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDV 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1458 RQNctalekrQKKFDQCLAEEKAVSARLAEERdraeadSREKETRCLALSRalqeaQDQKEELERanKQLRLEMEQlvnq 1537
Cdd:TIGR00618 631 RLH-------LQQCSQELALKLTALHALQLTL------TQERVREHALSIR-----VLPKELLAS--RQLALQKMQ---- 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1538 qddvgknvHELERARRTLETEAQnlrIQTQELEEELSEAENSRLRLEVTLQALKAQfeREISTNEEKGEEKRRALSKQVR 1617
Cdd:TIGR00618 687 --------SEKEQLTYWKEMLAQ---CQTLLRELETHIEEYDREFNEIENASSSLG--SDLAAREDALNQSLKELMHQAR 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1618 ELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDS- 1696
Cdd:TIGR00618 754 TVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQf 833
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774931 1697 ----EKKIQTLeAEVLHLTEELAVSERQKRQAQQERDEIAdEMVSSSSGKNVLSEEKR 1750
Cdd:TIGR00618 834 lsrlEEKSATL-GEITHQLLKYEECSKQLAQLTQEQAKII-QLSDKLNGINQIKIQFD 889
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1133-1938 |
3.12e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1133 EALSQVSELKEEV-ENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQ 1211
Cdd:PTZ00121 1091 EATEEAFGKAEEAkKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1212 LSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRsESERGRKRADNQLQELSARLAQADR 1291
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAK-KAEAVKKAEEAKKDAEEAKKAEEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1292 EREDREERMHKLQCEIESLSGNLSSSDSkslRLAKEISSLEsQLHDARELLQDESRQKMALASRvRALEEEKnglmerle 1371
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEA---RKADELKKAE-EKKKADEAKKAEEKKKADEAKK-KAEEAKK-------- 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1372 eeeerGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAiqrerqkeeekerverqrerlreeiedmt 1451
Cdd:PTZ00121 1317 -----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA----------------------------- 1362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1452 ialqRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEM 1531
Cdd:PTZ00121 1363 ----EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1532 EQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRRA 1611
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1612 LSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEA--------QVETANRGKEEAMKQLRRlqgqmKEVLRELDDSk 1683
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaeekkKAEEAKKAEEDKNMALRK-----AEEAKKAEEA- 1592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1684 vtRDDVISQSKDSEKKiqtLEAEVLHLTEELAVSERQKRQAQQERDEIademvssSSGKNVLSEEKRRldarvnqleeel 1763
Cdd:PTZ00121 1593 --RIEEVMKLYEEEKK---MKAEEAKKAEEAKIKAEELKKAEEEKKKV-------EQLKKKEAEEKKK------------ 1648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1764 eeeqtnnellTERLRKTALQVETLTVQL-QGERTLAQKAEAAREQLEKQNKELKARLGEMEGAvrgkhrmsvaaleakie 1842
Cdd:PTZ00121 1649 ----------AEELKKAEEENKIKAAEEaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA----------------- 1701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1843 tmeeqleqerqeraianklmrkteKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVE---EENSRSSAQKR 1919
Cdd:PTZ00121 1702 ------------------------KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKkkaEEAKKDEEEKK 1757
|
810
....*....|....*....
gi 1988774931 1920 KLQRELEELTDSSQTMNRE 1938
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKE 1776
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1097-1323 |
8.63e-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: 65.94 E-value: 8.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1097 SELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDT 1176
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1177 LDSTAAQ---QELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQN 1253
Cdd:COG4942 103 KEELAELlraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1254 LTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLR 1323
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1525-1831 |
1.12e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1525 KQLRLEME-QLVNQQDD---VGKNVHELERARRTLETEAQnlriQTQELEEELSEAENSRLRLEVT-LQALKAQFErEIS 1599
Cdd:TIGR02168 171 KERRKETErKLERTRENldrLEDILNELERQLKSLERQAE----KAERYKELKAELRELELALLVLrLEELREELE-ELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1600 TNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLREL 1679
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1680 DDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELA-------VSERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRL 1752
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774931 1753 DARVNQLEEELEEEQTNNELLTERLrkTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRGKHR 1831
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1019-1756 |
1.26e-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: 67.07 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1019 KKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQE----AVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDlgm 1094
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKfylrQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN--- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1095 LSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENE------------RGMRERAEKQRRDL 1162
Cdd:pfam15921 150 TVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmstmhfRSLGSAISKILREL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1163 SEELEALRTEL---EDTLDstAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAA---LDSLQEQLD----- 1231
Cdd:pfam15921 230 DTEISYLKGRIfpvEDQLE--ALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSArsqANSIQSQLEiiqeq 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1232 ----NSKRARQsLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEI 1307
Cdd:pfam15921 308 arnqNSMYMRQ-LSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1308 ESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMErleeeeergkelsRQIQTH 1387
Cdd:pfam15921 387 HKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQME-------------RQMAAI 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1388 SQQLTELRKQSeEVNSAVEAGDEIRRKLQRELDSaiqrerqkeeekerVERQRERLREEIEDMTIALQRERQNCTALEKR 1467
Cdd:pfam15921 454 QGKNESLEKVS-SLTAQLESTKEMLRKVVEELTA--------------KKMTLESSERTVSDLTASLQEKERAIEATNAE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1468 QKKFdqclaeEKAVSARLAE-ERDRAEADS-REKETRCLALSRALQEaQDQKEELERANKQlrlEMEQLVNQQddvGKNV 1545
Cdd:pfam15921 519 ITKL------RSRVDLKLQElQHLKNEGDHlRNVQTECEALKLQMAE-KDKVIEILRQQIE---NMTQLVGQH---GRTA 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1546 HELERARRTLETEAQNLRIQTQeLEEELSEAENSRLRlevTLQALKAQFEREISTNEEKGEEKRRALsKQVRELEIQLEE 1625
Cdd:pfam15921 586 GAMQVEKAQLEKEINDRRLELQ-EFKILKDKKDAKIR---ELEARVSDLELEKVKLVNAGSERLRAV-KDIKQERDQLLN 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1626 ErsqrsqSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEK------- 1698
Cdd:pfam15921 661 E------VKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKvamgmqk 734
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 1699 -------KIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKN-------VLSEEKRRLDARV 1756
Cdd:pfam15921 735 qitakrgQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNkmageleVLRSQERRLKEKV 806
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
41-86 |
1.38e-10 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 57.83 E-value: 1.38e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1988774931 41 AAKRLVWVPSEKQGFESASIREERGDEVEVElTDSQRRVTLSREEV 86
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVE-TEDGKTVTVKKDDV 45
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
862-1365 |
1.39e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.60 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 862 LLQVTRQDEEIQTREAalqkaKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEV 941
Cdd:PRK02224 189 LDQLKAQIEEKEEKDL-----HERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 942 LGELETRLEeeeergvqlanEKKKMQQNIQDLEEQLEEEESARQRlLLEKVTLEtkvkslETDLATAVEQRERLGKEKKQ 1021
Cdd:PRK02224 264 RETIAETER-----------EREELAEEVRDLRERLEELEEERDD-LLAEAGLD------DADAEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1022 LEERLNEVTDQLTEEEEKTKSLNKlknkqeaVIADLEERL--KREEQGRLeqekfkrrmESEAMEAQEQLSDlgmlsseL 1099
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLRE-------DADDLEERAeeLREEAAEL---------ESELEEAREAVED-------R 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1100 RGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALR-----TELE 1174
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1175 DT--LDSTAAQQELRSRREAELSELQRCVEEETRRHEtQLSELrVKHSAALDSLQEQLDNSKrarQSLEKAKATLEEERQ 1252
Cdd:PRK02224 463 GSphVETIEEDRERVEELEAELEDLEEEVEEVEERLE-RAEDL-VEAEDRIERLEERREDLE---ELIAERRETIEEKRE 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1253 NLTSELKSLQASRSESERGRKRAdnqlQELSARLAQADREREDREERMHKLQCEIESLsGNLSSSDSKSLRLAKEISSLE 1332
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAA----AEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLR 612
|
490 500 510
....*....|....*....|....*....|....
gi 1988774931 1333 SQLHDARElLQDESRQKMA-LASRVRALEEEKNG 1365
Cdd:PRK02224 613 EKREALAE-LNDERRERLAeKRERKRELEAEFDE 645
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1015-1359 |
1.39e-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: 65.47 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1015 LGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEerlkreeqgrleQEKfKRRMESEAMEAQEQLSdlgm 1094
Cdd:pfam19220 1 IGQRNELLRVRLGEMADRLEDLRSLKADFSQLIEPIEAILRELP------------QAK-SRLLELEALLAQERAA---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1095 lSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQ-------RRDLSEELE 1167
Cdd:pfam19220 64 -YGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQlaaeteqNRALEEENK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1168 ALRTEL----EDTLDSTAAQQELRSRR---EAELSELQRCVEE---ETRRHETQLSEL---RVKHSAALDSLQEQLDNSK 1234
Cdd:pfam19220 143 ALREEAqaaeKALQRAEGELATARERLallEQENRRLQALSEEqaaELAELTRRLAELetqLDATRARLRALEGQLAAEQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1235 RARQsleKAKATLEEERQNLTSELKSLqasrsesergrkraDNQLQELSARLAQADREREDREERMHKLQCEIESLSGNL 1314
Cdd:pfam19220 223 AERE---RAEAQLEEAVEAHRAERASL--------------RMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRL 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1988774931 1315 SSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRAL 1359
Cdd:pfam19220 286 KEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEML 330
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1185-1920 |
1.47e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1185 ELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQE--QLDNSKRARQSLEKAKATLEEERQNLTSELKSLQ 1262
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDarKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1263 ASRSESERgrkRADNQLQELSARLAQADREREDREERMHKLQCEieslsgnlSSSDSKSLRLAKEISSLESQLHDARELL 1342
Cdd:PTZ00121 1163 ARKAEEAR---KAEDAKKAEAARKAEEVRKAEELRKAEDARKAE--------AARKAEEERKAEEARKAEDAKKAEAVKK 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1343 QDESRQKmalASRVRALEEEKNGLMERLEEEEERGKELSRQ--IQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELD 1420
Cdd:PTZ00121 1232 AEEAKKD---AEEAKKAEEERNNEEIRKFEEARMAHFARRQaaIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAK 1308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1421 SAIQRERQKEEEKERVERQRERLREEIEDMtialqrerqnctalEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKE 1500
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKA--------------EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1501 TRclalSRALQEAQDQKEELERANkQLRLEMEQLVNQQDDVGKNVHELERARRtLETEAQNLRIQTQELEeelseaensr 1580
Cdd:PTZ00121 1375 EA----KKKADAAKKKAEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADE-AKKKAEEKKKADEAKK---------- 1438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1581 lrlevtlqalKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEE 1660
Cdd:PTZ00121 1439 ----------KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1661 AMKQLRRLQGQMKEVLRELDDSKVTRddvisQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSS 1740
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAK-----KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1741 GKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETlTVQLQGERTLAQKAEAAR--EQLEKQNKELKAR 1818
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE-EEKKKVEQLKKKEAEEKKkaEELKKAEEENKIK 1662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1819 LGEMEGAVRGKHRmsvAALEAKIEtmeeqleqerqeraianklmRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLK 1898
Cdd:PTZ00121 1663 AAEEAKKAEEDKK---KAEEAKKA--------------------EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
|
730 740
....*....|....*....|....*.
gi 1988774931 1899 QLKRQLEE----VEEENSRSSAQKRK 1920
Cdd:PTZ00121 1720 ELKKAEEEnkikAEEAKKEAEEDKKK 1745
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
864-1275 |
2.43e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 864 QVTRQDEEIQTREAalqKAKEQLTRAEQDYTELDRKHAQLLEEKA---VLADQLQAE-AELFAEAEEMRARLASRKQELE 939
Cdd:PTZ00121 1346 EAAKAEAEAAADEA---EAAEEKAEAAEKKKEEAKKKADAAKKKAeekKKADEAKKKaEEDKKKADELKKAAAAKKKADE 1422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 940 EVLGELETRLEEEEERGVQLAN---------EKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLET----DLA 1006
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKkadeakkkaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAkkkaDEA 1502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1007 TAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEA-VIADLEERLKREEQGRLEQEKFKRRMESEAMEA 1085
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK 1582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1086 QEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRE-----------R 1154
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEelkkaeeenkiK 1662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1155 AEKQRRDLSEE---LEALRTELEDtlDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLD 1231
Cdd:PTZ00121 1663 AAEEAKKAEEDkkkAEEAKKAEED--EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1988774931 1232 NSKRARQSLEKakatlEEERQNLTSELKSLQASRSESERGRKRA 1275
Cdd:PTZ00121 1741 EDKKKAEEAKK-----DEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
983-1423 |
2.63e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 983 ARQRLLLEKVTLETKvkslETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKtksLNKLKNKQEAVIADLEERLK 1062
Cdd:COG4913 272 AELEYLRAALRLWFA----QRRLELLEAELEELRAELARLEAELERLEARLDALREE---LDELEAQIRGNGGDRLEQLE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1063 REEQgRLEQEKfkRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELK 1142
Cdd:COG4913 345 REIE-RLEREL--EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1143 EEVENERgmrERAEKQRRDLSEELEALRTELEDTLDST----------------------AAQQELRSRR------EAEL 1194
Cdd:COG4913 422 RELEAEI---ASLERRKSNIPARLLALRDALAEALGLDeaelpfvgelievrpeeerwrgAIERVLGGFAltllvpPEHY 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1195 SELQRCVEE------------ETRRHETQLS---------ELRVKHSAALDSLQ---------------EQLDNSKRA-- 1236
Cdd:COG4913 499 AAALRWVNRlhlrgrlvyervRTGLPDPERPrldpdslagKLDFKPHPFRAWLEaelgrrfdyvcvdspEELRRHPRAit 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1237 --------------------RQSL------EKAKATLEEERQNLTSELKSLQASRSESERgRKRADNQLQELSARLAQAD 1290
Cdd:COG4913 579 ragqvkgngtrhekddrrriRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALEA-ELDALQERREALQRLAEYS 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1291 REREDREERMHKLQcEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLmerl 1370
Cdd:COG4913 658 WDEIDVASAEREIA-ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL---- 732
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1988774931 1371 eeEEERGKELSRQIQTHSQQLTELRKQseevnsavEAGDEIRRKLQRELDSAI 1423
Cdd:COG4913 733 --QDRLEAAEDLARLELRALLEERFAA--------ALGDAVERELRENLEERI 775
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
957-1730 |
3.29e-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: 65.51 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 957 VQLANEKKKMQQNIQDLEEQLEEEESARQRLLL--EKVTLETKVKSLET-DLATAVEQRERLGKEKKQLEERLNEVTDQL 1033
Cdd:pfam05483 95 VSIEAELKQKENKLQENRKIIEAQRKAIQELQFenEKVSLKLEEEIQENkDLIKENNATRHLCNLLKETCARSAEKTKKY 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1034 TEEEEKTKSLN-KLKNKQEAVIADLEERLKREEQGRLEQEkFKRRMESEAMEAQEQlsdlgmlssELRGSLAQKEKEITS 1112
Cdd:pfam05483 175 EYEREETRQVYmDLNNNIEKMILAFEELRVQAENARLEMH-FKLKEDHEKIQHLEE---------EYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1113 LQGRLEEEGARRAEAQRSLREALSQVSELKEEVE-NERGMRERAEKQRRdLSEELEALRTELEDTLDSTAAQQElrsrre 1191
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLLEESRDKANQLEEKTKlQDENLKELIEKKDH-LTKELEDIKMSLQRSMSTQKALEE------ 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1192 aELSELQRCVEEETRRHETQLSELrvkhsaaldslqeqldNSKRARQSLekakatLEEERQNLTSELKSLQasRSESERG 1271
Cdd:pfam05483 318 -DLQIATKTICQLTEEKEAQMEEL----------------NKAKAAHSF------VVTEFEATTCSLEELL--RTEQQRL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1272 RKRADnQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSsdskslrlakeisslesqlhdaRELLQDESRQKMA 1351
Cdd:pfam05483 373 EKNED-QLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE----------------------DEKLLDEKKQFEK 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1352 LASRVRALEEEKNGLMerleeeeergkelsrqiQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEE 1431
Cdd:pfam05483 430 IAEELKGKEQELIFLL-----------------QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1432 EKERVERQRERLREEIEDMTIALQRERQ---NCTALEKRQKKFDQCLaEEKAVSARLAEERDRAEADSREKETRClalsr 1508
Cdd:pfam05483 493 HCDKLLLENKELTQEASDMTLELKKHQEdiiNCKKQEERMLKQIENL-EEKEMNLRDELESVREEFIQKGDEVKC----- 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1509 ALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQ 1588
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELA 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1589 ALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRL 1668
Cdd:pfam05483 647 SAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSE 726
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 1669 QGQMKEVLRELDDSKVTRddvisqskdsEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDE 1730
Cdd:pfam05483 727 LGLYKNKEQEQSSAKAAL----------EIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
870-1276 |
3.75e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 870 EEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEaelfaeaeemRARLASRKQELEEVLGELETRL 949
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA----------REAVEDRREEIEELEEEIEELR 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 950 EEEEERGVQLANekkkmqqniqdleeqleeEESARQRLLLEKVTLETKVKSLETDLATAveqRERLGKEKKQLEERLNEV 1029
Cdd:PRK02224 398 ERFGDAPVDLGN------------------AEDFLEELREERDELREREAELEATLRTA---RERVEEAEALLEAGKCPE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1030 TDQLTEEEEKTKSLNKLKNKqeavIADLEERLkreEQGRLEQEKFKRRMES--EAMEAQEQLSDLGMLSSELRGSLAQKE 1107
Cdd:PRK02224 457 CGQPVEGSPHVETIEEDRER----VEELEAEL---EDLEEEVEEVEERLERaeDLVEAEDRIERLEERREDLEELIAERR 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1108 KEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEAL---RTELEDTLDSTAAQQ 1184
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLeriRTLLAAIADAEDEIE 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1185 ELRSRREAeLSELQRCVEEETRRHETQLSELRVKH-SAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQA 1263
Cdd:PRK02224 610 RLREKREA-LAELNDERRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
410
....*....|...
gi 1988774931 1264 SRSESERGRKRAD 1276
Cdd:PRK02224 689 ELEELEELRERRE 701
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1193-1942 |
4.07e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 65.14 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1193 ELSELQRCVEEETRRHETQLSELR---VKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELkslQASRSESE 1269
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRqsvIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHEL---EAAKCLKE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1270 RGRKRADNQLQEL-------SARLAQADREREDREERMHKLQCEIESLSG----NLSSSDSKSLR-LAKEISSLESQL-- 1335
Cdd:pfam15921 163 DMLEDSNTQIEQLrkmmlshEGVLQEIRSILVDFEEASGKKIYEHDSMSTmhfrSLGSAISKILReLDTEISYLKGRIfp 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1336 -HDARELLQDESRQKMAL-----ASRVRAL----EEEKNGLMERLEEEEERGKELSRQI-----QTHSQQLTELRKQSEE 1400
Cdd:pfam15921 243 vEDQLEALKSESQNKIELllqqhQDRIEQLisehEVEITGLTEKASSARSQANSIQSQLeiiqeQARNQNSMYMRQLSDL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1401 VNSAVEAGDEIRrKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTA-LEKRQKKfdqcLAEEK 1479
Cdd:pfam15921 323 ESTVSQLRSELR-EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAdLHKREKE----LSLEK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1480 AVSARLAEeRD----------RAEADSREKETRCL-ALSRALQ-EAQDQKEELERA--NKQLRLE-----MEQLVNQQDD 1540
Cdd:pfam15921 398 EQNKRLWD-RDtgnsitidhlRRELDDRNMEVQRLeALLKAMKsECQGQMERQMAAiqGKNESLEkvsslTAQLESTKEM 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1541 VGKNVHELERARRTLETEAQNLR-----IQTQELEEELSEAENSRLRLEVTLQALKAQFEReistNEEkgeEKRRALSKQ 1615
Cdd:pfam15921 477 LRKVVEELTAKKMTLESSERTVSdltasLQEKERAIEATNAEITKLRSRVDLKLQELQHLK----NEG---DHLRNVQTE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1616 VRELEIQLEEERSQRSQSvssKKQLEAELQEAEAQVETANRGKEEAMKqlrrLQGQMKEVLRELDDSKVTRDDVISQSKD 1695
Cdd:pfam15921 550 CEALKLQMAEKDKVIEIL---RQQIENMTQLVGQHGRTAGAMQVEKAQ----LEKEINDRRLELQEFKILKDKKDAKIRE 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1696 SEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEkrrldarvnqleeeleeeqtnNELLTE 1775
Cdd:pfam15921 623 LEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSED---------------------YEVLKR 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1776 RLRKTALQVETLTVQLQgertlaQKAEAAREQLEKQNKELKArlgeMEGAvrGKHRMSVAALEAKIETmeeqlEQERQER 1855
Cdd:pfam15921 682 NFRNKSEEMETTTNKLK------MQLKSAQSELEQTRNTLKS----MEGS--DGHAMKVAMGMQKQIT-----AKRGQID 744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1856 AIANKLmrkteKKLKEVMMQAEDERRHadqyreqldksmvrlkqLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTM 1935
Cdd:pfam15921 745 ALQSKI-----QFLEEAMTNANKEKHF-----------------LKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRL 802
|
....*..
gi 1988774931 1936 NREISSL 1942
Cdd:pfam15921 803 KEKVANM 809
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
983-1729 |
4.37e-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: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 983 ARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAV------IAD 1056
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIehnlskIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1057 LEERLKREEQGRLEQEKFKRRMESEAME----AQEQLSD----------------------LGMLSSELRgSLAQKEKEI 1110
Cdd:TIGR00606 267 LDNEIKALKSRKKQMEKDNSELELKMEKvfqgTDEQLNDlyhnhqrtvrekerelvdcqreLEKLNKERR-LLNQEKTEL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1111 TSLQGRLEEEGARRAEAQR---SLREALSQVSEL---KEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQ 1184
Cdd:TIGR00606 346 LVEQGRLQLQADRHQEHIRardSLIQSLATRLELdgfERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1185 ELRSRREAELSELQRCVEEETRRHETQLSELRVKHSaALDSLQEQLDNSKRARQSLEKAKATLEEERQN-----LTSELK 1259
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIK-ELQQLEGSSDRILELDQELRKAERELSKAEKNsltetLKKEVK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1260 SLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHK---------------------------LQCEIESLSG 1312
Cdd:TIGR00606 505 SLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKdeqirkiksrhsdeltsllgyfpnkkqLEDWLHSKSK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1313 NLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRV------RALEEEKNGLMERLEEEEERGKELSRQIQT 1386
Cdd:TIGR00606 585 EINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAV 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1387 HSQQLTELRKQSEEVNSAVEAGDEIRRKLQrELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNctALEK 1466
Cdd:TIGR00606 665 YSQFITQLTDENQSCCPVCQRVFQTEAELQ-EFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQS--IIDL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1467 RQKKFDQCLAEEKAVSARLAEERDRAEADSREKET---------RCLALSRALQEAQDQKEELERANKQLRLEMeqlvnQ 1537
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTimpeeesakVCLTDVTIMERFQMELKDVERKIAQQAAKL-----Q 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1538 QDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQfEREISTNEEKG---EEKRRALSK 1614
Cdd:TIGR00606 817 GSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE-KLQIGTNLQRRqqfEEQLVELST 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1615 QVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAM----KQLRRLQGQMKEVLRELDDSKvtrDDvi 1690
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVndikEKVKNIHGYMKDIENKIQDGK---DD-- 970
|
810 820 830
....*....|....*....|....*....|....*....
gi 1988774931 1691 sQSKDSEKKIQTLEAEvlhlteelaVSERQKRQAQQERD 1729
Cdd:TIGR00606 971 -YLKQKETELNTVNAQ---------LEECEKHQEKINED 999
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1639-1928 |
4.59e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1639 QLEAELQEAEAQVETANRGKEeAMKQLRRLQGQMKevLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSE 1718
Cdd:COG1196 197 ELERQLEPLERQAEKAERYRE-LKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1719 RQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLA 1798
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1799 QKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKK------LKEV 1872
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELeeleeaLAEL 433
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774931 1873 MMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKLQRELEEL 1928
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1452-1705 |
6.23e-10 |
|
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: 64.37 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1452 IALQRERQ-NCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLE 1530
Cdd:pfam17380 342 MAMERERElERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1531 MEQLVNQQDDVGK---NVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVtlqalkaqfEREISTNEEKGEE 1607
Cdd:pfam17380 422 MEQIRAEQEEARQrevRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL---------EKEKRDRKRAEEQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1608 KRRALSKQVRE-LEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELD--DSKV 1684
Cdd:pfam17380 493 RRKILEKELEErKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSrlEAME 572
|
250 260
....*....|....*....|.
gi 1988774931 1685 TRDDVISQSKDSEKKIQTLEA 1705
Cdd:pfam17380 573 REREMMRQIVESEKARAEYEA 593
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1032-1809 |
8.39e-10 |
|
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: 64.22 E-value: 8.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1032 QLTEEEEK--TKSLNKLKNKQEAVIADLEeRLKREEQGR---LEQEKFKRRMESEAMEAQEQLSDLgmLSSELRGSLAQK 1106
Cdd:TIGR00618 108 QLYLEQKKgrGRILAAKKSETEEVIHDLL-KLDYKTFTRvvlLPQGEFAQFLKAKSKEKKELLMNL--FPLDQYTQLALM 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1107 EKEIT-SLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQE 1185
Cdd:TIGR00618 185 EFAKKkSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1186 LRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQ-------LDNSKRARQSLEKAKATLEEERQNLTSEL 1258
Cdd:TIGR00618 265 LRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQaqrihteLQSKMRSRAKLLMKRAAHVKQQSSIEEQR 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1259 KSLQASRSESERGRKRADNQLqelsARLAQaDREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDA 1338
Cdd:TIGR00618 345 RLLQTLHSQEIHIRDAHEVAT----SIREI-SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1339 RELlqdesRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEvnsaveagdEIRRKLQRE 1418
Cdd:TIGR00618 420 RDL-----QGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ---------TKEQIHLQE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1419 LDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRErQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSRE 1498
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG-PLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQ 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1499 ketrclalsraLQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAEN 1578
Cdd:TIGR00618 565 -----------MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1579 SRlRLEVTLQALKAQFEREIstnEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGK 1658
Cdd:TIGR00618 634 LQ-QCSQELALKLTALHALQ---LTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1659 EEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQS-------KDSEKKIQTLEAEVLHLTEELAV----SERQKRQAQQE 1727
Cdd:TIGR00618 710 ETHIEEYDREFNEIENASSSLGSDLAAREDALNQSlkelmhqARTVLKARTEAHFNNNEEVTAALqtgaELSHLAAEIQF 789
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1728 RDEIADEMVSSSSGKNVLSEEKRRLDARVnQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQ 1807
Cdd:TIGR00618 790 FNRLREEDTHLLKTLEAEIGQEIPSDEDI-LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQ 868
|
..
gi 1988774931 1808 LE 1809
Cdd:TIGR00618 869 AK 870
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1223-1947 |
1.59e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.12 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1223 LDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHK 1302
Cdd:TIGR04523 42 LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1303 LQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGL---MERLEEEEERGKE 1379
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIqknIDKIKNKLLKLEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1380 LSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELdsaiqrerqkeeekervERQRERLREEIEDMTIALQRERQ 1459
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI-----------------NEKTTEISNTQTQLNQLKDEQNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1460 NCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLalsralqeaQDQKEELERANKQLRlemeQLVNQQD 1539
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWN---------KELKSELKNQEKKLE----EIQNQIS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1540 DVGKNVHELERARRTLETEAQNLRiqtqeleeelseAENSRLRLEvtLQALKAQFEREISTNEEKGEEKRRaLSKQVREL 1619
Cdd:TIGR04523 332 QNNKIISQLNEQISQLKKELTNSE------------SENSEKQRE--LEEKQNEIEKLKKENQSYKQEIKN-LESQINDL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1620 EIQLEEersqrsqsvssKKQLEAELQEaeaQVETANRGKEEAMKQLRRLqgqmkevLRELDDSKVTRDDVISQSKDSEKK 1699
Cdd:TIGR04523 397 ESKIQN-----------QEKLNQQKDE---QIKKLQQEKELLEKEIERL-------KETIIKNNSEIKDLTNQDSVKELI 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1700 IQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNelltERLRK 1779
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI----EKLES 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1780 TALQVETLTVQLQGErTLAQKAEAAREQLEKQNKELKARLGEMegavrgKHrmsvaaleakietmeeqleqerqeraiAN 1859
Cdd:TIGR04523 532 EKKEKESKISDLEDE-LNKDDFELKKENLEKEIDEKNKEIEEL------KQ---------------------------TQ 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1860 KLMRKTEKKLKEVMMQAEDERrhaDQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREI 1939
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEK---KDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
....*...
gi 1988774931 1940 SSLRNQLS 1947
Cdd:TIGR04523 655 KEIRNKWP 662
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1483-1947 |
1.71e-09 |
|
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: 63.27 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1483 ARLAEERDRAEADSREKETrclaLSRALQEAQDQKEELERANKQLRLE----------MEQLVNQQDDVGKnvhELERAR 1552
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKK----MQQHIQDLEEQLDEEEAARQKLQLEkvtteakikkLEEDILLLEDQNS---KLSKER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1553 RTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKgEEKRRALSKQVRELEIQLEEERSQRSQ 1632
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQEL-EKAKRKLEGESTDLQEQIAELQAQIAE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1633 SVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTE 1712
Cdd:pfam01576 234 LRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1713 ELAVSERQKRQAQQERDEIademvssssgKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLR-------KTALQVE 1785
Cdd:pfam01576 314 TTAAQQELRSKREQEVTEL----------KKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKrnkanleKAKQALE 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1786 TLTVQLQGE-RTLAQ---KAEAAREQLEKQNKELKARLGEMEgAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKL 1861
Cdd:pfam01576 384 SENAELQAElRTLQQakqDSEHKRKKLEGQLQELQARLSESE-RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1862 MRKTEKKLKEVMMQAEDERRHADQYREQLdksmvrlkqlkRQLEEveeensrssaQKRKLQRELEELTDSSQTMNREISS 1941
Cdd:pfam01576 463 VSSLESQLQDTQELLQEETRQKLNLSTRL-----------RQLED----------ERNSLQEQLEEEEEAKRNVERQLST 521
|
....*.
gi 1988774931 1942 LRNQLS 1947
Cdd:pfam01576 522 LQAQLS 527
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
864-1406 |
2.06e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 864 QVTRQDEEIQTREAALQKAKEQLTRAEqdytELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKqeleevlg 943
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAA----EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK-------- 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 944 eletrleeeeergvqlANEKKKMQQniqdleeqleeeesarqrllLEKVTLETKVKSLEtdLATAVEQRERLGKEKKQLE 1023
Cdd:PTZ00121 1387 ----------------AEEKKKADE--------------------AKKKAEEDKKKADE--LKKAAAAKKKADEAKKKAE 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1024 ERlnEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSL 1103
Cdd:PTZ00121 1429 EK--KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1104 AQKEK--EITSLQGRLEEEGARRAEAQRSLREAlsqvsELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTA 1181
Cdd:PTZ00121 1507 EAKKKadEAKKAEEAKKADEAKKAEEAKKADEA-----KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1182 AQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAAldslqEQLDNSKRARQSLEKAKATLEEERQNLTSELKSL 1261
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-----EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1262 QASRSESERGRKRADNQLQElsARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDAREL 1341
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKKK--AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774931 1342 LQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQltELRKQSEEVNSAVE 1406
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVD 1797
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1096-1674 |
2.18e-09 |
|
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: 62.85 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1096 SSELRGSLAQKEKeiTSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRdlsEELEALRTELED 1175
Cdd:pfam07111 52 SLELEGSQALSQQ--AELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQ---AEAEGLRAALAG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1176 tldSTAAQQELRSRREAELSELQRCveeetrrHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEE----- 1250
Cdd:pfam07111 127 ---AEMVRKNLEEGSQRELEEIQRL-------HQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQlaeaq 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1251 ------RQNLTSELKSLQASRSESERGRKRADNQL-------------QELSARLAQADREREDREERMHKLQCEIESLS 1311
Cdd:pfam07111 197 keaellRKQLSKTQEELEAQVTLVESLRKYVGEQVppevhsqtwelerQELLDTMQHLQEDRADLQATVELLQVRVQSLT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1312 GNLSSSDSKSLRLAKEISSLESQL-HDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKElsrQIQTHSQQ 1390
Cdd:pfam07111 277 HMLALQEEELTRKIQPSDSLEPEFpKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQE---QVTSQSQE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1391 LTELRKQSEEVNSAVEAGDEIRRKLQRELDSAiqrerqkeeeKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKK 1470
Cdd:pfam07111 354 QAILQRALQDKAAEVEVERMSAKGLQMELSRA----------QEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTR 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1471 FDQCLAEEKAVSARLAEERdRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQ------------- 1537
Cdd:pfam07111 424 VEQAVARIPSLSNRLSYAV-RKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREErnrldaelqlsah 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1538 --QDDVGKNVHELERARRTLETEAQNLRiqtQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKR---RAL 1612
Cdd:pfam07111 503 liQQEVGRAREQGEAERQQLSEVAQQLE---QELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEiygQAL 579
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 1613 SKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKE 1674
Cdd:pfam07111 580 QEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARK 641
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
860-1274 |
2.59e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 860 KPLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAE-AELFAEAEEMRARLASRKQEL 938
Cdd:PRK03918 345 KKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEiEEEISKITARIGELKKEIKEL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 939 EEVLGELETRLEEEEERGVQLANEKKKMqqniqdleeqleeeesarqrlLLEKVTLEtkVKSLETDLATAVEQRERLGKE 1018
Cdd:PRK03918 425 KKAIEELKKAKGKCPVCGRELTEEHRKE---------------------LLEEYTAE--LKRIEKELKEIEEKERKLRKE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1019 KKQLEE---------RLNEVTDQLTEEEEKTKSLNKLKNKQEAViadlEERLKREEQGRLEQEkfKRRMESEAMEAQEQL 1089
Cdd:PRK03918 482 LRELEKvlkkeseliKLKELAEQLKELEEKLKKYNLEELEKKAE----EYEKLKEKLIKLKGE--IKSLKKELEKLEELK 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1090 SDLGMLSSELRgslaQKEKEITSLQGRLEEEGArraeaqRSLREALSQVSELkEEVENERGMRERAEKQRRDLSEELEAL 1169
Cdd:PRK03918 556 KKLAELEKKLD----ELEEELAELLKELEELGF------ESVEELEERLKEL-EPFYNEYLELKDAEKELEREEKELKKL 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1170 RTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRhetQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEE 1249
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE---ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE 701
|
410 420
....*....|....*....|....*...
gi 1988774931 1250 ERQNLTS---ELKSLQASRSESERGRKR 1274
Cdd:PRK03918 702 ELEEREKakkELEKLEKALERVEELREK 729
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
821-1289 |
2.69e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 821 RKAFLKKQQQLSALRVMQRNCAAYLKLRNWQwwRLFTKVKPLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKH 900
Cdd:COG4913 241 HEALEDAREQIELLEPIRELAERYAAARERL--AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 901 AQLLEEKAVLADQLQaeAELFAEAEEMRARLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEE 980
Cdd:COG4913 319 DALREELDELEAQIR--GNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 981 ESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEeektkslnkLKNKQEAV--IADLE 1058
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA---------LGLDEAELpfVGELI 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1059 ERLKREEQGRLEQEK----FKRRM------ESEAMEAQEQLSDLGMLSSE----LRGSLAQKEKEITSLQGRLE-EEGAR 1123
Cdd:COG4913 468 EVRPEEERWRGAIERvlggFALTLlvppehYAAALRWVNRLHLRGRLVYErvrtGLPDPERPRLDPDSLAGKLDfKPHPF 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1124 RAEAQRSLREALS-----QVSELKEE---------VENERGMRE---------------RAEKQRRDLSEELEALRTELE 1174
Cdd:COG4913 548 RAWLEAELGRRFDyvcvdSPEELRRHpraitragqVKGNGTRHEkddrrrirsryvlgfDNRAKLAALEAELAELEEELA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1175 DTLDSTAAQQELRSRREAELSELQRC------------VEEETRRHETQLSELRvKHSAALDSLQEQLDNSKRARQSLEK 1242
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRLaeyswdeidvasAEREIAELEAELERLD-ASSDDLAALEEQLEELEAELEELEE 706
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 1243 AKATLEEERQNLTSELKSLQASRSESER-----GRKRADNQLQELSARLAQA 1289
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEEELDELQDrleaaEDLARLELRALLEERFAAA 758
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
867-1285 |
2.69e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.67 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 867 RQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEaelfaeaeemRARLasrkqeleevlgele 946
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAA----------SDHL--------------- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 947 trleeeeergvQLANEKKKMQQNIQdleeqleeeesaRQRLLLEKvtLETKVKSLETDLATAVEQRERLGKEKKQLEERL 1026
Cdd:PRK04863 338 -----------NLVQTALRQQEKIE------------RYQADLEE--LEERLEEQNEVVEEADEQQEENEARAEAAEEEV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1027 NEVTDQLTE-----EEEKTKSLnklkNKQEAVIAdLEERLKREEQGRLEQEKFKRRMesEAMEAQEQLSDLGMLSSELRG 1101
Cdd:PRK04863 393 DELKSQLADyqqalDVQQTRAI----QYQQAVQA-LERAKQLCGLPDLTADNAEDWL--EEFQAKEQEATEELLSLEQKL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1102 SLAQKEKE--------ITSLQGRLEeegarRAEAQRSLREALSQVSELKEEVENERGMR------ERAEKQRRDLSEELE 1167
Cdd:PRK04863 466 SVAQAAHSqfeqayqlVRKIAGEVS-----RSEAWDVARELLRRLREQRHLAEQLQQLRmrlselEQRLRQQQRAERLLA 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1168 ALRTELEDTLDSTAAQQELRSRREAELSELQRCVEE------ETRRHETQLSELRVKHSA----------ALDSLQEQLD 1231
Cdd:PRK04863 541 EFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEarerrmALRQQLEQLQARIQRLAArapawlaaqdALARLREQSG 620
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1988774931 1232 NSKRARQSlekakatLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSAR 1285
Cdd:PRK04863 621 EEFEDSQD-------VTEYMQQLLERERELTVERDELAARKQALDEEIERLSQP 667
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
864-1541 |
3.73e-09 |
|
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: 62.01 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 864 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQL---LEEKAVLADQLQaeaelfaeaeemrARLASRKQELEE 940
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELereIEEERKRRDKLT-------------EEYAELKEELED 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 941 VLGELEtrleEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQrerlgkeKK 1020
Cdd:TIGR02169 369 LRAELE----EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK-------IN 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1021 QLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLeerlkREEQGRLEQEKFKRRMESEAMEAQEQLSDLG------- 1093
Cdd:TIGR02169 438 ELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL-----KEEYDRVEKELSKLQRELAEAEAQARASEERvrggrav 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1094 --MLSSELR---GSLAQ----KEKEITSLQ----GRL-----EEEG--------ARRAEAQRS-------LREALSQVSE 1140
Cdd:TIGR02169 513 eeVLKASIQgvhGTVAQlgsvGERYATAIEvaagNRLnnvvvEDDAvakeaielLKRRKAGRAtflplnkMRDERRDLSI 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1141 LKEE---------VENERGMRERAEKQRRD--LSEELEALRTELED----TLDS--------------TAAQQELRSRRE 1191
Cdd:TIGR02169 593 LSEDgvigfavdlVEFDPKYEPAFKYVFGDtlVVEDIEAARRLMGKyrmvTLEGelfeksgamtggsrAPRGGILFSRSE 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1192 -AELSELQRCVEEETRRHETQLSELRvKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESER 1270
Cdd:TIGR02169 673 pAELQRLRERLEGLKRELSSLQSELR-RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1271 GRKRADNQLQELSARLAQadreredREERMHKLQCEIESLSGNLSSSDSKSLRlaKEISSLESQLHDARELLQDESRQKM 1350
Cdd:TIGR02169 752 EIENVKSELKELEARIEE-------LEEDLHKLEEALNDLEARLSHSRIPEIQ--AELSKLEEEVSRIEARLREIEQKLN 822
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1351 ALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKE 1430
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1431 EEKERVERQRERLREEIEDMTIALQRERQNCTALEkRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLA----- 1505
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLaiqey 981
|
730 740 750
....*....|....*....|....*....|....*...
gi 1988774931 1506 --LSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDV 1541
Cdd:TIGR02169 982 eeVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
868-1417 |
3.76e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 868 QDEEIQTReaaLQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGE--- 944
Cdd:PRK03918 187 RTENIEEL---IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKire 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 945 LETRLEEEEERGVQLaNEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQ---RERLGKEKKQ 1021
Cdd:PRK03918 264 LEERIEELKKEIEEL-EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERikeLEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1022 LEERLNEVTDQLTEEEEKTKSLNKLKNKQEAViadleERLKREEQGrLEQEKFKRRMES---EAMEAQEQLSDLGMLSSE 1098
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAKAKKEEL-----ERLKKRLTG-LTPEKLEKELEElekAKEEIEEEISKITARIGE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1099 LRGSLAQKEKEITSLQG----------RLEEEgaRRAEAQRSLREALSQVS-ELKEEVENERGMRERAEKQRRDLSEELE 1167
Cdd:PRK03918 417 LKKEIKELKKAIEELKKakgkcpvcgrELTEE--HRKELLEEYTAELKRIEkELKEIEEKERKLRKELRELEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1168 ALRteLEDTLDS-TAAQQELRSRREAELSElqrcVEEETRRHETQLSELRVKHSAALDSLqEQLDNSKRARQSLEKAKAT 1246
Cdd:PRK03918 495 LIK--LKELAEQlKELEEKLKKYNLEELEK----KAEEYEKLKEKLIKLKGEIKSLKKEL-EKLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1247 LEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAK 1326
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1327 EISSLESQLHDarELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQThsqqLTELRKQSEEVNSAVE 1406
Cdd:PRK03918 648 ELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE----REKAKKELEKLEKALE 721
|
570
....*....|.
gi 1988774931 1407 AGDEIRRKLQR 1417
Cdd:PRK03918 722 RVEELREKVKK 732
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1032-1260 |
1.03e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1032 QLTEEEEKTKSLNKLKNKqeavIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEIT 1111
Cdd:COG4942 18 QADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1112 SLQGRLEEegaRRAEAQRSLREA--LSQVSELK--------EEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTA 1181
Cdd:COG4942 94 ELRAELEA---QKEELAELLRALyrLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774931 1182 AQQELRSRREAELSELQRCVEEETRRHETQLSELRvkhsAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKS 1260
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLE----KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1132-1671 |
1.17e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1132 REALSQVSELKEEVENERGMRERAEKQRR---------DLSEELEALRTELE------DTLDSTAAQQELR------SRR 1190
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqiellepirELAERYAAARERLAeleylrAALRLWFAQRRLElleaelEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1191 EAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESER 1270
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1271 G-----------RKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSL----RLAKEISSLESQL 1335
Cdd:COG4913 381 EfaalraeaaalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLalrdALAEALGLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1336 HDARELLQ---DESRQKMAL-----------------ASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLtelr 1395
Cdd:COG4913 461 PFVGELIEvrpEEERWRGAIervlggfaltllvppehYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSL---- 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1396 kqSEEVNSAV-EAGDEIRRKLQRELD--------------SAIQRERQKEEEKERVERQRERLREEI-------EDMTIA 1453
Cdd:COG4913 537 --AGKLDFKPhPFRAWLEAELGRRFDyvcvdspeelrrhpRAITRAGQVKGNGTRHEKDDRRRIRSRyvlgfdnRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1454 LQRERQNCTA-LEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRclALSRALQEAQDQKEELERAN---KQLRL 1529
Cdd:COG4913 615 LEAELAELEEeLAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA--SAEREIAELEAELERLDASSddlAALEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1530 EMEQLVNQQDDVGKNVHELERARRTLETEAQnlRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREIStnEEKGEEKR 1609
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELE--QAEEELDELQDRLEAAEDLARLELRALLEERFAAALG--DAVERELR 768
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774931 1610 RALSKQVRELEIQLEEERSQRSQSVSS-KKQLEAELQEAEAQVETAnrgkEEAMKQLRRLQGQ 1671
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESL----PEYLALLDRLEED 827
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1050-1289 |
1.26e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1050 QEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQR 1129
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1130 SLREALSQVSELkeevenergMRErAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEetrrhe 1209
Cdd:COG4942 98 ELEAQKEELAEL---------LRA-LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1210 tqLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQA 1289
Cdd:COG4942 162 --LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1056-1930 |
1.38e-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: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1056 DLEERLKREEQGR-LEQEKFKRRMESEAMEAQ------EQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQ 1128
Cdd:pfam12128 213 PPKSRLNRQQVEHwIRDIQAIAGIMKIRPEFTklqqefNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1129 RSLREALSQV--------SELKEEVENERGMRERAEKQ-RRDLSEELEALRTELEDtLDSTAAQQELRSRREAELSELQR 1199
Cdd:pfam12128 293 RTLDDQWKEKrdelngelSAADAAVAKDRSELEALEDQhGAFLDADIETAAADQEQ-LPSWQSELENLEERLKALTGKHQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1200 CVEEETRRHETQLSElrvKHSAALDSLQEQLDNSKRARqslEKAKATLEEERQNLTSELKS-LQASRSESERGRKRADNQ 1278
Cdd:pfam12128 372 DVTAKYNRRRSKIKE---QNNRDIAGIKDKLAKIREAR---DRQLAVAEDDLQALESELREqLEAGKLEFNEEEYRLKSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1279 LQELSARLAQADREREDREERMHKlQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRA 1358
Cdd:pfam12128 446 LGELKLRLNQATATPELLLQLENF-DERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1359 LEEeknglmerleeeeergkelsrQIQTHSQQLTE-LRKQseevnsAVEAGDEIRRKLQRELdsaiqreRQKEEEKERVE 1437
Cdd:pfam12128 525 LEL---------------------QLFPQAGTLLHfLRKE------APDWEQSIGKVISPEL-------LHRTDLDPEVW 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1438 RQRERLREEIEDMTIALQRERQNctalekrqkkfdQCLAEEKAVSARLAeerdraeadsreketrclALSRALQEAQDQK 1517
Cdd:pfam12128 571 DGSVGGELNLYGVKLDLKRIDVP------------EWAASEEELRERLD------------------KAEEALQSAREKQ 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1518 EELErankqlrlemEQLVNQQDDVGKNVHELERARRTLETEAQNLRiqtqeleeelseaensrlRLEVTLQALKAQFERE 1597
Cdd:pfam12128 621 AAAE----------EQLVQANGELEKASREETFARTALKNARLDLR------------------RLFDEKQSEKDKKNKA 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1598 ISTNEEKGEEKRRALSKQVRELEIQL--------EEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKqlRRLQ 1669
Cdd:pfam12128 673 LAERKDSANERLNSLEAQLKQLDKKHqawleeqkEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAK--AELK 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1670 GQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEK 1749
Cdd:pfam12128 751 ALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQL 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1750 RRLDARVNQLEEEleeeqtnneLLTERLRKTALQVEtLTVQLQGERTLAQKAeaAREQLEKQNKELKARLGEMEGAV--- 1826
Cdd:pfam12128 831 ARLIADTKLRRAK---------LEMERKASEKQQVR-LSENLRGLRCEMSKL--ATLKEDANSEQAQGSIGERLAQLedl 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1827 RGKHRMSVAALEAKIETMEEQLEQERQERAIANKL-MRKTEKKLKEVMMQAEDERRHAdQYREQLDKSMVR-----LKQL 1900
Cdd:pfam12128 899 KLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWEsLREEDHYQNDKGIRLLDYRKLV-PYLEQWFDVRVPqsimvLREQ 977
|
890 900 910
....*....|....*....|....*....|....*...
gi 1988774931 1901 KRQLEEVEEE--------NSRSSAQKRKLQRELEELTD 1930
Cdd:pfam12128 978 VSILGVDLTEfydvladfDRRIASFSRELQREVGEEAF 1015
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1010-1217 |
1.39e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.03 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1010 EQRERLGKEKKQLEERLNEVTDQLTEEEEKtksLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQL 1089
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAA---LEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1090 SDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVEN-ERGMRERAEKQRRDLSEELEA 1168
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAlRAQLQQEAQRILASLEAELEA 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774931 1169 LRT---ELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHET---QLSELRV 1217
Cdd:COG3206 325 LQAreaSLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESllqRLEEARL 379
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1050-1560 |
1.51e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1050 QEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLsdlgmlsselRGSLAQKEKEITSLQGRLEEEGARRAEAQR 1129
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEE----------LKEAEEKEEEYAELQEELEELEEELEELEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1130 SLREALSQVSELKEEVENERGMRER--AEKQRRDLSEELEALRTELEDTLDstaaQQELRSRREAELSELQrcveeetRR 1207
Cdd:COG4717 110 ELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQ-------EE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1208 HETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLqasrsESERGRKRADNQLQELSARLA 1287
Cdd:COG4717 179 LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL-----ENELEAAALEERLKEARLLLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1288 QADReredreermhklqceIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNgLM 1367
Cdd:COG4717 254 IAAA---------------LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE-LE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1368 ERLEEEEERGKELSRQIQTHsqQLTELRKQSEEVNSAVEAGDEIRRKLQREldsaiqrerqkeEEKERVERQRERLREEI 1447
Cdd:COG4717 318 EEELEELLAALGLPPDLSPE--ELLELLDRIEELQELLREAEELEEELQLE------------ELEQEIAALLAEAGVED 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1448 EDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKEtrclaLSRALQEAQDQKEELERANKQL 1527
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE-----LEEELEELEEELEELREELAEL 458
|
490 500 510
....*....|....*....|....*....|...
gi 1988774931 1528 RLEMEQLVNqQDDVGKNVHELERARRTLETEAQ 1560
Cdd:COG4717 459 EAELEQLEE-DGELAELLQELEELKAELRELAE 490
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1102-1330 |
2.75e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1102 SLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVEnergmreRAEKQRRDLSEELEALRTELEDTLDSTA 1181
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-------ALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1182 AQQELRSRREAELSELQRCVEEETRRHETQL---SELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSEL 1258
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 1259 KSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISS 1330
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
985-1194 |
8.96e-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: 8.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 985 QRLLLEKVTLETKVKSLETdlataveQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKRe 1064
Cdd:COG1579 6 LRALLDLQELDSELDRLEH-------RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1065 eqgrleqekfkrrmeseameAQEQLSDlgmlsselrgslAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEE 1144
Cdd:COG1579 78 --------------------YEEQLGN------------VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEE 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1988774931 1145 VENERGMRERAEKQRRDLSEELEALRTELEDTLDS-TAAQQELRSRREAEL 1194
Cdd:COG1579 126 LAELEAELAELEAELEEKKAELDEELAELEAELEElEAEREELAAKIPPEL 176
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
870-1360 |
1.02e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 870 EEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLgeletrl 949
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRD------- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 950 EEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEV 1029
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1030 TDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFkrRMESEAMEAQEQLSDlgmlsSELRGSLAQKEKE 1109
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL--LEAGKCPECGQPVEG-----SPHVETIEEDRER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1110 ITSLQGRLEEegarrAEAQRSLREAlsQVSELKEEVENERGMRERAEkqRRDLSEEleaLRTELEDTLDSTAAQQELRSR 1189
Cdd:PRK02224 477 VEELEAELED-----LEEEVEEVEE--RLERAEDLVEAEDRIERLEE--RREDLEE---LIAERRETIEEKRERAEELRE 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1190 REAELSElqrcvEEETRRHETQLSELRV-KHSAALDSLQEQLDNSKRARQSLEKAkATLEEERQNLTSELKSLQASRSE- 1267
Cdd:PRK02224 545 RAAELEA-----EAEEKREAAAEAEEEAeEAREEVAELNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREAl 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1268 SERGRKRADnQLQELSAR---LAQADREREDREERMHKLQCE--IESLSGNLSSSDSKSLRLAKEISSLESQLhDARELL 1342
Cdd:PRK02224 619 AELNDERRE-RLAEKRERkreLEAEFDEARIEEAREDKERAEeyLEQVEEKLDELREERDDLQAEIGAVENEL-EELEEL 696
|
490
....*....|....*...
gi 1988774931 1343 QDEsrqKMALASRVRALE 1360
Cdd:PRK02224 697 RER---REALENRVEALE 711
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1462-1946 |
1.02e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1462 TALEKRQKKFDQCLAEEKAVSARLAEERDRAE--ADSREKETRCLALSRALQEA-QDQKEELERANKQLRLEMEQLVNQQ 1538
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEelEEERDDLLAEAGLDDADAEAvEARREELEDRDEELRDRLEECRVAA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1539 DDVGKNVHELERARRTLETEAQNLRiqtqeleeelseaeNSRLRLEVTLQALKAQFEREISTNEEKgEEKRRALSKQVRE 1618
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELR--------------EEAAELESELEEAREAVEDRREEIEEL-EEEIEELRERFGD 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1619 LEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAmkqlRRLQ--GQMKEVLRELDDSKVTrdDVISqskDS 1696
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA----EALLeaGKCPECGQPVEGSPHV--ETIE---ED 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1697 EKKIQTLEAEVLHLTEELAVSErqkrqaqqERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNelltER 1776
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERA----EE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1777 LRKTALQVETltvQLQGERTLAQKAEAAREQLEKQNKELKARLGEmegavrgkhrmsvaaLEAKIETMEEQLEQERQERA 1856
Cdd:PRK02224 542 LRERAAELEA---EAEEKREAAAEAEEEAEEAREEVAELNSKLAE---------------LKERIESLERIRTLLAAIAD 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1857 IANKLMRKTEKklKEVMMQAEDERrhadqyREQLDKSMVRlkqlKRQLEEVEEENSRSSAQKRKLQRE---------LEE 1927
Cdd:PRK02224 604 AEDEIERLREK--REALAELNDER------RERLAEKRER----KRELEAEFDEARIEEAREDKERAEeyleqveekLDE 671
|
490
....*....|....*....
gi 1988774931 1928 LTDSSQTMNREISSLRNQL 1946
Cdd:PRK02224 672 LREERDDLQAEIGAVENEL 690
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1012-1418 |
1.11e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1012 RERLGKEKKQLE-ERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLK-REEQGRLEQEKFKRRMESEAMEAQEQL 1089
Cdd:COG4717 48 LERLEKEADELFkPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEElEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1090 SDLGMLSSELRGSLA----------QKEKEITSLQGRLEEEGARRAEAQRSLREAL--------SQVSELKEEVENERGM 1151
Cdd:COG4717 128 LPLYQELEALEAELAelperleeleERLEELRELEEELEELEAELAELQEELEELLeqlslateEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1152 RERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELS--------------------------------ELQR 1199
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1200 CVEEETRRHETQLSEL--RVKHSAALDSLQEQldNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADN 1277
Cdd:COG4717 288 LLFLLLAREKASLGKEaeELQALPALEELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1278 Q--LQELSARLAQAD-------REREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEIS--SLESQLHDARELLQDES 1346
Cdd:COG4717 366 EelEQEIAALLAEAGvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELE 445
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 1347 RQKMALASRVRALEEEKNGLMERLEEEEERgkelsRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRE 1418
Cdd:COG4717 446 EELEELREELAELEAELEQLEEDGELAELL-----QELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
864-1275 |
2.29e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 864 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLleekavlaDQLQAEAELFAEAEEMRARLASrkqeleevLG 943
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL--------EKLLQLLPLYQELEALEAELAE--------LP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 944 ELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEeesARQRLLLEKvtlETKVKSLETDLATAVEQRERLGKEKKQLE 1023
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEE---LLEQLSLAT---EEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1024 ERLNEVTDQLTEEEEKTKSLNKLKNKQEA------------------------------------VIADLEERLKREE-- 1065
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEArlllliaaallallglggsllsliltiagvlflvlgLLALLFLLLAREKas 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1066 --QGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKE 1143
Cdd:COG4717 300 lgKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1144 EVENERGMRERAE--KQRRDLSEELEALRTELEDTLDSTAAQQELRSRR--EAELSELQRCVEEETRRHETQLSELrvkh 1219
Cdd:COG4717 380 GVEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREEL---- 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774931 1220 sAALDSLQEQLDNSKRARQsLEKAKATLEEERQNLTSELKSLQASRSESERGRKRA 1275
Cdd:COG4717 456 -AELEAELEQLEEDGELAE-LLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1220-1423 |
2.69e-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: 55.16 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1220 SAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREER 1299
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1300 MHKLQCEIESL------SGNLSS-----SDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLME 1368
Cdd:COG4942 99 LEAQKEELAELlralyrLGRQPPlalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774931 1369 RLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAI 1423
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1487-1930 |
4.34e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1487 EERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLvNQQDDVGKNVHELERARRTLETEAQNLRiQT 1566
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLE-EL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1567 QELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQE 1646
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1647 AEAQVETANrgKEEAMKQLRRLQGQMKEVLrelddSKVTRDDVISQSKDSEKKIQTLEAEVLHLteELAVSERQKRQAQQ 1726
Cdd:COG4717 232 LENELEAAA--LEERLKEARLLLLIAAALL-----ALLGLGGSLLSLILTIAGVLFLVLGLLAL--LFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1727 ERDEIADEmvssSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLtvqlqgertlaqKAEAARE 1806
Cdd:COG4717 303 EAEELQAL----PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL------------EEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1807 QLEKQNKELKARLG-EMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEvmmQAEDERRHADQ 1885
Cdd:COG4717 367 ELEQEIAALLAEAGvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE---ELEELEEELEE 443
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1988774931 1886 YREQLDKSMVRLKQLKRQLEEVEEENsRSSAQKRKLQRELEELTD 1930
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDG-ELAELLQELEELKAELRE 487
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
863-1400 |
5.77e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.97 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 863 LQVTRQDEEIQTREAALQKAKEQLTRA-------EQDYTELDRKHAQLLEE------KAVLADQLQAEAELFAEAEEMRA 929
Cdd:TIGR00618 235 LQQTQQSHAYLTQKREAQEEQLKKQQLlkqlrarIEELRAQEAVLEETQERinrarkAAPLAAHIKAVTQIEQQAQRIHT 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 930 RLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQniQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAV 1009
Cdd:TIGR00618 315 ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ--EIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLT 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1010 EQRERLGKEKKQLEERLNEVTDQLTEE----------------EEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEK 1073
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATIDTRTSAFrdlqgqlahakkqqelQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKERE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1074 FK--------RRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEI---------TSLQGRLEEEGARRAEAQRSLR---- 1132
Cdd:TIGR00618 473 QQlqtkeqihLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnpgplTRRMQRGEQTYAQLETSEEDVYhqlt 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1133 EALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQqelrsrreaelSELQRCVEEETRRHETQL 1212
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL-----------SEAEDMLACEQHALLRKL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1213 SELRVKHSAALDSLQEQldnskrarQSLEKAKATLEEERQNLTSE--LKSLQASRSESERGRKRADNQLQELSARLAQAD 1290
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCS--------QELALKLTALHALQLTLTQErvREHALSIRVLPKELLASRQLALQKMQSEKEQLT 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1291 REREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQD-ESRQKMALASRV----RALEEEKNG 1365
Cdd:TIGR00618 694 YWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLKARTeahfNNNEEVTAA 773
|
570 580 590
....*....|....*....|....*....|....*..
gi 1988774931 1366 LMERLEEE--EERGKELSRQIQTHSQQLTELRKQSEE 1400
Cdd:TIGR00618 774 LQTGAELShlAAEIQFFNRLREEDTHLLKTLEAEIGQ 810
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1454-1946 |
9.40e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1454 LQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKEtRCLALSRALQEAQDQKEELERANKQLRLEMEQ 1533
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1534 LVNQQDDVGKNVHELERARR---TLETEAQNLRIQTQELEEELSEAENSRLRLEvTLQALKAQFEREISTNEEKgEEKRR 1610
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKelkELKEKAEEYIKLSEFYEEYLDELREIEKRLS-RLEEEINGIEERIKELEEK-EERLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1611 ALSKQVRELEIQLEEeRSQRSQSVSSKKQLEAELQEAEAqvETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVI 1690
Cdd:PRK03918 342 ELKKKLKELEKRLEE-LEERHELYEEAKAKKEELERLKK--RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1691 SQSKDSEKKIQTLE--------------------------AEVLHLTEELAVSERQKRQAQQERDEIADEMVSSS--SGK 1742
Cdd:PRK03918 419 KEIKELKKAIEELKkakgkcpvcgrelteehrkelleeytAELKRIEKELKEIEEKERKLRKELRELEKVLKKESelIKL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1743 NVLSEEKRRLDARVNQLEEELEEEQTNN-ELLTERLRKTALQVETLTVQLQGERTLAQKaeaaREQLEKQNKELKARLGE 1821
Cdd:PRK03918 499 KELAEQLKELEEKLKKYNLEELEKKAEEyEKLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAE 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1822 MEGAVRGKHRMSVAALEAKIETMEEQLEQERQeraianklMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLK 1901
Cdd:PRK03918 575 LLKELEELGFESVEELEERLKELEPFYNEYLE--------LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELR 646
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774931 1902 RQLEEV-----EEENSRSSAQKRKLQRE-------LEELTDSSQTMNREISSLRNQL 1946
Cdd:PRK03918 647 KELEELekkysEEEYEELREEYLELSRElaglraeLEELEKRREEIKKTLEKLKEEL 703
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1054-1243 |
9.44e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1054 IADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLS--SELRGSLAQKEKEITSLQGRLEEegarraeaqrsL 1131
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeySWDEIDVASAEREIAELEAELER-----------L 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1132 REALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDS-TAAQQELRSRREAELSELQRCVEEetRRHET 1210
Cdd:COG4913 681 DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEElDELQDRLEAAEDLARLELRALLEE--RFAAA 758
|
170 180 190
....*....|....*....|....*....|....
gi 1988774931 1211 QLSELRVKHSAALDSLQEQLDNSK-RARQSLEKA 1243
Cdd:COG4913 759 LGDAVERELRENLEERIDALRARLnRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1503-1743 |
1.17e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1503 CLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLR 1582
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1583 LEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEiQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAM 1662
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFL-DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1663 KQLRRLQGQMKEVLRELDDSKVTRDDVISQskdSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGK 1742
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
.
gi 1988774931 1743 N 1743
Cdd:COG4942 251 L 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1334-1906 |
1.31e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1334 QLHDARELLQDESRQKMALAsRVRALEEEKNGLMERLEEEEERGKElsRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRR 1413
Cdd:COG4913 236 DLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1414 KLQRELDsaiqrerqkeeekerverqrerlreeiedmtiALQRERQNCTAlEKRQKKFDQclaeekavSARLAEERDRAE 1493
Cdd:COG4913 313 RLEARLD--------------------------------ALREELDELEA-QIRGNGGDR--------LEQLEREIERLE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1494 ADSREKETRCLALSRALQ----EAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRiqtqel 1569
Cdd:COG4913 352 RELEERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE------ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1570 eEELSEAENSRLRLEVTLQALKAQFEREISTNEE-----------KGEEKR-----------RALS--------KQVRE- 1618
Cdd:COG4913 426 -AEIASLERRKSNIPARLLALRDALAEALGLDEAelpfvgelievRPEEERwrgaiervlggFALTllvppehyAAALRw 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1619 ---------LEIQLEEERSQRSQSVSSKKQ----------------LEAELQEAE--AQVETanrgkEEAMKQLRR---L 1668
Cdd:COG4913 505 vnrlhlrgrLVYERVRTGLPDPERPRLDPDslagkldfkphpfrawLEAELGRRFdyVCVDS-----PEELRRHPRaitR 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1669 QGQMKE--VLRELDD-SKVTRDDVISQskDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEmvssssgKNVL 1745
Cdd:COG4913 580 AGQVKGngTRHEKDDrRRIRSRYVLGF--DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQER-------REAL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1746 SEEKRRLDARVNQLEEELEEEQTNNELltERLRKTALQVETLTVQLqgertlaQKAEAAREQLEKQNKELKARLGEmega 1825
Cdd:COG4913 651 QRLAEYSWDEIDVASAEREIAELEAEL--ERLDASSDDLAALEEQL-------EELEAELEELEEELDELKGEIGR---- 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1826 vrgkhrmsvaaLEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLE 1905
Cdd:COG4913 718 -----------LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAE 786
|
.
gi 1988774931 1906 E 1906
Cdd:COG4913 787 E 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1306-1825 |
1.36e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1306 EIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQ 1385
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1386 THSQQLTELRKQSEEVNSAVEAGDEIRR--KLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTA 1463
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEYIKlsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1464 LEKRQ---KKFDQCLAEEKAVSARLAEERDRAEADSREKetrclaLSRALQEAQDQKEELERANKQLRLEMEQLVNQQDD 1540
Cdd:PRK03918 350 LEKRLeelEERHELYEEAKAKKEELERLKKRLTGLTPEK------LEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1541 VGKNVHELERARRTLETeaqnlriqtqeleeelseaeNSRLRLEVTLQALKAQFEREISTNEE---KGEEKRRALSKQVR 1617
Cdd:PRK03918 424 LKKAIEELKKAKGKCPV--------------------CGRELTEEHRKELLEEYTAELKRIEKelkEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1618 ELEIQLEEERSQRSQSVSSK--KQLEAELQEAEAQ-VETANRGKEEAMKQLRRLQGQMKEVLRELDDSKvtrdDVISQSK 1694
Cdd:PRK03918 484 ELEKVLKKESELIKLKELAEqlKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE----ELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1695 DSEKKIQTLE---AEVLHLTEELAVSERQKRQAQ-QERDEIADEMVSSSSGKNVLSEEKRRLDA---RVNQLEEELEEEQ 1767
Cdd:PRK03918 560 ELEKKLDELEeelAELLKELEELGFESVEELEERlKELEPFYNEYLELKDAEKELEREEKELKKleeELDKAFEELAETE 639
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1768 TNNELLTERL------------RKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGA 1825
Cdd:PRK03918 640 KRLEELRKELeelekkyseeeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1637-1982 |
1.49e-06 |
|
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: 53.53 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1637 KKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDdviSQSKDSEKKIQTLEAEVLHLTEELAV 1716
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKRE---YEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1717 SERQKRQAQQERDEIADEMVSSssgKNVLSEEKRRLDARVNQLEEEleeeqtnnelLTERLRKTALQVETLtvqlqgERT 1796
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEI---EQLLEELNKKIKDLGEEEQLR----------VKEKIGELEAEIASL------ERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1797 LAQKAEAArEQLEKQNKELKARLGEMEGAVRGkhrmsvaaLEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQA 1876
Cdd:TIGR02169 310 IAEKEREL-EDAEERLAKLEAEIDKLLAEIEE--------LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1877 EDERRHADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLSFPEWR---- 1952
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKleql 460
|
330 340 350
....*....|....*....|....*....|
gi 1988774931 1953 PDIRAALPLSMRGRRALVDDLSLENSDSEE 1982
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1476-1946 |
1.55e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.57 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1476 AEEKAVSARLAEERDRAEADSR-------EKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHEL 1548
Cdd:pfam05483 99 AELKQKENKLQENRKIIEAQRKaiqelqfENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYER 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1549 ERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTL-------QALKAQFEREISTNEekgeekrralsKQVRELEI 1621
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLkedhekiQHLEEEYKKEINDKE-----------KQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1622 QLEEERSQRSQSVSskkqLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKevlRELDDSKVTRDDVISQSKDSEKKIQ 1701
Cdd:pfam05483 248 QITEKENKMKDLTF----LLEESRDKANQLEEKTKLQDENLKELIEKKDHLT---KELEDIKMSLQRSMSTQKALEEDLQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1702 TLEAEVLHLTEELAVSERQKRQAQQERDEIADEM-VSSSSGKNVLSEEKRRLDarvnqleeeleEEQTNNELLTERLRKT 1780
Cdd:pfam05483 321 IATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFeATTCSLEELLRTEQQRLE-----------KNEDQLKIITMELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1781 ALQVETLT-------VQLQGERTLAQKAEA---AREQLEKQNKELKARLGEMEGAVRGKHRmSVAALEAKIETMEEQLEQ 1850
Cdd:pfam05483 390 SSELEEMTkfknnkeVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREK-EIHDLEIQLTAIKTSEEH 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1851 ERqeraianklmrkteKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKR-------QLEEVEEENSRSSAQKRKLQR 1923
Cdd:pfam05483 469 YL--------------KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQeasdmtlELKKHQEDIINCKKQEERMLK 534
|
490 500
....*....|....*....|...
gi 1988774931 1924 ELEELTDSSQTMNREISSLRNQL 1946
Cdd:pfam05483 535 QIENLEEKEMNLRDELESVREEF 557
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1508-1973 |
1.76e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1508 RALQEAQDQKEELE--RANKQLRLEMEQLVNQQDDVGK--NVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRL 1583
Cdd:COG4913 242 EALEDAREQIELLEpiRELAERYAAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1584 EVTLQALKAQ-----------FEREISTNEEKGEEKRRA---LSKQVRELEIQLEEErsqrsqsvssKKQLEAELQEAEA 1649
Cdd:COG4913 322 REELDELEAQirgnggdrleqLEREIERLERELEERERRrarLEALLAALGLPLPAS----------AEEFAALRAEAAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1650 QVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEvlhLTEELAVSERQKR------- 1722
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA---LAEALGLDEAELPfvgelie 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1723 -QAQQERDEIADEMVSSSSGKNVLSEEKRRLDA----------------RVNQLEEELEEEQTNNELLTERL-------- 1777
Cdd:COG4913 469 vRPEEERWRGAIERVLGGFALTLLVPPEHYAAAlrwvnrlhlrgrlvyeRVRTGLPDPERPRLDPDSLAGKLdfkphpfr 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1778 ---------RKTALQVE------------TLTVQLQGERTLAQK---------------AEAAREQLEKQNKELKARLge 1821
Cdd:COG4913 549 awleaelgrRFDYVCVDspeelrrhpraiTRAGQVKGNGTRHEKddrrrirsryvlgfdNRAKLAALEAELAELEEEL-- 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1822 megavrgkhrmsvAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKevMMQAEDERRHADQYREQLDKSMVRLKQLK 1901
Cdd:COG4913 627 -------------AEAEERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERLDASSDDLAALE 691
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 1902 RQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLSFPEWRPDIRAALPLSMRGRRALVDDL 1973
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1079-1289 |
1.80e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1079 ESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENER---GMRERA 1155
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReelGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1156 EKQRRDLSEELEAL--RTELEDTLDSTAAQQELRSRREAELSELQRcVEEETRRHETQLSELRVKHSAALDSLQEQLDNS 1233
Cdd:COG3883 95 LYRSGGSVSYLDVLlgSESFSDFLDRLSALSKIADADADLLEELKA-DKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774931 1234 KRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQA 1289
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
851-1366 |
2.19e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.05 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 851 QWWRLFTKVKPLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVL-----ADQLQAEAELFAEAE 925
Cdd:TIGR00618 383 TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELcaaaiTCTAQCEKLEKIHLQ 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 926 EMRARLASRKQeleevlgeletrleeeeergvQLANEKKKMQQNIQ-DLEEQLEEEESARQRLLLEKVTLETKVKSLETD 1004
Cdd:TIGR00618 463 ESAQSLKEREQ---------------------QLQTKEQIHLQETRkKAVVLARLLELQEEPCPLCGSCIHPNPARQDID 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1005 LATAVEQR-ERLGKEKKQLEERLNEVTDQLTEEeekTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAM 1083
Cdd:TIGR00618 522 NPGPLTRRmQRGEQTYAQLETSEEDVYHQLTSE---RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1084 EAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENE----RGMRERAEKQR 1159
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHalsiRVLPKELLASR 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1160 RDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQS 1239
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKA 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1240 LEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERmhkLQCEIESLSGNLSSSDS 1319
Cdd:TIGR00618 759 RTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLS 835
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1988774931 1320 KSLRLAKEISSLESQLHDARELLQdESRQKMALASRVRALEEEKNGL 1366
Cdd:TIGR00618 836 RLEEKSATLGEITHQLLKYEECSK-QLAQLTQEQAKIIQLSDKLNGI 881
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1098-1534 |
2.61e-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: 53.03 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1098 ELRGSLAQKEKEITSLQGRLEE---EGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRrdlsEELEALRTELE 1174
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEmarELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQ----EDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1175 DTLDSTAAQQELRSRREAELSElqrcVEEETRRHETQLSELRvkhsAALDSLQEQLDNSKRARQSLEKAKATLEEERQNL 1254
Cdd:COG3096 365 EQEEVVEEAAEQLAEAEARLEA----AEEEVDSLKSQLADYQ----QALDVQQTRAIQYQQAVQALEKARALCGLPDLTP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1255 TSELKSLQASRSESERgrkrADNQLQELSARLAQADreredreerMHKLQCE-----IESLSGNLSSSDSKSlrlakeis 1329
Cdd:COG3096 437 ENAEDYLAAFRAKEQQ----ATEEVLELEQKLSVAD---------AARRQFEkayelVCKIAGEVERSQAWQ-------- 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1330 slesqlhDARELLQDESRQKmALASRVRALEeeknglmerleeeeergkelsrqiqthsQQLTELRKQSEEVNSAVEAGD 1409
Cdd:COG3096 496 -------TARELLRRYRSQQ-ALAQRLQQLR----------------------------AQLAELEQRLRQQQNAERLLE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1410 EIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMtIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEER 1489
Cdd:COG3096 540 EFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQR-SELRQQLEQLRARIKELAARAPAWLAAQDALERLREQS 618
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1988774931 1490 DRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQL 1534
Cdd:COG3096 619 GEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
868-1091 |
3.95e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 868 QDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEaeeMRARLASRKQELEEVLGELET 947
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA---LEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 948 RLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLN 1027
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774931 1028 EVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSD 1091
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1137-1943 |
5.25e-06 |
|
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: 51.97 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1137 QVSELKEEVENERGMRERAEKQRRDLSE---ELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLS 1213
Cdd:TIGR00606 225 QITSKEAQLESSREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLN 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1214 ELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLA----QA 1289
Cdd:TIGR00606 305 DLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfER 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1290 DREREDREERMHKLQCEIESlsgnlsssdSKSLRLAKEISSLESQLHDARELLqDESRQKMALASRVRALEEEKnglMER 1369
Cdd:TIGR00606 385 GPFSERQIKNFHTLVIERQE---------DEAKTAAQLCADLQSKERLKQEQA-DEIRDEKKGLGRTIELKKEI---LEK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1370 LEEEEERGKELSRQIQTHSQQL----TELRKQSEEV-----NSAVEAGDEIRRKLQRE---LDSAIQRERQKEEEKERVE 1437
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRIleldQELRKAERELskaekNSLTETLKKEVKSLQNEkadLDRKLRKLDQEMEQLNHHT 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1438 RQRERLREEIEDMTIALQRERQNctalEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQK 1517
Cdd:TIGR00606 532 TTRTQMEMLTKDKMDKDEQIRKI----KSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNK 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1518 EELeraNKQLRLEMEQLVNQQD-------------DVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLE 1584
Cdd:TIGR00606 608 NHI---NNELESKEEQLSSYEDklfdvcgsqdeesDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQ 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1585 VTLQALKA--QFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAM 1662
Cdd:TIGR00606 685 RVFQTEAElqEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1663 KQLRRLQGQMKEVLRELDDSKVTRDDVI------SQSKDSEKKIQTLEAEVlhLTEELAVSERQKRQAQQERDEIADEMV 1736
Cdd:TIGR00606 765 NDIEEQETLLGTIMPEEESAKVCLTDVTimerfqMELKDVERKIAQQAAKL--QGSDLDRTVQQVNQEKQEKQHELDTVV 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1737 SSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQgerTLAQKAEAAREQLEKQNKELK 1816
Cdd:TIGR00606 843 SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQ---SLIREIKDAKEQDSPLETFLE 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1817 ARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKL-------MRKTEKKLKEVMMQAEDERRHADQYREQ 1889
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIqdgkddyLKQKETELNTVNAQLEECEKHQEKINED 999
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1988774931 1890 LdksmvRLKQLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLR 1943
Cdd:TIGR00606 1000 M-----RLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1510-1928 |
5.61e-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: 51.88 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1510 LQEAQDQKEELERANKQLRLEMEQLVNQQDDVGknvhELERARRTLETEAQnlriqtqeleeelseAENSRLRLevTLQA 1589
Cdd:COG3096 284 SERALELRRELFGARRQLAEEQYRLVEMARELE----ELSARESDLEQDYQ---------------AASDHLNL--VQTA 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1590 LKAQfereistneEKGEEKRRALSkqvrELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRG---KEEAMKQLR 1666
Cdd:COG3096 343 LRQQ---------EKIERYQEDLE----ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQladYQQALDVQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1667 RLQGQMKEVLRELDDSK-------VTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSE---RQKRQAQQERDEIADEMV 1736
Cdd:COG3096 410 TRAIQYQQAVQALEKARalcglpdLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADaarRQFEKAYELVCKIAGEVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1737 SS---SSGKNVLsEEKRRLDARVNQLEEELEEEQTNNELLtERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNK 1813
Cdd:COG3096 490 RSqawQTARELL-RRYRSQQALAQRLQQLRAQLAELEQRL-RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLE 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1814 ELKARLGEmEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLmrktekklkevmmqaederrhADQYREQLDKS 1893
Cdd:COG3096 568 ELEEQAAE-AVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERL---------------------REQSGEALADS 625
|
410 420 430
....*....|....*....|....*....|....*...
gi 1988774931 1894 ---MVRLKQLKRQLEEVEEENSRSSAQKRKLQRELEEL 1928
Cdd:COG3096 626 qevTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1457-1754 |
6.13e-06 |
|
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: 51.28 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1457 ERQNCTALEKRQKKFDQC----LAEEKAVSARLAEERDRAEA--DSREKETRCLALSRALQE--AQDQKEELERANKQLR 1528
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMeqerLRQEKEEKAREVERRRKLEEaeKARQAEMDRQAAIYAEQErmAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1529 -LEMEQLVNQQDDVG-KNVHELERARrtLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREiSTNEEKGE 1606
Cdd:pfam17380 359 kRELERIRQEEIAMEiSRMRELERLQ--MERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA-EQEEARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1607 EKRRALSKQVRELEIQLEEERSQRSQSVSSKKQlEAELQEAEAQVETANRGKEEAMKQLRR-LQGQMKEVLRELDDSKVT 1685
Cdd:pfam17380 436 EVRRLEEERAREMERVRLEEQERQQQVERLRQQ-EEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774931 1686 RDDVISQSKDSEKKIQtlEAEVLHLTEElavsERQKRQAQQERDEIADEMvssssgkNVLSEEKRRLDA 1754
Cdd:pfam17380 515 RKLLEKEMEERQKAIY--EEERRREAEE----ERRKQQEMEERRRIQEQM-------RKATEERSRLEA 570
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
971-1285 |
6.25e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.05 E-value: 6.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 971 QDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQ--------------LTEE 1036
Cdd:pfam07888 55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEkdallaqraahearIREL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1037 EEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGR 1116
Cdd:pfam07888 135 EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1117 LEEEGARRAEAQRslrealsQVSELKEEVENERGMRERAEKQRRdlseELEALRTELEdtldSTAAQqelRSRREAELse 1196
Cdd:pfam07888 215 ITTLTQKLTTAHR-------KEAENEALLEELRSLQERLNASER----KVEGLGEELS----SMAAQ---RDRTQAEL-- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1197 lqrcveeetRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSEL----KSLQASRSESER-- 1270
Cdd:pfam07888 275 ---------HQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELqrleERLQEERMEREKle 345
|
330
....*....|....*...
gi 1988774931 1271 ---GRKRADNQLQELSAR 1285
Cdd:pfam07888 346 velGREKDCNRVQLSESR 363
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1069-1362 |
6.84e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 50.30 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1069 LEQEKfkRRMESEAMEAQEQLSdlgmlsSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENE 1148
Cdd:pfam00038 23 LEQQN--KLLETKISELRQKKG------AEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1149 RGMRERAEKQRRDLSEELEAL---RTELEDTLDSTaaQQELRSRR---EAELSELQRCVEEETRRHETQLSeLRVKHSAA 1222
Cdd:pfam00038 95 LNLRTSAENDLVGLRKDLDEAtlaRVDLEAKIESL--KEELAFLKknhEEEVRELQAQVSDTQVNVEMDAA-RKLDLTSA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1223 LDSLQEQLDN-SKRARQSLEKA-KATLEEERQNLTSELKSLQASRSESERGRKradnQLQELSARLAQADREREDREERM 1300
Cdd:pfam00038 172 LAEIRAQYEEiAAKNREEAEEWyQSKLEELQQAAARNGDALRSAKEEITELRR----TIQSLEIELQSLKKQKASLERQL 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 1301 HKLQceiESLSGNLSSSDSKslrlakeISSLESQLHDARELLQDESRQKMALASRVRALEEE 1362
Cdd:pfam00038 248 AETE---ERYELQLADYQEL-------ISELEAELQETRQEMARQLREYQELLNVKLALDIE 299
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1033-1281 |
8.32e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.89 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1033 LTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEK--------FKRRMESEAMEAQEQLSDLGMLSSELRGSLA 1104
Cdd:pfam17380 265 MTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKeekareveRRRKLEEAEKARQAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1105 QKEKEITSLqgRLEEegaRRAEAQRSLREALSQvsELKEEVENERGMRERAEKQRRdLSEELEALRTE--LEDTLDSTAA 1182
Cdd:pfam17380 345 ERERELERI--RQEE---RKRELERIRQEEIAM--EISRMRELERLQMERQQKNER-VRQELEAARKVkiLEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1183 QQ-----ELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKA---KATLEEERQN- 1253
Cdd:pfam17380 417 QQkvemeQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEkrdRKRAEEQRRKi 496
|
250 260
....*....|....*....|....*...
gi 1988774931 1254 LTSELKSLQASRSESERGRKRADNQLQE 1281
Cdd:pfam17380 497 LEKELEERKQAMIEEERKRKLLEKEMEE 524
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
864-1066 |
9.95e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 9.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 864 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEaelfaeaeemRARLASRKQELEEVLG 943
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ----------KEELAELLRALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 944 ELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLE 1023
Cdd:COG4942 119 QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1988774931 1024 ERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQ 1066
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1083-1258 |
1.14e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1083 MEAQEQLSDLGMLSSELRGSLAQKE---KEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQR 1159
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKelpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1160 RDLS--EELEALRTELEdtldstaAQQELRSRREAELSELqrcvEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRAR 1237
Cdd:COG1579 83 GNVRnnKEYEALQKEIE-------SLKRRISDLEDEILEL----MERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|.
gi 1988774931 1238 QSLEKAKATLEEERQNLTSEL 1258
Cdd:COG1579 152 AELEAELEELEAEREELAAKI 172
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1019-1288 |
1.30e-05 |
|
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: 50.34 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1019 KKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQgrleqekfKRRMESEAMEAQEQLSdlgmlSSE 1098
Cdd:COG5185 256 EKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTK--------SIDIKKATESLEEQLA-----AAE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1099 LRGSLAQKEKEITSLQGRLEEEGARRaeaQRSLREALSQVSELKEEVENERGMRERAEKQrRDLSEELEALRTEL-EDTL 1177
Cdd:COG5185 323 AEQELEESKRETETGIQNLTAEIEQG---QESLTENLEAIKEEIENIVGEVELSKSSEEL-DSFKDTIESTKESLdEIPQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1178 DSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKhSAALDSLQEQLDnsKRARQSLEKAKATLEEERQNLTSE 1257
Cdd:COG5185 399 NQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEV-SKLLNELISELN--KVMREADEESQSRLEEAYDEINRS 475
|
250 260 270
....*....|....*....|....*....|.
gi 1988774931 1258 LKSlqaSRSESERGRKRADNQLQELSARLAQ 1288
Cdd:COG5185 476 VRS---KKEDLNEELTQIESRVSTLKATLEK 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1588-1819 |
1.85e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1588 QALKAQFEREISTNEEKGEEKRRALS---KQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQ 1664
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAalkKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1665 LRRLQGQMKEVLRELDD-SKVTRDDVISQSKD---SEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSS 1740
Cdd:COG4942 99 LEAQKEELAELLRALYRlGRQPPLALLLSPEDfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774931 1741 GKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLqgERTLAQKAEAAREQLEKQNKELKARL 1819
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI--ARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1127-1346 |
1.87e-05 |
|
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: 50.22 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1127 AQRSLREALSQVSELKEE---VENERGMRERAEKQRRDLSEE----LEAL---RTELEDTlDSTAAQQELRSRREAeLSE 1196
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQddaAQNALADKERAEADRQRLEQEkqqqLAAIsgsQSQLEST-DQNALETNGQAQRDA-ILE 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1197 LQRCVEEETRRHETQLSELRVKHSAA---------------LDSLQEQLDNSKR-ARQSLEKAKATLEEERQNLTSELKS 1260
Cdd:NF012221 1614 ESRAVTKELTTLAQGLDALDSQATYAgesgdqwrnpfagglLDRVQEQLDDAKKiSGKQLADAKQRHVDNQQKVKDAVAK 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1261 LQASRSESERGRKRADNQLQElsarlAQADREREDREERMHKLQCEIESLSGNLSSSDSKSlRLAKEISSLESQLH---- 1336
Cdd:NF012221 1694 SEAGVAQGEQNQANAEQDIDD-----AKADAEKRKDDALAKQNEAQQAESDANAAANDAQS-RGEQDASAAENKANqaqa 1767
|
250
....*....|
gi 1988774931 1337 DARELLQDES 1346
Cdd:NF012221 1768 DAKGAKQDES 1777
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
993-1176 |
1.90e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 993 TLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKS-LNKLKNKQEAVIADLEERLKREEQGRLEQ 1071
Cdd:PHA02562 185 TLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAeIEELTDELLNLVMDIEDPSAALNKLNTAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1072 EKFKRRMESEAMEAQ------------EQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARR---AEAQRSLREALS 1136
Cdd:PHA02562 265 AKIKSKIEQFQKVIKmyekggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMdefNEQSKKLLELKN 344
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1988774931 1137 QVSELKEEVENERGMR-------ERAEKQRRDLSEELEALRTELEDT 1176
Cdd:PHA02562 345 KISTNKQSLITLVDKAkkvkaaiEELQAEFVDNAEELAKLQDELDKI 391
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1476-1727 |
2.10e-05 |
|
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: 49.64 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1476 AEEKAVSARLAEERDRAEADSREKETrclaLSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTL 1555
Cdd:pfam05667 226 WNSQGLASRLTPEEYRKRKRTKLLKR----IAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1556 ETE----AQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFErEISTNEEKGEEKRRALSKQVRELEIQLEEERSQRS 1631
Cdd:pfam05667 302 HTEklqfTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLE-DLESSIQELEKEIKKLESSIKQVEEELEELKEQNE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1632 QSVSS---KKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEV-------LRELDDSKVTRDDVISQSKDsekKIQ 1701
Cdd:pfam05667 381 ELEKQykvKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHrvplieeYRALKEAKSNKEDESQRKLE---EIK 457
|
250 260
....*....|....*....|....*.
gi 1988774931 1702 TLEAEVLHLTEELAVSERQKRQAQQE 1727
Cdd:pfam05667 458 ELREKIKEVAEEAKQKEELYKQLVAE 483
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1102-1334 |
2.23e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1102 SLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVEnergmreRAEKQRRDLSEELEALRTELEdtldstA 1181
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-------ELQAELEALQAEIDKLQAEIA------E 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1182 AQQELRSRREaELSELQRcVEEETRRHETQLSELRVKHSAA-----LDSLQEQLDNSKRARQSLEKAKATLEEERQNLTS 1256
Cdd:COG3883 77 AEAEIEERRE-ELGERAR-ALYRSGGSVSYLDVLLGSESFSdfldrLSALSKIADADADLLEELKADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774931 1257 ELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQ 1334
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1675-1947 |
2.28e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1675 VLRELDDSKVTRDDVISQ-----SKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEiADEMVSSSSGKNvlsEEK 1749
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQieekeEKDLHERLNGLESELAELDEEIERYEEQREQARETRDE-ADEVLEEHEERR---EEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1750 RRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRgK 1829
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLE-E 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1830 HRMSVAALEAKIETMEEQLeqerqeraianklmRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEE 1909
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDA--------------DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270
....*....|....*....|....*....|....*...
gi 1988774931 1910 ENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLS 1947
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1654-1871 |
2.71e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1654 ANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKI-------QTLEAEVLHLTEELAVSERQKRQAQQ 1726
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIaalarriRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1727 ERDEIADEMvssSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAARE 1806
Cdd:COG4942 98 ELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774931 1807 QLEKQNKELKARLGEMEGAVRGKHRMsVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKE 1871
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKL-LARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
883-1548 |
2.81e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.45 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 883 KEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEemrARLASRKQELEEVLGELETRLEEEEERGVQLANE 962
Cdd:pfam12128 215 KSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAE---LRLSHLHFGYKSDETLIASRQEERQETSAELNQL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 963 KKKMQQNIQDLeeqleeeesaRQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEK----KQLEERLNEVTDQLTEEEE 1038
Cdd:pfam12128 292 LRTLDDQWKEK----------RDELNGELSAADAAVAKDRSELEALEDQHGAFLDADietaAADQEQLPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1039 KTKSL----NKLKNKQEAVIADLEERLKREEQGrLEQEKFKRRmESEAMEAQEQLSDLGMLSSELRGSLAQKEKEItslq 1114
Cdd:pfam12128 362 RLKALtgkhQDVTAKYNRRRSKIKEQNNRDIAG-IKDKLAKIR-EARDRQLAVAEDDLQALESELREQLEAGKLEF---- 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1115 grlEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRrdlsEELEALRTELEDTLDSTAAqqeLRSRREAEL 1194
Cdd:pfam12128 436 ---NEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAR----EEQEAANAEVERLQSELRQ---ARKRRDQAS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1195 SELQRCvEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRA-RQSLEKAKATLEEERQNLTSELKSLQASRSESERGRK 1273
Cdd:pfam12128 506 EALRQA-SRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDwEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1274 RADNQL---------QELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDskslrlaKEISSLESQLHDARELLQD 1344
Cdd:pfam12128 585 LDLKRIdvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS-------REETFARTALKNARLDLRR 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1345 ESRQKMALASRV-RALEEEKNGLMERLEEEEERGKELSRQIQTHSQ----QLTELRKQSEEVNSAVE-AGDEIRRKLQRE 1418
Cdd:pfam12128 658 LFDEKQSEKDKKnKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeqkeQKREARTEKQAYWQVVEgALDAQLALLKAA 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1419 LDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAE-EKAVSARLAEERDRAEADSR 1497
Cdd:pfam12128 738 IAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRyFDWYQETWLQRRPRLATQLS 817
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1988774931 1498 EKETrclALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHEL 1548
Cdd:pfam12128 818 NIER---AISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGL 865
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
958-1145 |
2.85e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 958 QLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQL---- 1033
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaell 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1034 ---------------------TEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDL 1092
Cdd:COG4942 111 ralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1988774931 1093 GMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEV 1145
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1112-1352 |
3.05e-05 |
|
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: 48.87 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1112 SLQGRLEEEGARRAEAQRSLREALSQvseLKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRRE 1191
Cdd:pfam05667 230 GLASRLTPEEYRKRKRTKLLKRIAEQ---LRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1192 AELSELQRCVEEETRRHETQlSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERG 1271
Cdd:pfam05667 307 QFTNEAPAATSSPPTKVETE-EELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1272 RKR----------ADNQLQELSARLAQADREREDREERMHK----LQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHD 1337
Cdd:pfam05667 386 YKVkkktldllpdAEENIAKLQALVDASAQRLVELAGQWEKhrvpLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKE 465
|
250
....*....|....*
gi 1988774931 1338 ArellQDESRQKMAL 1352
Cdd:pfam05667 466 V----AEEAKQKEEL 476
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1007-1362 |
3.53e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.05 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1007 TAVEQRER-LGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKfkrRMESeameA 1085
Cdd:pfam10174 334 TAKEQRAAiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQK---KIEN----L 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1086 QEQLSDlgmlsselrgslaqKEKEITSLQGR---LEEEGARRAEAQRSLREALSQvselKEEV-ENERGMRERAEKQRRd 1161
Cdd:pfam10174 407 QEQLRD--------------KDKQLAGLKERvksLQTDSSNTDTALTTLEEALSE----KERIiERLKEQREREDRERL- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1162 lsEELEALRTELEDTLDSTAAQQELRSRREAELSELQrcveeetrRHETQLSELRVKHSAALDSL----QEQLDNSKRAR 1237
Cdd:pfam10174 468 --EELESLKKENKDLKEKVSALQPELTEKESSLIDLK--------EHASSLASSGLKKDSKLKSLeiavEQKKEECSKLE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1238 QSLEKAKATLEEERQN--LTSELKSLqasrsESERGRKRAD-NQLQELSARLAQADREREDREERMHKLQCEIESLSGNL 1314
Cdd:pfam10174 538 NQLKKAHNAEEAVRTNpeINDRIRLL-----EQEVARYKEEsGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQ 612
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1988774931 1315 SSSDSKSLRLAKEISSLESQlhDARELLQDESRQKMALASRVRALEEE 1362
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKK--KGAQLLEEARRREDNLADNSQQLQLE 658
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
871-1692 |
3.62e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.27 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 871 EIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGELETRLE 950
Cdd:TIGR00606 313 TVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 951 EEEERGV--QLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNE 1028
Cdd:TIGR00606 393 KNFHTLVieRQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1029 VtdqLTEEEEKTKSLNKLKNKQEAviADLEERLKREEQGRLEQEKFKRRMESEAmeaqEQLSDLGMLSSELRGSLAQKEK 1108
Cdd:TIGR00606 473 I---LELDQELRKAERELSKAEKN--SLTETLKKEVKSLQNEKADLDRKLRKLD----QEMEQLNHHTTTRTQMEMLTKD 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1109 EITSLQgRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRS 1188
Cdd:TIGR00606 544 KMDKDE-QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLS 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1189 RREAELSELQRCVEEETRrhetqlselrvkhsaaLDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSES 1268
Cdd:TIGR00606 623 SYEDKLFDVCGSQDEESD----------------LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRV 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1269 ERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLH----DARELLQD 1344
Cdd:TIGR00606 687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQkvnrDIQRLKND 766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1345 ESRQKMALASRVRALEEEKN-----GLMERLEEEEERGKELSRQIQTHSQQlTELRKQSEEVNSAVEAGDEIRRKLQREL 1419
Cdd:TIGR00606 767 IEEQETLLGTIMPEEESAKVcltdvTIMERFQMELKDVERKIAQQAAKLQG-SDLDRTVQQVNQEKQEKQHELDTVVSKI 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1420 DSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREK 1499
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1500 ETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDD---------------VGKNVHELERARRTLETEAQNLR- 1563
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgkddylkqketelntVNAQLEECEKHQEKINEDMRLMRq 1005
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1564 -IQTQELEEELSEAENSRLRLEVTLQALK---AQFEREIstNEEKGEEKRRALSKQVRELE-IQLEEERSQRSQSVSSKK 1638
Cdd:TIGR00606 1006 dIDTQKIQERWLQDNLTLRKRENELKEVEeelKQHLKEM--GQMQVLQMKQEHQKLEENIDlIKRNHVLALGRQKGYEKE 1083
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1988774931 1639 QLEAELQEAEAQVETANRGKEEAMKQLRrlqgQMKEVLRELDDSKVTRDDVISQ 1692
Cdd:TIGR00606 1084 IKHFKKELREPQFRDAEEKYREMMIVMR----TTELVNKDLDIYYKTLDQAIMK 1133
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1464-1950 |
3.84e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.89 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1464 LEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERAN-KQLRLEMEQLVNQQDDVG 1542
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHqRTVREKERELVDCQRELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1543 KNVHEL-ERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFERE----------ISTNEEKGEEKRRA 1611
Cdd:TIGR00606 330 KLNKERrLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpfserqiknfHTLVIERQEDEAKT 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1612 LSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLREldDSKVTRDDVIS 1691
Cdd:TIGR00606 410 AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL--DQELRKAEREL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1692 QSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADE------MVSSSSGKNVLSEEKRRLDARVNQLEEELEE 1765
Cdd:TIGR00606 488 SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHtttrtqMEMLTKDKMDKDEQIRKIKSRHSDELTSLLG 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1766 EQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAV------------------- 1826
Cdd:TIGR00606 568 YFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsqdeesdlerlkee 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1827 ---RGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKsmvRLKQLKRQ 1903
Cdd:TIGR00606 648 iekSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTES---ELKKKEKR 724
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1988774931 1904 LEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLSFPE 1950
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE 771
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
983-1146 |
3.93e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 983 ARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKtksLNKLKNKQEAVIADLEERLK 1062
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNVRNNKEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1063 REEQGRLEQEkfkrrmESEAMEAQEqlsdlgmlssELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELK 1142
Cdd:COG1579 102 KRRISDLEDE------ILELMERIE----------ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....
gi 1988774931 1143 EEVE 1146
Cdd:COG1579 166 EELA 169
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
996-1335 |
3.97e-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: 48.86 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 996 TKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEqgrleqekfk 1075
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK---------- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1076 rrmeseamEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEegarraeAQRSLREALSQVSELKEEVENERGMRERA 1155
Cdd:TIGR04523 215 --------SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN-------TQTQLNQLKDEQNKIKKQLSEKQKELEQN 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1156 EKQRRDLSEELEALRTELEDTldSTAAQQELRSRREAELSELQRCVEE---ETRRHETQLSELR---------VKHSAAL 1223
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDL--NNQKEQDWNKELKSELKNQEKKLEEiqnQISQNNKIISQLNeqisqlkkeLTNSESE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1224 DS-LQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHK 1302
Cdd:TIGR04523 358 NSeKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
330 340 350
....*....|....*....|....*....|...
gi 1988774931 1303 LQCEIESLSGNLSSSDSKSLRLAKEISSLESQL 1335
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1714-1947 |
4.40e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1714 LAVSERQKRQAQQERDEiademvssssgknvLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQG 1793
Cdd:COG4942 15 AAAQADAAAEAEAELEQ--------------LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1794 ERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIaNKLMRKTEKKLKEVM 1873
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774931 1874 MQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEEN----SRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLS 1947
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERqkllARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1039-1194 |
4.66e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.65 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1039 KTKSLNKLkNKQeavIADLEERLKREEQGrleqekfkrrmeSEAMEAQeqlsdlgmlSSELRGSLAQKEKEITSLQGRLE 1118
Cdd:PRK09039 51 KDSALDRL-NSQ---IAELADLLSLERQG------------NQDLQDS---------VANLRASLSAAEAERSRLQALLA 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774931 1119 EEGARRAEAQRslrealsQVSELKEEVENERGMRERAEKQRRDLSEELEALRTEL---EDTLDSTAAQQELRSRREAEL 1194
Cdd:PRK09039 106 ELAGAGAAAEG-------RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLaalEAALDASEKRDRESQAKIADL 177
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1146-1404 |
4.89e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1146 ENERGMRERAEKQRRDLSEELEALRTELEdtldstAAQQELRS-RREAELSELqrcvEEETRRHETQLSELRvkhsAALD 1224
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELE------EAEAALEEfRQKNGLVDL----SEEAKLLLQQLSELE----SQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1225 SLQEQLDNSKRARQSLEKAKATLEEERQNLTselkslqasrsesergrkrADNQLQELSARLAQADReredreermhklq 1304
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPELL-------------------QSPVIQQLRAQLAELEA------------- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1305 cEIESLSGNLSSSDSKSLRLAKEISSLESQLHD-ARELLQDESRQKMALASRVRALEEEKNGL---MERLEEEEERGKEL 1380
Cdd:COG3206 278 -ELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLearLAELPELEAELRRL 356
|
250 260
....*....|....*....|....
gi 1988774931 1381 SRQIQTHSQQLTELRKQSEEVNSA 1404
Cdd:COG3206 357 EREVEVARELYESLLQRLEEARLA 380
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1646-1960 |
5.17e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1646 EAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIqtlEAEVLHLTEELAVSERQKRQAQ 1725
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKR---EYEGYELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1726 QERDEIADEMvssssgknvlseEKrrldarvnqleeeleeeqtnnelLTERLRKTALQVETLtvqlqgERTLAQKAEAAR 1805
Cdd:TIGR02169 244 RQLASLEEEL------------EK-----------------------LTEEISELEKRLEEI------EQLLEELNKKIK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1806 EQLEKQNKELKARLGEMEGavrgkhrmSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQ 1885
Cdd:TIGR02169 283 DLGEEEQLRVKEKIGELEA--------EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774931 1886 YREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQL-SFPEWRPDIRAALP 1960
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELqRLSEELADLNAAIA 430
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
982-1283 |
5.62e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 48.39 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 982 SARQRLLLEKVTLETKvKSLETDLATAVEQRERlGKEKKQLEERLnevtdQLTEEEEKTKSL-NKLKNKQEAVIAdLEER 1060
Cdd:PLN03188 1012 SARKRNSLLKLTYSCE-PSQAPPLNTIPESTDE-SPEKKLEQERL-----RWTEAESKWISLaEELRTELDASRA-LAEK 1083
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1061 LKREeqgrLEQEKFKRRMESEAMEAQ--------EQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAqRSLR 1132
Cdd:PLN03188 1084 QKHE----LDTEKRCAEELKEAMQMAmegharmlEQYADLEEKHIQLLARHRRIQEGIDDVKKAAARAGVRGAES-KFIN 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1133 EALSQVSELKEEvenergmrerAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSR-REAE--LSELQRC---VEEETR 1206
Cdd:PLN03188 1159 ALAAEISALKVE----------REKERRYLRDENKSLQAQLRDTAEAVQAAGELLVRlKEAEeaLTVAQKRamdAEQEAA 1228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774931 1207 RHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSEL-KSLQASRSESERGRKRADNQLQELS 1283
Cdd:PLN03188 1229 EAYKQIDKLKRKHENEISTLNQLVAESRLPKEAIRPACNDDCMAKYDAGEPLsEGDQQWREEFEPFYKKEDGELSKLA 1306
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1099-1821 |
5.68e-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: 48.09 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1099 LRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERgmreraeKQRRDLSEELEALRTELEDtld 1178
Cdd:TIGR04523 45 IKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK-------DKINKLNSDLSKINSEIKN--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1179 staaQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAaLDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSEL 1258
Cdd:TIGR04523 115 ----DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1259 KSLQasrsesergrkradNQLQELSARLAqadreredreermhklqceieslsgNLSSSDSKSLRLAKEISSLESQ---L 1335
Cdd:TIGR04523 190 DKIK--------------NKLLKLELLLS-------------------------NLKKKIQKNKSLESQISELKKQnnqL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1336 HDARELLQDESRQKMALASRVralEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEagdEIRRKL 1415
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNT---QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS---DLNNQK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1416 QRELDSAIQRERQkeeekerverqrerlreeiedmtialQRERQnctaLEKRQKKFDQclaEEKAVSaRLAEERDRAEAD 1495
Cdd:TIGR04523 305 EQDWNKELKSELK--------------------------NQEKK----LEEIQNQISQ---NNKIIS-QLNEQISQLKKE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1496 SREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSE 1575
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1576 AENSRLRLEVTLQALK---AQFEREIstneEKGEEKRRALSKQVRELEIQLEEERSQRsqsvsskKQLEAELQEAEAQVE 1652
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTnqdSVKELII----KNLDNTRESLETQLKVLSRSINKIKQNL-------EQKQKELKSKEKELK 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1653 TANRGK---EEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQ------SKDSEKKIQTLEAEVLHLTEELAVSERQKR- 1722
Cdd:TIGR04523 500 KLNEEKkelEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDledelnKDDFELKKENLEKEIDEKNKEIEELKQTQKs 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1723 --QAQQERDEIADEMvssSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQK 1800
Cdd:TIGR04523 580 lkKKQEEKQELIDQK---EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
730 740
....*....|....*....|.
gi 1988774931 1801 AEAAREQLEKQNKELKARLGE 1821
Cdd:TIGR04523 657 IRNKWPEIIKKIKESKTKIDD 677
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
995-1269 |
6.21e-05 |
|
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: 48.21 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 995 ETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEK--TKSLNKLKNKQEAVIADLEERLK-------REE 1065
Cdd:pfam09731 160 KAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQseEEAAPPLLDAAPETPPKLPEHLDnveekveKAQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1066 QGRLEQEKFKRRMESEAMEAQEQLS------------DLGMLSSELRGSLAQKEKEITSLQGRL------EEEGARRA-- 1125
Cdd:pfam09731 240 SLAKLVDQYKELVASERIVFQQELVsifpdiipvlkeDNLLSNDDLNSLIAHAHREIDQLSKKLaelkkrEEKHIERAle 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1126 ---EAQRSLREALSQ-------VSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAeLS 1195
Cdd:pfam09731 320 kqkEELDKLAEELSArleevraADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREF-LQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1196 ELQRCVEEETRRHETQLSEL--RVKH-SAALDSLQEQLDNSKRARQ---SLEKAKATLE-----EERQNLTSELKSLQAS 1264
Cdd:pfam09731 399 DIKEKVEEERAGRLLKLNELlaNLKGlEKATSSHSEVEDENRKAQQlwlAVEALRSTLEdgsadSRPRPLVRELKALKEL 478
|
....*
gi 1988774931 1265 RSESE 1269
Cdd:pfam09731 479 ASDDE 483
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1582-1952 |
6.64e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1582 RLEVTLQALKAQFE--REISTNEEKGEEKRRALSKQVRELEIQLE--EERSQRSQSVSSKKQLEAELQEAEAQVETAnrg 1657
Cdd:COG4717 75 ELEEELKEAEEKEEeyAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEEL--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1658 kEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQ-SKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMV 1736
Cdd:COG4717 152 -EERLEELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1737 SSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQL--------QGERTLAQKAEAAREQL 1808
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLlallflllAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1809 EKQNKELKARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQA-----EDERRHA 1883
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEagvedEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1884 DQYREQLDKSMVRLKQLKRQL----------------EEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLS 1947
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLeellgeleellealdeEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
....*
gi 1988774931 1948 FPEWR 1952
Cdd:COG4717 471 LAELL 475
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1034-1289 |
6.65e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1034 TEEEEKTKSLNKLKNKQEAVIADLEErlkreeqgrleqekfkrrMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSL 1113
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDA------------------LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1114 QGRLEEEGARRAEAQRSLREALSQVSELK--------EEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQE 1185
Cdd:COG3883 78 EAEIEERREELGERARALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1186 LRSRREAELSELQRCVEEETRRHETQLSELrvkhSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASR 1265
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQL----SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
250 260
....*....|....*....|....
gi 1988774931 1266 SESERGRKRADNQLQELSARLAQA 1289
Cdd:COG3883 234 AAAAAAAAAAASAAGAGAAGAAGA 257
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1228-1946 |
7.29e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1228 EQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASrsesergrkradnqLQELSARLAQADREREDREERMHKLQCEI 1307
Cdd:TIGR00618 184 MEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHER--------------KQVLEKELKHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1308 ESLSGNLSSSD--SKSLRLAKEISSLESQLHDARELLqDESRQKMALASRVRALEE---EKNGLMERLEEEEERGKELSR 1382
Cdd:TIGR00618 250 EAQEEQLKKQQllKQLRARIEELRAQEAVLEETQERI-NRARKAAPLAAHIKAVTQieqQAQRIHTELQSKMRSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1383 QIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELdsaiqrerQKEEEKERVERQRERLREEIEDMTIALQRERQNCT 1462
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT--------SIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1463 ALEK---RQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQd 1539
Cdd:TIGR00618 401 ELDIlqrEQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE- 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1540 dvgkNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRR------ALS 1613
Cdd:TIGR00618 480 ----QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDvyhqltSER 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1614 KQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDsKVTRDDVISQS 1693
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP-EQDLQDVRLHL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1694 KDSEKKIQTLEAEVLHLTEELAvserQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELL 1773
Cdd:TIGR00618 635 QQCSQELALKLTALHALQLTLT----QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1774 TERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIEtmeeqLEQERQ 1853
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE-----LSHLAA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1854 ERAIANKLMRKTEKKLKEVMMQAEDERRHADQYRE-QLDKSMVRLKQLKRQLEEveeeNSRSSAQKRKLQRELEELTDSS 1932
Cdd:TIGR00618 786 EIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLEE----KSATLGEITHQLLKYEECSKQL 861
|
730
....*....|....
gi 1988774931 1933 QTMNREISSLRNQL 1946
Cdd:TIGR00618 862 AQLTQEQAKIIQLS 875
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1027-1678 |
8.67e-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: 47.71 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1027 NEVTDQLTEEEEKTKSLNKLKNK---QEAVIADLEERL-KREEQGRLEQEKFKrRMESEAMEAQEQL-----------SD 1091
Cdd:TIGR04523 26 NIANKQDTEEKQLEKKLKTIKNElknKEKELKNLDKNLnKDEEKINNSNNKIK-ILEQQIKDLNDKLkknkdkinklnSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1092 LGMLSSELRGSLAQK---EKEITSLQGRLEEEgarraeaQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEA 1168
Cdd:TIGR04523 105 LSKINSEIKNDKEQKnklEVELNKLEKQKKEN-------KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1169 LRTELEDTLDSTAAQQELRSRREAELSELQRCVEEEtrrhetqlselrvkhsaalDSLQEQLDNSKRARQSLEKAKATLE 1248
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-------------------KSLESQISELKKQNNQLKDNIEKKQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1249 EERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLR----- 1323
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKselkn 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1324 LAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNS 1403
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLES 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1404 AVEAGDEIRRKLQRELDSaiqrerqkeeekerverqrerlreeiedmtiaLQRERQnctALEKRQKKFdqclaeeKAVSA 1483
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKK--------------------------------LQQEKE---LLEKEIERL-------KETII 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1484 RLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLR 1563
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1564 IQTQELEEELSEaensrlrlevtLQALKAQFEREISTNEEKGEE-----KRRALSKQVRELEIQLEEERSQRSQSVSSKK 1638
Cdd:TIGR04523 517 KKISSLKEKIEK-----------LESEKKEKESKISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1988774931 1639 QLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRE 1678
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
675-699 |
8.95e-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: 45.03 E-value: 8.95e-05
10 20
....*....|....*....|....*
gi 1988774931 675 YKESLTKLMATLRNTNPNFLRCIIP 699
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
958-1277 |
9.99e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 958 QLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEvTDQLTEEE 1037
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE-GDHLRNVQ 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1038 EKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRL 1117
Cdd:pfam15921 548 TECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1118 EEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALR-------TELEDTLDS-----TAAQQE 1185
Cdd:pfam15921 628 SDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKrnfrnksEEMETTTNKlkmqlKSAQSE 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1186 LRSRREAELSelqrcvEEETRRHETQLSELRVKHSAA----LDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKS- 1260
Cdd:pfam15921 708 LEQTRNTLKS------MEGSDGHAMKVAMGMQKQITAkrgqIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTv 781
|
330 340
....*....|....*....|....*..
gi 1988774931 1261 ----------LQASRSESERGRKRADN 1277
Cdd:pfam15921 782 ateknkmageLEVLRSQERRLKEKVAN 808
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
864-1669 |
1.02e-04 |
|
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: 47.73 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 864 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLleeKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLG 943
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEI---KALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 944 ELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLE 1023
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1024 ERL--NEVTDQLTEEEEKTKSLNKLKNKQEAviadlEERLKREEQGRLEQEK--FKRRMESEAMEAQEQLSDLGMLSSEL 1099
Cdd:TIGR00606 389 ERQikNFHTLVIERQEDEAKTAAQLCADLQS-----KERLKQEQADEIRDEKkgLGRTIELKKEILEKKQEELKFVIKEL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1100 RgSLAQKEKEITSLqgrleEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEdtlds 1179
Cdd:TIGR00606 464 Q-QLEGSSDRILEL-----DQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTT----- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1180 TAAQQELRSRREAELSElqrcveeetrrhetQLSELRVKHSAALDSLQEQLDNSKRARQ---SLEKAKATLEEERQNLTS 1256
Cdd:TIGR00606 533 TRTQMEMLTKDKMDKDE--------------QIRKIKSRHSDELTSLLGYFPNKKQLEDwlhSKSKEINQTRDRLAKLNK 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1257 ELKSLQASRSESERGRKRADNQLQELSARLAQAdREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLH 1336
Cdd:TIGR00606 599 ELASLEQNKNHINNELESKEEQLSSYEDKLFDV-CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQ 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1337 DARELLQDESRQKMALASRVRALEeekNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQ 1416
Cdd:TIGR00606 678 SCCPVCQRVFQTEAELQEFISDLQ---SKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1417 ---RELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQnctaLEKRQKKFDQCLAEEKAVSARLAEERDRAE 1493
Cdd:TIGR00606 755 kvnRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQME----LKDVERKIAQQAAKLQGSDLDRTVQQVNQE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1494 ADSREKETRclALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHEleraRRTLETEAQNLRIQTQELEEEL 1573
Cdd:TIGR00606 831 KQEKQHELD--TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR----RQQFEEQLVELSTEVQSLIREI 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1574 SEAENSRLRLEVTLQALKAQFEREISTNEE---KGEEKRRALSKQVRELEIQLEE-ERSQRSQSVSSKKQLEAELQEAEA 1649
Cdd:TIGR00606 905 KDAKEQDSPLETFLEKDQQEKEELISSKETsnkKAQDKVNDIKEKVKNIHGYMKDiENKIQDGKDDYLKQKETELNTVNA 984
|
810 820
....*....|....*....|
gi 1988774931 1650 QVETANRGKEEAMKQLRRLQ 1669
Cdd:TIGR00606 985 QLEECEKHQEKINEDMRLMR 1004
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1008-1325 |
1.09e-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: 47.64 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1008 AVEQRERLGKEKKQL---EERLNEVTDQLTEEEEKTKSL-----------NKLKN---KQEAV------IADLEERLkrE 1064
Cdd:COG3096 287 ALELRRELFGARRQLaeeQYRLVEMARELEELSARESDLeqdyqaasdhlNLVQTalrQQEKIeryqedLEELTERL--E 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1065 EQG---------RLEQEKFKRRMESEAMEAQEQLSD----LGMLSS-------------ELRGSLAQKEKEITSLQGRLE 1118
Cdd:COG3096 365 EQEevveeaaeqLAEAEARLEAAEEEVDSLKSQLADyqqaLDVQQTraiqyqqavqaleKARALCGLPDLTPENAEDYLA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1119 EEGARRAEAQRSLREALSQVSELKEEV-ENERGM-----------RERAEKQRRDL----------SEELEALRTELEDt 1176
Cdd:COG3096 445 AFRAKEQQATEEVLELEQKLSVADAARrQFEKAYelvckiageveRSQAWQTARELlrryrsqqalAQRLQQLRAQLAE- 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1177 ldstaAQQELRSRREAE--LSELQRCVEEEtRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNL 1254
Cdd:COG3096 524 -----LEQRLRQQQNAErlLEEFCQRIGQQ-LDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKEL 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1255 TSE----------LKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRL 1324
Cdd:COG3096 598 AARapawlaaqdaLERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRLLAL 677
|
.
gi 1988774931 1325 A 1325
Cdd:COG3096 678 A 678
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
994-1289 |
1.29e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 994 LETKVKSLETDLATA---VEQRERLGKEKKQLEERLNEVTDQLTEeeeKTKSLNKLKNKQEAVIAdleERLKREEQGRLE 1070
Cdd:PRK11281 54 LEAEDKLVQQDLEQTlalLDKIDRQKEETEQLKQQLAQAPAKLRQ---AQAELEALKDDNDEETR---ETLSTLSLRQLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1071 QEKFKRRmeSEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEegarraeaqrsLREALSQVSELKEEVENERG 1150
Cdd:PRK11281 128 SRLAQTL--DQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ-----------IRNLLKGGKVGGKALRPSQR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1151 MRERAEKQRRDLSEELEalRTELEdtlDSTAAQQELRSRREaELSELQRCVEeetrrHETQLselrvkhsaaldsLQEQL 1230
Cdd:PRK11281 195 VLLQAEQALLNAQNDLQ--RKSLE---GNTQLQDLLQKQRD-YLTARIQRLE-----HQLQL-------------LQEAI 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774931 1231 dNSKRARQSLEKAKatlEEERQNLTSELKSLQASRSESERGRKradnqlqeLSARLAQA 1289
Cdd:PRK11281 251 -NSKRLTLSEKTVQ---EAQSQDEAARIQANPLVAQELEINLQ--------LSQRLLKA 297
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1072-1539 |
1.33e-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: 47.04 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1072 EKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGM 1151
Cdd:pfam05557 12 SQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1152 RERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHeTQLSELRVKHSAALDSLQEQLD 1231
Cdd:pfam05557 92 LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKA-SEAEQLRQNLEKQQSSLAEAEQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1232 NSKRARQSLEkakatLEEERQNLTSELKSLQASRSESERGRKRadnqLQELSARLAQADREREDREERMHKLQCEIESLS 1311
Cdd:pfam05557 171 RIKELEFEIQ-----SQEQDSEIVKNSKSELARIPELEKELER----LREHNKHLNENIENKLLLKEEVEDLKRKLEREE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1312 GnlssSDSKSLRLAKEISSLESQLHDARELLQD---ESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHS 1388
Cdd:pfam05557 242 K----YREEAATLELEKEKLEQELQSWVKLAQDtglNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1389 QQLTELRKQSEEVNSAVEAGDEIRRKLQRELD---------SAIQRERQKEEEKERVERQRERLREEIEDMTIALQR--- 1456
Cdd:pfam05557 318 QELAQYLKKIEDLNKKLKRHKALVRRLQRRVLlltkerdgyRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAhne 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1457 --ERQNCTALEKRQKKFDQCLAEEKAVSARLAEErdrAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQL 1534
Cdd:pfam05557 398 emEAQLSVAEEELGGYKQQAQTLERELQALRQQE---SLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERR 474
|
....*
gi 1988774931 1535 VNQQD 1539
Cdd:pfam05557 475 CLQGD 479
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
959-1720 |
1.38e-04 |
|
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: 47.04 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 959 LANEKKKMQQNIQDLeeqleeeesarqrllleKVTLETKVKSLETdlataveqrerlgkeKKQLEErlnevtDQLTEEEE 1038
Cdd:pfam15921 129 MADIRRRESQSQEDL-----------------RNQLQNTVHELEA---------------AKCLKE------DMLEDSNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1039 KTKSLNKLKNKQEAVIADLEERLKreeqgRLEQEKFKRRMESEAMEAQEQLSdlgmLSSELRGSLAQKEKEITSLQGRL- 1117
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSILV-----DFEEASGKKIYEHDSMSTMHFRS----LGSAISKILRELDTEISYLKGRIf 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1118 ---EEEGARRAEAQRSLREALSQVSELKEEVENER-----GMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSR 1189
Cdd:pfam15921 242 pveDQLEALKSESQNKIELLLQQHQDRIEQLISEHeveitGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1190 REAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEqldnSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESE 1269
Cdd:pfam15921 322 LESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTE----ARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1270 RGRKR-----------ADNQLQELSARLAQADREREDREERMHKLQCEIESlsgNLSSSDSKSLRLAKeISSLESQLHDA 1338
Cdd:pfam15921 398 EQNKRlwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMER---QMAAIQGKNESLEK-VSSLTAQLEST 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1339 RELL----QDESRQKMALASRVRALEEEKNGLmerleeeeergKELSRQIQTHSQQLTELRKQS----EEVNSAVEAGDE 1410
Cdd:pfam15921 474 KEMLrkvvEELTAKKMTLESSERTVSDLTASL-----------QEKERAIEATNAEITKLRSRVdlklQELQHLKNEGDH 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1411 IrRKLQRELDSaiqrerqKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERD 1490
Cdd:pfam15921 543 L-RNVQTECEA-------LKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKD 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1491 RAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQ----QDDVGKNVHELERARRTLETEAQNLRIQT 1566
Cdd:pfam15921 615 KKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEvktsRNELNSLSEDYEVLKRNFRNKSEEMETTT 694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1567 QELEEELSEAENSRLRLEVTLQALKAQ--FEREISTNEEKGEEKRRAlskQVRELEIQLEEERSQRSQSVSSKKQLEAEL 1644
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTLKSMEGSdgHAMKVAMGMQKQITAKRG---QIDALQSKIQFLEEAMTNANKEKHFLKEEK 771
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774931 1645 QEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEV--LHLTEELAVSERQ 1720
Cdd:pfam15921 772 NKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESvrLKLQHTLDVKELQ 849
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1099-1611 |
1.58e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1099 LRGSLAQKEKEITSLQGRLEEEGARRAEAQRS-LREALSQVSELKEEVENergmRERAEKQRRDLSEELEALRTELEDtl 1177
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEeLKEAEEKEEEYAELQEE----LEELEEELEELEAELEELREELEK-- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1178 dstAAQQELRSRREAELSELQRCVEEETRRhetqlselrvkhsaaLDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSE 1257
Cdd:COG4717 121 ---LEKLLQLLPLYQELEALEAELAELPER---------------LEELEERLEELRELEEELEELEAELAELQEELEEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1258 LKSLQASrsesergrkrADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLsssdsKSLRLAKEISSLESQLHD 1337
Cdd:COG4717 183 LEQLSLA----------TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL-----EQLENELEAAALEERLKE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1338 ARELLqdesrqkmALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQR 1417
Cdd:COG4717 248 ARLLL--------LIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1418 ELDSAIQRERQKEEEKERVERQRERLREeiedmtiALQRERQNCTALEKRqkkfdqclAEEKAVSARLAEERDRAEADSR 1497
Cdd:COG4717 320 ELEELLAALGLPPDLSPEELLELLDRIE-------ELQELLREAEELEEE--------LQLEELEQEIAALLAEAGVEDE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1498 EKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDvgknvHELERARRTLETEAQNLRIQTQELEEELSEAE 1577
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEELEELREELAELE 459
|
490 500 510
....*....|....*....|....*....|....*.
gi 1988774931 1578 N--SRLRLEVTLQALKAQFEREISTNEEKGEEKRRA 1611
Cdd:COG4717 460 AelEQLEEDGELAELLQELEELKAELRELAEEWAAL 495
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1008-1281 |
1.67e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1008 AVEQRERLgkekKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQgRLEQEKFKRRMESE------ 1081
Cdd:pfam02029 15 AREERRRQ----KEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTA-KREERRQKRLQEALerqkef 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1082 ---AMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGAR---RAEAQRSLREALSQVSELKEEVENERGMRERA 1155
Cdd:pfam02029 90 dptIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEireKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1156 EKQR-RDLSEELEALRTELEDTLDSTAAQQELRSRRE-----AELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQ 1229
Cdd:pfam02029 170 PTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEvksqnGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQK 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 1230 LDNSKRARQSLEKAKAT-LEEERQNLTSELKSLQASR-------SESERGRK--RADNQLQE 1281
Cdd:pfam02029 250 LEELRRRRQEKESEEFEkLRQKQQEAELELEELKKKReerrkllEEEEQRRKqeEAERKLRE 311
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
994-1245 |
1.87e-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: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 994 LETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREeqgrleqek 1073
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1074 fkrrmeseAMEAQEQLSDLGMLSSeLRGSlaqkeKEITSLQGRLEeegaRRAEAQRSLREALSQVSELKEEVENERgmrE 1153
Cdd:COG3883 92 --------ARALYRSGGSVSYLDV-LLGS-----ESFSDFLDRLS----ALSKIADADADLLEELKADKAELEAKK---A 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1154 RAEKQRrdlsEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNS 1233
Cdd:COG3883 151 ELEAKL----AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
250
....*....|..
gi 1988774931 1234 KRARQSLEKAKA 1245
Cdd:COG3883 227 AAAAAAAAAAAA 238
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
868-1215 |
2.10e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 868 QDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGELET 947
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 948 RLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLn 1027
Cdd:pfam07888 123 QRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSL- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1028 evtdqlteeEEKTKSLNKLKNKqeavIADLEERLKREEQGRLEQEKFKRRMES--EAMEAQEQLSDLgmLSSELRGSLAQ 1105
Cdd:pfam07888 202 ---------AQRDTQVLQLQDT----ITTLTQKLTTAHRKEAENEALLEELRSlqERLNASERKVEG--LGEELSSMAAQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1106 KEKEITSL-QGRLE--EEGARRAEAQRSLREALSQVSELKE------EVENERGMRERAEKQRRD--LSEEL---EALRT 1171
Cdd:pfam07888 267 RDRTQAELhQARLQaaQLTLQLADASLALREGRARWAQEREtlqqsaEADKDRIEKLSAELQRLEerLQEERmerEKLEV 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1988774931 1172 ELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSEL 1215
Cdd:pfam07888 347 ELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
867-1124 |
2.48e-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: 46.27 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 867 RQDEEIQTREAALQKAK-EQLTRAEQDYTELDRKHAQLLEekAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGEL 945
Cdd:pfam17380 360 RELERIRQEEIAMEISRmRELERLQMERQQKNERVRQELE--AARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 946 ETRLEEEEERGVQLANEKKKMQQNIQdlEEQLEEEESARQRLLLEKVtletkvkslETDLATAVEQRerlgkeKKQLEER 1025
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVE--RLRQQEEERKRKKLELEKE---------KRDRKRAEEQR------RKILEKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1026 LNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRmeseamEAQEQLsdlgMLSSELRGSLAQ 1105
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR------RIQEQM----RKATEERSRLEA 570
|
250
....*....|....*....
gi 1988774931 1106 KEKEITSLQGRLEEEGARR 1124
Cdd:pfam17380 571 MEREREMMRQIVESEKARA 589
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
864-1049 |
2.70e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 864 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRK----HAQLLEEKAVLADQLQAEAELFAEAEEMR-------ARLA 932
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEiaelRAELEAQKEELAELLRALYRLGRQPPLALllspedfLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 933 SRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQR 1012
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
170 180 190
....*....|....*....|....*....|....*..
gi 1988774931 1013 ERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNK 1049
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1323-1724 |
3.10e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1323 RLAKEISSLESQLHDARELLQ--DESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEE 1400
Cdd:COG4717 92 ELQEELEELEEELEELEAELEelREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1401 VNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRER---QNCTALEKRQKKFDQCLAE 1477
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELeqlENELEAAALEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1478 EKAVSARLAEERDRAEADSREKE-------------TRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGkn 1544
Cdd:COG4717 252 LLIAAALLALLGLGGSLLSLILTiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALG-- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1545 vheLERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEE------KGEEKRRALSKQVRE 1618
Cdd:COG4717 330 ---LPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelraalEQAEEYQELKEELEE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1619 LEIQLEEER--SQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVL--RELDDSKVTRDDVISQSK 1694
Cdd:COG4717 407 LEEQLEELLgeLEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELR 486
|
410 420 430
....*....|....*....|....*....|
gi 1988774931 1695 DSEKKIQTLEAEVLHLTEELAVSERQKRQA 1724
Cdd:COG4717 487 ELAEEWAALKLALELLEEAREEYREERLPP 516
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1488-1679 |
3.30e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1488 ERDRAEADSREK--ETRCLALSRALQEAQDQKEELERANK--QLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLR 1563
Cdd:COG3206 167 ELRREEARKALEflEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1564 IQTQELEEELSEAENSRL--RLEVTLQALKAQfEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQsvsskkQLE 1641
Cdd:COG3206 247 AQLGSGPDALPELLQSPViqQLRAQLAELEAE-LAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA------SLE 319
|
170 180 190
....*....|....*....|....*....|....*...
gi 1988774931 1642 AELQEAEAQVETANRGKEEAMKQLRRLQGQMKEvLREL 1679
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAE-LRRL 356
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1127-1363 |
3.44e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1127 AQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRcveeetr 1206
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1207 rhetQLSELRvkhsAALDSLQEQLDNSKRARQSLEKA-KATLEEERQNLTSELKSLQASRSESERGRKRADnQLQELSAR 1285
Cdd:COG4942 91 ----EIAELR----AELEAQKEELAELLRALYRLGRQpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774931 1286 LAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEK 1363
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1221-1366 |
3.71e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1221 AALDSLQE---QLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLA--QADRERED 1295
Cdd:COG1579 7 RALLDLQEldsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyEEQLGNVR 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774931 1296 REERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQ----KMALASRVRALEEEKNGL 1366
Cdd:COG1579 87 NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekKAELDEELAELEAELEEL 161
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
985-1218 |
3.92e-04 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 44.63 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 985 QRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIAD-------L 1057
Cdd:pfam04849 90 QSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHgcvqldaL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1058 EERLKR--EEQGRLEQEKFKRRMESEAMEAQEQlsdlgMLSSELRGSLAQKEKEItslqGRLEEEGARRAEAQRSLREA- 1134
Cdd:pfam04849 170 QEKLRGleEENLKLRSEASHLKTETDTYEEKEQ-----QLMSDCVEQLSEANQQM----AELSEELARKMEENLRQQEEi 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1135 ---LSQVSELkeevenergmreraEKQRRDLSEELEALRTELEDTLDstaAQQELRSrreaELSELQ-RCVEEETRRHET 1210
Cdd:pfam04849 241 tslLAQIVDL--------------QHKCKELGIENEELQQHLQASKE---AQRQLTS----ELQELQdRYAECLGMLHEA 299
|
250
....*....|
gi 1988774931 1211 Q--LSELRVK 1218
Cdd:pfam04849 300 QeeLKELRKK 309
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1102-1270 |
4.56e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.09 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1102 SLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRD------LSEELEALRTELED 1175
Cdd:PRK12705 23 VLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREeerlvqKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1176 TLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLT 1255
Cdd:PRK12705 103 LENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNIL 182
|
170
....*....|....*
gi 1988774931 1256 SELKSLQASRSESER 1270
Cdd:PRK12705 183 AQAMQRIASETASDL 197
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1077-1230 |
4.70e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1077 RMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRE--- 1153
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyea 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1154 ------RAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQ 1227
Cdd:COG1579 94 lqkeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
...
gi 1988774931 1228 EQL 1230
Cdd:COG1579 174 PEL 176
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1154-1534 |
4.78e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1154 RAEKQRRDLSEELEALRTELEDTLDSTAAQQELrsrreaeLSELQRCVEEETRRhetqLSELRVKHSAALDSL------- 1226
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYR-------LVEMARELAELNEA----ESDLEQDYQAASDHLnlvqtal 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1227 --QEQLdnsKRARQSLEKAKATLEEerQNLTSELKSLQasRSESERGRKRADNQLQELSARLA----------------- 1287
Cdd:PRK04863 345 rqQEKI---ERYQADLEELEERLEE--QNEVVEEADEQ--QEENEARAEAAEEEVDELKSQLAdyqqaldvqqtraiqyq 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1288 QADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLqDESRQKMALA-------SRVRALE 1360
Cdd:PRK04863 418 QAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAH-SQFEQAYQLVrkiagevSRSEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1361 EEKNGLmerleEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQR 1440
Cdd:PRK04863 497 VARELL-----RRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1441 ERLREEIEDMTiALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEEL 1520
Cdd:PRK04863 572 ESVSEARERRM-ALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDEL 650
|
410
....*....|....
gi 1988774931 1521 ERANKQLRLEMEQL 1534
Cdd:PRK04863 651 AARKQALDEEIERL 664
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1598-1928 |
4.88e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1598 ISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLR 1677
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1678 ELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVN 1757
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1758 QLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAAL 1837
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1838 EAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQ 1917
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
330
....*....|.
gi 1988774931 1918 KRKLQRELEEL 1928
Cdd:COG4372 349 GLLDNDVLELL 359
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
876-1284 |
4.91e-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: 45.33 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 876 EAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEaelfaeaeemRARLAsrkqeleevlgeletrleeeeer 955
Cdd:COG3096 291 RRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAA----------SDHLN----------------------- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 956 GVQLAnekKKMQQNIQdleeqleeeesaRQRLLLEKvtLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTE 1035
Cdd:COG3096 338 LVQTA---LRQQEKIE------------RYQEDLEE--LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1036 -----EEEKTKSLnklkNKQEAVIAdLEERLKREEQGRLEQEKFKRRMesEAMEAQEQLSDLGMLSSELRGSLAQKEKE- 1109
Cdd:COG3096 401 yqqalDVQQTRAI----QYQQAVQA-LEKARALCGLPDLTPENAEDYL--AAFRAKEQQATEEVLELEQKLSVADAARRq 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1110 -------ITSLQGRLEeegarRAEAQRSLREALSQVSELKEEVENERGMR------ERAEKQRRDLSEELEAL----RTE 1172
Cdd:COG3096 474 fekayelVCKIAGEVE-----RSQAWQTARELLRRYRSQQALAQRLQQLRaqlaelEQRLRQQQNAERLLEEFcqriGQQ 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1173 LEDTLDSTAAQQELRSRREAELSELQRCVEE--ETRRHETQL----SELRVKH------SAALDSLQEQLDnskrarQSL 1240
Cdd:COG3096 549 LDAAEELEELLAELEAQLEELEEQAAEAVEQrsELRQQLEQLrariKELAARApawlaaQDALERLREQSG------EAL 622
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1988774931 1241 EKAKAtLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSA 1284
Cdd:COG3096 623 ADSQE-VTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1179-1408 |
5.64e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1179 STAAQQELRSRREAELSELQrcveEETRRHETQLSELRVKHSAA---LDSLQEQLDNSKRARQSLEKAKATLEEERQNLT 1255
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQ----QEIAELEKELAALKKEEKALlkqLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1256 SELKSLQASRSESERGRKRADNQLQELSAR-----------LAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRL 1324
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1325 AKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSA 1404
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
....
gi 1988774931 1405 VEAG 1408
Cdd:COG4942 250 ALKG 253
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1153-1947 |
5.94e-04 |
|
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: 45.04 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1153 ERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQrCVEEETRRHETQLSEL--RVKHSAALDSLQEQL 1230
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLE-SSREIVKSYENELDPLknRLKEIEHNLSKIMKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1231 DNSKRARQSLEKakatleeERQNLTSELKSLQasrsesERGRKRADNQLQELSARLAQADREREDREERMHKlqcEIESL 1310
Cdd:TIGR00606 268 DNEIKALKSRKK-------QMEKDNSELELKM------EKVFQGTDEQLNDLYHNHQRTVREKERELVDCQR---ELEKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1311 SGNLSSSDSKSLRLAKEIS--SLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHS 1388
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGrlQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1389 QQLTELrkqSEEVNSAVEAGDEIRRKlQRELDSAIQRERQKEEEKERVERQRerlreeiedmtialQRERQNCTALEKRQ 1468
Cdd:TIGR00606 412 QLCADL---QSKERLKQEQADEIRDE-KKGLGRTIELKKEILEKKQEELKFV--------------IKELQQLEGSSDRI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1469 KKFDQCLAEEKAvsaRLAEERDRAEADSREKETRCLalsralqeaQDQKEELERANKQLRLEMEQLvNQQDDVGKNVHEL 1548
Cdd:TIGR00606 474 LELDQELRKAER---ELSKAEKNSLTETLKKEVKSL---------QNEKADLDRKLRKLDQEMEQL-NHHTTTRTQMEML 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1549 ERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALkaqfereiSTNEEKGEEKRRALSKQVRELE-----IQL 1623
Cdd:TIGR00606 541 TKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSK--------SKEINQTRDRLAKLNKELASLEqnknhINN 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1624 EEERSQRSQSVSSKKQLEA-ELQEAEAQVETANRGKEEAMKQLRRLQGQM---KEVLRELDDSKVTRDDVISQSKDSEKK 1699
Cdd:TIGR00606 613 ELESKEEQLSSYEDKLFDVcGSQDEESDLERLKEEIEKSSKQRAMLAGATavySQFITQLTDENQSCCPVCQRVFQTEAE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1700 IQT----LEAEVLHLTEELAVSERQKRQAQQERDEIadeMVSSSSGKNVLSEEKRRLDArvnqleeeleeeqtnnelLTE 1775
Cdd:TIGR00606 693 LQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEM---LGLAPGRQSIIDLKEKEIPE------------------LRN 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1776 RLRKTALQVETLTVQLQGERTLAQKAEAAreqlEKQNKELKARLGEMEgavrgKHRMSVAALEAKIETMEEQLEQERQER 1855
Cdd:TIGR00606 752 KLQKVNRDIQRLKNDIEEQETLLGTIMPE----EESAKVCLTDVTIME-----RFQMELKDVERKIAQQAAKLQGSDLDR 822
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1856 AIANKLMRKTEK--KLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEensrSSAQKRKLQRELEELTDSSQ 1933
Cdd:TIGR00606 823 TVQQVNQEKQEKqhELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGT----NLQRRQQFEEQLVELSTEVQ 898
|
810
....*....|....
gi 1988774931 1934 TMNREISSLRNQLS 1947
Cdd:TIGR00606 899 SLIREIKDAKEQDS 912
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
958-1174 |
7.16e-04 |
|
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: 44.63 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 958 QLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEE 1037
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1038 EKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRL 1117
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL 547
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774931 1118 EE--EGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELE 1174
Cdd:TIGR04523 548 NKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1058-1189 |
8.21e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.59 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1058 EERLKREEQGRLEQEKFKRRMESEAMEAQEQLSdlgmlSSELRgslaqkeKEITSLQGRLEEEGARRAEAQRSLREALSQ 1137
Cdd:pfam09787 55 ERDLLREEIQKLRGQIQQLRTELQELEAQQQEE-----AESSR-------EQLQELEEQLATERSARREAEAELERLQEE 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 1138 VSELKEEVENERGMREraeKQRRDLSEELEALRTELEDTLDSTAAQQELRSR 1189
Cdd:pfam09787 123 LRYLEEELRRSKATLQ---SRIKDREAEIEKLRNQLTSKSQSSSSQSELENR 171
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
879-1257 |
8.34e-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: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 879 LQKAKEQLTRAEQDYTElDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLasRKQELEEVLGELETRLEEEEERGVQ 958
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE-KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEM--DRQAAIYAEQERMAMERERELERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 959 LANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKsletdlatavEQRERLGKEKKQLEERLNEVTDQLTEEEE 1038
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVR----------QELEAARKVKILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1039 KTKSLNKLKNKQEAVIAdlEERLKREEQGRLEQekfkrrmeseaMEAQEQLSDLgmlsselrgslaqkekeitslqgRLE 1118
Cdd:pfam17380 425 IRAEQEEARQREVRRLE--EERAREMERVRLEE-----------QERQQQVERL-----------------------RQQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1119 EEGARRAeaqrslrealsqvselKEEVENERGMRERAEKQRRD-LSEELEALRTE-LEDTLDSTAAQQELRSRREAELSE 1196
Cdd:pfam17380 469 EEERKRK----------------KLELEKEKRDRKRAEEQRRKiLEKELEERKQAmIEEERKRKLLEKEMEERQKAIYEE 532
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774931 1197 LQRCVEEETRRHETQLSELRvkhsaaldSLQEQLDNSKRARQSLEKAKATLEEERQNLTSE 1257
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERR--------RIQEQMRKATEERSRLEAMEREREMMRQIVESE 585
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1028-1196 |
8.60e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.62 E-value: 8.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1028 EVTDQLTEE----------EEKTKSlnklknkQEAVIADLEERLKREEQGRLEQEKFKRRMESEameaqeqlsdlgmlss 1097
Cdd:PTZ00491 639 EPVDERTRDslqksvqlaiEITTKS-------QEAAARHQAELLEQEARGRLERQKMHDKAKAE---------------- 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1098 ELRGSLAQKEKEITSlqgrLEEEGARRAEAqrslrEALSQVSELKEEVENERGmRERAEKQRRDLSEELEALRTELEDTL 1177
Cdd:PTZ00491 696 EQRTKLLELQAESAA----VESSGQSRAEA-----LAEAEARLIEAEAEVEQA-ELRAKALRIEAEAELEKLRKRQELEL 765
|
170
....*....|....*....
gi 1988774931 1178 DSTAAQQELRSRREAELSE 1196
Cdd:PTZ00491 766 EYEQAQNELEIAKAKELAD 784
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
997-1250 |
8.61e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.09 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 997 KVKSLETDLATAVEQ--------RERLGKEKkqLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEE---RLK--- 1062
Cdd:COG2268 98 KVNSDPEDIANAAERflgrdpeeIEELAEEK--LEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKnglELEsva 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1063 ----REEQGRLEQEKFKRRMESEAMEAQEQlsdlgmlsselrgSLAQKEKEITSLQGRLEEEGARrAEAQRslrealsqv 1138
Cdd:COG2268 176 itdlEDENNYLDALGRRKIAEIIRDARIAE-------------AEAERETEIAIAQANREAEEAE-LEQER--------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1139 selkeEVENERGMRERAEKQRRDLSEELEALRTELEdtldstaAQQELRSRREAELSELQRCVEEETRRHETQLSELRVK 1218
Cdd:COG2268 233 -----EIETARIAEAEAELAKKKAEERREAETARAE-------AEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAE 300
|
250 260 270
....*....|....*....|....*....|..
gi 1988774931 1219 HSaaldslQEQLDNSKRARQSLEKAKATLEEE 1250
Cdd:COG2268 301 RE------EAELEADVRKPAEAEKQAAEAEAE 326
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
826-1197 |
8.73e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 826 KKQQQLSALRVMQRNCAAYLKLRNWQWWRLFTKVkpLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLE 905
Cdd:COG4717 164 ELEELEAELAELQEELEELLEQLSLATEEELQDL--AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 906 EKAVlaDQLQAEAELFAEAEEMRARLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQ 985
Cdd:COG4717 242 EERL--KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 986 RL--LLEKVTLETKV-KSLETDLATAVEQRERLGKEKKQLEERLnevtDQLTEEEEKTKSLNKLKNKQEAVIADLEERLK 1062
Cdd:COG4717 320 ELeeLLAALGLPPDLsPEELLELLDRIEELQELLREAEELEEEL----QLEELEQEIAALLAEAGVEDEEELRAALEQAE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1063 REEQGRLEQEKFKRRMESEAMEAQEQLSDLgmlsselrgSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELK 1142
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEAL---------DEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774931 1143 E--EVENERGMRERAEKQRRDLSEELEALRTeLEDTLDstAAQQELRSRREAELSEL 1197
Cdd:COG4717 467 EdgELAELLQELEELKAELRELAEEWAALKL-ALELLE--EAREEYREERLPPVLER 520
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1606-1734 |
8.79e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1606 EEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQG--QMKEVLRELDDSK 1683
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLK 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1988774931 1684 VTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADE 1734
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1021-1154 |
8.95e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1021 QLEERLNEVTDQLTEEEEKtkslnklKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELR 1100
Cdd:PRK11637 174 ELKQTREELAAQKAELEEK-------QSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLR 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1988774931 1101 GSLAQKEKEItslQGRLEEEgARRAEAQRSLREALSQVSELKEEVENERGMRER 1154
Cdd:PRK11637 247 DSIARAEREA---KARAERE-AREAARVRDKQKQAKRKGSTYKPTESERSLMSR 296
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
963-1242 |
9.48e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 43.65 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 963 KKKMQQNIQDLEEQLEEEESARqRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEeeeKTKS 1042
Cdd:pfam15905 62 KKKSQKNLKESKDQKELEKEIR-ALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLE---LTRV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1043 LNKLKNKQEAviadlEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGA 1122
Cdd:pfam15905 138 NELLKAKFSE-----DGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1123 RRAEAQrslrealSQVSELKEEVENERGMRERAEKQRRD---LSEELEALRTELEDTLDSTAAQQELRSRREAELSELQR 1199
Cdd:pfam15905 213 EKIEEK-------SETEKLLEYITELSCVSEQVEKYKLDiaqLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCK 285
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1988774931 1200 CVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEK 1242
Cdd:pfam15905 286 LLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
992-1165 |
1.09e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 992 VTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNklknkQEAVIADLEERLKREEQGRLEQ 1071
Cdd:COG3206 208 VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL-----QSPVIQQLRAQLAELEAELAEL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1072 EKFKRRMESEAMEAQEQLSDL-GMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQ---RSLREALSQVSELKEEVEN 1147
Cdd:COG3206 283 SARYTPNHPDVIALRAQIAALrAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEarlAELPELEAELRRLEREVEV 362
|
170
....*....|....*...
gi 1988774931 1148 ERGMRERAEKQRRDLSEE 1165
Cdd:COG3206 363 ARELYESLLQRLEEARLA 380
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1640-1946 |
1.12e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1640 LEAELQEAEAQVETANRGKEEAMKQLrrlqGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSER 1719
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETR----DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1720 QKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLT---ERLRKTALQVETLTVQLQGE-R 1795
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNeeaESLREDADDLEERAEELREEaA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1796 TLAQKAEAAREQLEKQN---KELKARLGEMEGAV--------------------RGKHRMSVAALEAKIETMEEQLEQER 1852
Cdd:PRK02224 367 ELESELEEAREAVEDRReeiEELEEEIEELRERFgdapvdlgnaedfleelreeRDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1853 QERAianklmrktEKKLKEVMMQAEDERR--HADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKrKLQRELEELTD 1930
Cdd:PRK02224 447 ALLE---------AGKCPECGQPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEE 516
|
330
....*....|....*.
gi 1988774931 1931 SSQTMNREISSLRNQL 1946
Cdd:PRK02224 517 RREDLEELIAERRETI 532
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1502-1815 |
1.23e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1502 RCLALSRALQEAQDQKEEL----ERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAE 1577
Cdd:pfam07888 28 RAELLQNRLEECLQERAELlqaqEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1578 NSRLRLEVTLQALKAQFEREISTNEEKgEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAE---LQEAEAQVETA 1654
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIREL-EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAErkqLQAKLQQTEEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1655 NRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQkrqAQQERDEIADE 1734
Cdd:pfam07888 187 LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERK---VEGLGEELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1735 MVSSSSGKNVLseEKRRLDArvnqleeeleeeqtnnELLTERLRKTALQVETLTVQLQGER-TLAQKAEAAREQLEKQNK 1813
Cdd:pfam07888 264 AAQRDRTQAEL--HQARLQA----------------AQLTLQLADASLALREGRARWAQEReTLQQSAEADKDRIEKLSA 325
|
..
gi 1988774931 1814 EL 1815
Cdd:pfam07888 326 EL 327
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1006-1260 |
1.29e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.12 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1006 ATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEaVIADLEERLKREEQGRLEQEKFKRRMESEAMEA 1085
Cdd:PLN02939 152 LQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVE-ILEEQLEKLRNELLIRGATEGLCVHSLSKELDV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1086 --QEQLS---DLGMLSSEL------RGSLAQKEKEITSLQGRLEEEGARRAEAQrslrEALSQVSELK-----EEVENER 1149
Cdd:PLN02939 231 lkEENMLlkdDIQFLKAELievaetEERVFKLEKERSLLDASLRELESKFIVAQ----EDVSKLSPLQydcwwEKVENLQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1150 GMRERAEK----------QRRDLSEELEALRTELEDTLDSTAA-------QQELRSRREaelsELQRCveeetrrHETQL 1212
Cdd:PLN02939 307 DLLDRATNqvekaalvldQNQDLRDKVDKLEASLKEANVSKFSsykvellQQKLKLLEE----RLQAS-------DHEIH 375
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1988774931 1213 SELRVKHsaalDSLQEQLDNSKRARQslEKAKATLEEERQNLTSELKS 1260
Cdd:PLN02939 376 SYIQLYQ----ESIKEFQDTLSKLKE--ESKKRSLEHPADDMPSEFWS 417
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1029-1249 |
1.34e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.79 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1029 VTDQLTEEEEKTKSLNK---LKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQ 1105
Cdd:pfam15709 305 VTGNMESEEERSEEDPSkalLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1106 KEKEITSLQGRLEEEGARRAEAQRSLRealsqvseLKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQE 1185
Cdd:pfam15709 385 RFEEIRLRKQRLEEERQRQEEEERKQR--------LQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKE 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774931 1186 LRSRREAELSELQRCVEEEtrrhetQLSELRVKHSAALDSLQEQldnSKRARQSLEKAKATLEE 1249
Cdd:pfam15709 457 LEMQLAEEQKRLMEMAEEE------RLEYQRQKQEAEEKARLEA---EERRQKEEEAARLALEE 511
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1505-1928 |
1.93e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1505 ALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGknvhELERARRTLETEAQNlriqtqeleeelseaenSRLRLE 1584
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQA-----------------ASDHLN 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1585 VTLQALKAQfereistneEKGEEKRRALSkqvrELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVET-----ANRGKE 1659
Cdd:PRK04863 339 LVQTALRQQ---------EKIERYQADLE----ELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDElksqlADYQQA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1660 EAMKQLRRLQ-GQMKEVLRE----LDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSE---RQKRQAQQERDEI 1731
Cdd:PRK04863 406 LDVQQTRAIQyQQAVQALERakqlCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQaahSQFEQAYQLVRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1732 ADEMVSS---SSGKNVL--SEEKRRLDARVNQLEEELEEEQTNNELL--TERLRKTALQVetLTVQLQGERTLAQKAEAA 1804
Cdd:PRK04863 486 AGEVSRSeawDVARELLrrLREQRHLAEQLQQLRMRLSELEQRLRQQqrAERLLAEFCKR--LGKNLDDEDELEQLQEEL 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1805 REQLEKQNKELkarlgEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEvmmqaederrhad 1884
Cdd:PRK04863 564 EARLESLSESV-----SEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFED------------- 625
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1988774931 1885 qyREQLDKSMvrlKQLKRQLEEVEEENSRSSAQKRKLQRELEEL 1928
Cdd:PRK04863 626 --SQDVTEYM---QQLLERERELTVERDELAARKQALDEEIERL 664
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
927-1362 |
2.13e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 927 MRARLASRKQELEEVLGELETRLeeeeergvqlanekkKMQQNIQDLEEQLEEEESARQRLllekVTLETKVKSLETDLa 1006
Cdd:pfam10174 142 MELRIETQKQTLGARDESIKKLL---------------EMLQSKGLPKKSGEEDWERTRRI----AEAEMQLGHLEVLL- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1007 tavEQRErlgKEKKQLEERLNEvTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEqgrLEQEKFKRRMESEAMEAQ 1086
Cdd:pfam10174 202 ---DQKE---KENIHLREELHR-RNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTEDRE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1087 EQLSDLGMLSS----------ELRGSLAQKEKEITSLQGRLEEEGARRAEAQRS---LREAL-----------SQVSELK 1142
Cdd:pfam10174 272 EEIKQMEVYKShskfmknkidQLKQELSKKESELLALQTKLETLTNQNSDCKQHievLKESLtakeqraailqTEVDALR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1143 EEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTaaqqELRSRREAELSELQRCVEEETRRHETQLSELRvkhsAA 1222
Cdd:pfam10174 352 LRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDML----DVKERKINVLQKKIENLQEQLRDKDKQLAGLK----ER 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1223 LDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSL-QASRSESERGRKradnQLQELSARLAQADREREDREERMH 1301
Cdd:pfam10174 424 VKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREdRERLEELESLKK----ENKDLKEKVSALQPELTEKESSLI 499
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774931 1302 KLQCEIESL--SGNLSSSDSKSLRLA-----KEISSLESQLHDARElLQDESRQKMALASRVRALEEE 1362
Cdd:pfam10174 500 DLKEHASSLasSGLKKDSKLKSLEIAveqkkEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQE 566
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1461-1680 |
2.52e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1461 CTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDD 1540
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1541 VGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKaQFEREISTNEEKGEEKRRALSKQVRELE 1620
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1621 IQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELD 1680
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1045-1178 |
2.71e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1045 KLKNKQEAVIADLEERLKREEQGRLEQEKFKRrmeSEAMEAQEQLSdlgmlssELRGSLAQKEKEITSLQGRLEEEgarr 1124
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKK---EQDEASFERLA-------ELRDELAELEEELEALKARWEAE---- 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1988774931 1125 aeaqrslREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLD 1178
Cdd:COG0542 467 -------KELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1104-1267 |
2.93e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.71 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1104 AQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRR------DLSEELEALRTELEDTL 1177
Cdd:pfam05667 331 QQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKvkkktlDLLPDAEENIAKLQALV 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1178 DSTAAQ-QELRSRREA----------ELSELQRCVEEETRRhetQLSELRvkhsaaldSLQEQLdnskraRQSLEKAKAT 1246
Cdd:pfam05667 411 DASAQRlVELAGQWEKhrvplieeyrALKEAKSNKEDESQR---KLEEIK--------ELREKI------KEVAEEAKQK 473
|
170 180
....*....|....*....|...
gi 1988774931 1247 lEEERQNLTSELKSL--QASRSE 1267
Cdd:pfam05667 474 -EELYKQLVAEYERLpkDVSRSA 495
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1007-1231 |
3.07e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 41.63 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1007 TAVEQRERLGKEKKQlEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQ 1086
Cdd:pfam06008 24 LTKQLQEYLSPENAH-KIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEIN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1087 EQLSDLGMLSSELRGS-LAQKEKEITSLQGRLEEE--GARRAEAQRSLREA---LSQVSELKEEVENE-RGMRERAEKQR 1159
Cdd:pfam06008 103 EKVATLGENDFALPSSdLSRMLAEAQRMLGEIRSRdfGTQLQNAEAELKAAqdlLSRIQTWFQSPQEEnKALANALRDSL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 1160 RDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVeEETRRHETQLSELRVKHSAALDSLQEQLD 1231
Cdd:pfam06008 183 AEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKK-EEVSEQKNQLEETLKTARDSLDAANLLLQ 253
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1085-1231 |
3.22e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 40.71 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1085 AQEQLSDLGMLSSELRGSLAQKEKEIT-SLQGRLEEEGARRAEAQRSLREALSQ-VSELKEEVENE-RGMRERAEKQRRD 1161
Cdd:pfam01442 13 AEELQEQLGPVAQELVDRLEKETEALReRLQKDLEEVRAKLEPYLEELQAKLGQnVEELRQRLEPYtEELRKRLNADAEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1162 LSEELEA----LRTELEDTLDSTAAQ-----QELRSRREAELSELQRCVEEETRRHETQLS----ELRVKHSAALDSLQE 1228
Cdd:pfam01442 93 LQEKLAPygeeLRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAEEVQAQLSqrlqELREKLEPQAEDLRE 172
|
...
gi 1988774931 1229 QLD 1231
Cdd:pfam01442 173 KLD 175
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1130-1289 |
3.57e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 40.32 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1130 SLREALSQVSELKEEVENERGMRERAEKQRrdLSEELEALRTELEDtlDSTAAQQELRSRREAELSELQRCVEEETRRHE 1209
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDR--LEKETEALRERLQK--DLEEVRAKLEPYLEELQAKLGQNVEELRQRLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1210 TQLSELRVKHSAALDSLQEQLDNS-----KRARQSLEKAKATL----EEERQNLTSELKSLQAS-RSESERGRKRADNQL 1279
Cdd:pfam01442 77 PYTEELRKRLNADAEELQEKLAPYgeelrERLEQNVDALRARLapyaEELRQKLAERLEELKESlAPYAEEVQAQLSQRL 156
|
170
....*....|
gi 1988774931 1280 QELSARLAQA 1289
Cdd:pfam01442 157 QELREKLEPQ 166
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1124-1284 |
3.61e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1124 RAEAQRSLREALSQVSELKEEVENErgmreraekqrrdLSEELEALRTELEdtldstaaqQELRSRREaelsELQRcVEE 1203
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALLE-------------AKEEIHKLRNEFE---------KELRERRN----ELQK-LEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1204 ETRRHEtqlselrvkhsaaldslqEQLDNSKrarQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELS 1283
Cdd:PRK12704 90 RLLQKE------------------ENLDRKL---ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIS 148
|
.
gi 1988774931 1284 A 1284
Cdd:PRK12704 149 G 149
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
870-1258 |
4.13e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 870 EEIQTREAALQKAkEQLTRAEQdytelDRKHAQLLEEKAvladqlqaeaelfaeaeemrarlasrkqeleevlgeletrl 949
Cdd:PTZ00121 1610 EEAKKAEEAKIKA-EELKKAEE-----EKKKVEQLKKKE----------------------------------------- 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 950 eeeeergvqlANEKKKMQQniqdleeqleeeesarqrllLEKVTLETKVKSLEtdLATAVEQRERLGKEKKQLEERLNEV 1029
Cdd:PTZ00121 1643 ----------AEEKKKAEE--------------------LKKAEEENKIKAAE--EAKKAEEDKKKAEEAKKAEEDEKKA 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1030 TDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEqlsdlgmlsselrgslAQKEKE 1109
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE----------------AKKDEE 1754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1110 ITSLQGRLEEEGARRAEAQRSLREALSQvSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSR 1189
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIE-EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIK 1833
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774931 1190 REAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSEL 1258
Cdd:PTZ00121 1834 EVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1012-1119 |
4.16e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1012 RERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERL----KREEQGRLEQE-KFKRRMESEAMEAQ 1086
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKeklqEEEDKLLEEAEkEAQQAIKEAKKEAD 587
|
90 100 110
....*....|....*....|....*....|...
gi 1988774931 1087 EQLSDLGMLssELRGSLAQKEKEITSLQGRLEE 1119
Cdd:PRK00409 588 EIIKELRQL--QKGGYASVKAHELIEARKRLNK 618
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
997-1199 |
4.36e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 997 KVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQE-------------AVIADLEERLKR 1063
Cdd:COG1340 72 KVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQtevlspeeekelvEKIKELEKELEK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1064 EEQGRLEQEKFKRrMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEegaRRAEAqrslREALSQVSELKE 1143
Cdd:COG1340 152 AKKALEKNEKLKE-LRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADE---LRKEA----DELHKEIVEAQE 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774931 1144 EVENERGMRERAEKQRRDLSEELEALRTELEDTLdSTAAQQELRSRREAELSELQR 1199
Cdd:COG1340 224 KADELHEEIIELQKELRELRKELKKLRKKQRALK-REKEKEELEEKAEEIFEKLKK 278
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1610-1735 |
4.38e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.57 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1610 RALSKQVRELEIQLEEERSQRSQSVSSKKQlEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVL---RELDDSKVTR 1686
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAvsqQELDEARAAL 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1988774931 1687 DDVISQSKDSEKKIQTLEAEVLhLTEELAVSERQKRQAQQERDEIADEM 1735
Cdd:COG1566 158 DAAQAQLEAAQAQLAQAQAGLR-EEEELAAAQAQVAQAEAALAQAELNL 205
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1021-1197 |
4.57e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.58 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1021 QLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLK------REEQGRLEQEKfKRRMESEAMEAQEQLSDLGM 1094
Cdd:COG1842 34 DMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARlalekgREDLAREALER-KAELEAQAEALEAQLAQLEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1095 LSSELRGSLAQKEKEITSLQGRLEEEGAR--RAEAQRSLREALSQVSElkeevENERGMRERAEKQRRDLSEELEALRT- 1171
Cdd:COG1842 113 QVEKLKEALRQLESKLEELKAKKDTLKARakAAKAQEKVNEALSGIDS-----DDATSALERMEEKIEEMEARAEAAAEl 187
|
170 180
....*....|....*....|....*.
gi 1988774931 1172 ELEDTLDSTAAQQELRSRREAELSEL 1197
Cdd:COG1842 188 AAGDSLDDELAELEADSEVEDELAAL 213
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
982-1725 |
4.89e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 982 SARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSL-NKLKNKQEA-------- 1052
Cdd:COG3096 333 SDHLNLVQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLkSQLADYQQAldvqqtra 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1053 -----VIADLEERLKREEQGRLEQEKFKRRMEseAMEAQEQLSDLGMLSSELRGSLAQKEKE--------ITSLQGRLEe 1119
Cdd:COG3096 413 iqyqqAVQALEKARALCGLPDLTPENAEDYLA--AFRAKEQQATEEVLELEQKLSVADAARRqfekayelVCKIAGEVE- 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1120 egarRAEAQRSLREALSQVSELKEEVENERGMR------ERAEKQRRDLSEELEAL----RTELEDTLDSTAAQQELRSR 1189
Cdd:COG3096 490 ----RSQAWQTARELLRRYRSQQALAQRLQQLRaqlaelEQRLRQQQNAERLLEEFcqriGQQLDAAEELEELLAELEAQ 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1190 REAELSELQRCVEE--ETRRHETQL----SELRVKH------SAALDSLQEQLDnskrarQSLEKAKAtLEEERQNLTSE 1257
Cdd:COG3096 566 LEELEEQAAEAVEQrsELRQQLEQLrariKELAARApawlaaQDALERLREQSG------EALADSQE-VTAAMQQLLER 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1258 LKSLQASRSESERGRKRADNQLQELSA-------RLAQADreredreermhklqceiESLSGNLSSS--DSKSLRLAKEI 1328
Cdd:COG3096 639 EREATVERDELAARKQALESQIERLSQpggaedpRLLALA-----------------ERLGGVLLSEiyDDVTLEDAPYF 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1329 SSL----------------ESQLHDARELLQDE---SRQKMALASRVRALEEEKNGLMERLEEeeergkelsRQIQ---- 1385
Cdd:COG3096 702 SALygparhaivvpdlsavKEQLAGLEDCPEDLyliEGDPDSFDDSVFDAEELEDAVVVKLSD---------RQWRysrf 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1386 ---------THSQQLTELRKQSEEVnsaVEAGDEIRRKLQReldsaiqrerqkeeekerverqrerlreeiedmtiaLQR 1456
Cdd:COG3096 773 pevplfgraAREKRLEELRAERDEL---AEQYAKASFDVQK------------------------------------LQR 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1457 ERQNctalekrqkkFDQCLAEEKAVsarlaeerdrAEADSREKETRclALSRALQEAQDQKEELERANKQLRLEMEQLVN 1536
Cdd:COG3096 814 LHQA----------FSQFVGGHLAV----------AFAPDPEAELA--ALRQRRSELERELAQHRAQEQQLRQQLDQLKE 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1537 QQDDVGKNVHELER-ARRTLETEAQNLRIQTQELEEELSEAENSRLRLEV------TLQALKAQFErEISTNEEKGEEKR 1609
Cdd:COG3096 872 QLQLLNKLLPQANLlADETLADRLEELREELDAAQEAQAFIQQHGKALAQleplvaVLQSDPEQFE-QLQADYLQAKEQQ 950
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1610 RALSKQV--------RELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQvetanrgKEEAMKQLRRLQGQMKEVLRELDD 1681
Cdd:COG3096 951 RRLKQQIfalsevvqRRPHFSYEDAVGLLGENSDLNEKLRARLEQAEEA-------RREAREQLRQAQAQYSQYNQVLAS 1023
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1988774931 1682 SKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQ 1725
Cdd:COG3096 1024 LKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELHEE 1067
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1464-1946 |
4.91e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1464 LEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGK 1543
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1544 N-------VHELERARRTLE----TEAQNLR----------IQTQELEEELSEAENSRLRLEVTLQALKA---------- 1592
Cdd:pfam05483 343 AkaahsfvVTEFEATTCSLEellrTEQQRLEknedqlkiitMELQKKSSELEEMTKFKNNKEVELEELKKilaedeklld 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1593 ---QFER---EISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLR 1666
Cdd:pfam05483 423 ekkQFEKiaeELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENK 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1667 RLQGQMKEVLRELddsKVTRDDVISQSKDSE---KKIQTLEAEVLHLTEELavsERQKRQAQQERDEIADEMVSSSSGKN 1743
Cdd:pfam05483 503 ELTQEASDMTLEL---KKHQEDIINCKKQEErmlKQIENLEEKEMNLRDEL---ESVREEFIQKGDEVKCKLDKSEENAR 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1744 VLSEEkrrldarvnqleeeleeeqtnnellterLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARlGEME 1823
Cdd:pfam05483 577 SIEYE----------------------------VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK-GSAE 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1824 GAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDK-------SMVR 1896
Cdd:pfam05483 628 NKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKrcqhkiaEMVA 707
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1988774931 1897 L-KQLKRQLEE-VEEENSRSSAQKRKLQreleELTDSSQTMNREISSLRNQL 1946
Cdd:pfam05483 708 LmEKHKHQYDKiIEERDSELGLYKNKEQ----EQSSAKAALEIELSNIKAEL 755
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
994-1267 |
5.06e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 994 LETKVKSLETD-------LATAVEQR-------ERLGKEKKQLE-ERLNEVTD---QLTEEEEKTKSLNKLKNKQEAVIA 1055
Cdd:pfam10174 420 LKERVKSLQTDssntdtaLTTLEEALsekeriiERLKEQREREDrERLEELESlkkENKDLKEKVSALQPELTEKESSLI 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1056 DLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLG--MLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLRE 1133
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLEnqLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQA 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1134 ALSQVSELKEEVENERGMRERaeKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRH-ETQL 1212
Cdd:pfam10174 580 EVERLLGILREVENEKNDKDK--KIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSqQLQL 657
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774931 1213 SELrvkhsaaldslqeqLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSE 1267
Cdd:pfam10174 658 EEL--------------MGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAE 698
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1483-1684 |
5.09e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.40 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1483 ARLAEERDRAEADSrEKETRcLALSRALQEAQDQKEELERANKQLRLEMEQlvnqqddvgknvHELERARRTLETEAQNL 1562
Cdd:COG2268 195 AEIIRDARIAEAEA-ERETE-IAIAQANREAEEAELEQEREIETARIAEAE------------AELAKKKAEERREAETA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1563 RIQTQELEEELSEaensRLRLEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRE------LEIQLEEERSQRSQSVSS 1636
Cdd:COG2268 261 RAEAEAAYEIAEA----NAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKpaeaekQAAEAEAEAEAEAIRAKG 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1988774931 1637 KKQLEAELQEAEAQVETANRGKEEAM-KQLRRLQGQMKEVLRELDDSKV 1684
Cdd:COG2268 337 LAEAEGKRALAEAWNKLGDAAILLMLiEKLPEIAEAAAKPLEKIDKITI 385
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1012-1343 |
5.47e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1012 RERLGKEKKQLEERLNEVTDQ-LTEEEEKTKSLN----------KLKNK-QEAV---IADLEERLKREEQGrLEQEKFKR 1076
Cdd:PRK04778 24 RKRNYKRIDELEERKQELENLpVNDELEKVKKLNltgqseekfeEWRQKwDEIVtnsLPDIEEQLFEAEEL-NDKFRFRK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1077 -------------RMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKE 1143
Cdd:PRK04778 103 akheineieslldLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1144 EVE--NERGMRERAEKQRRDLSEELEALRTELED------TLDSTAAQQ--ELRS-RREAE-----------LSELQRcV 1201
Cdd:PRK04778 183 QFVelTESGDYVEAREILDQLEEELAALEQIMEEipellkELQTELPDQlqELKAgYRELVeegyhldhldiEKEIQD-L 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1202 EEETRRHETQLSELRVKH--------SAALDSLQEQLDNSKRARQSLEKAKATL-------EEERQNLTSELKSLQASR- 1265
Cdd:PRK04778 262 KEQIDENLALLEELDLDEaeekneeiQERIDQLYDILEREVKARKYVEKNSDTLpdflehaKEQNKELKEEIDRVKQSYt 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1266 -SESERGRKRA-DNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQ 1343
Cdd:PRK04778 342 lNESELESVRQlEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLE 421
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
988-1148 |
6.90e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 988 LLEKVTLETKVKSLETDLATAVEQRERLGKEKKQleERLNEVTDQLTEEEEKTKSLNKLKNKQeavIADLEERLKREEQg 1067
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKK--EALLEAKEEIHKLRNEFEKELRERRNE---LQKLEKRLLQKEE- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1068 RLEQ-----EKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGrLEEEGAR-------RAEAQrslREAL 1135
Cdd:PRK12704 97 NLDRklellEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG-LTAEEAKeillekvEEEAR---HEAA 172
|
170
....*....|...
gi 1988774931 1136 SQVSELKEEVENE 1148
Cdd:PRK12704 173 VLIKEIEEEAKEE 185
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1022-1143 |
7.14e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1022 LEERLNEVTDQLTEEEEKTKSLNKLKnkQEAVIADLEERLKREEqGRLEQ-EKFKRRMESEAMEAQEQLSDLGMLSSELR 1100
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEH--EERELTEEEEEIRRLE-EQVERlEAEVEELEAELEEKDERIERLERELSEAR 454
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1988774931 1101 GSL---AQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKE 1143
Cdd:COG2433 455 SEErreIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1002-1289 |
7.27e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1002 ETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLkNKQEAVIAD--LEERLK--REEQGRLEQ-EKFKR 1076
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL-LPQANLLADetLADRLEelREELDAAQEaQAFIQ 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1077 RMeseameaQEQLSDLGMLSSELRGSLAQKEkeitSLQGRLEEEGARRAEAQRSLrEALSQV----------------SE 1140
Cdd:COG3096 914 QH-------GKALAQLEPLVAVLQSDPEQFE----QLQADYLQAKEQQRRLKQQI-FALSEVvqrrphfsyedavgllGE 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1141 LKEEVENERGMRERAEKQRRDLSEELEALRTELEDtldSTAAQQELRSRREAELSELQRCVEEetrrhetqLSELRVKHS 1220
Cdd:COG3096 982 NSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQ---YNQVLASLKSSRDAKQQTLQELEQE--------LEELGVQAD 1050
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774931 1221 AAldslqeqldnskrarqslekAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQA 1289
Cdd:COG3096 1051 AE--------------------AEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKA 1099
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
987-1176 |
7.57e-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: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 987 LLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEErlnevtdqlteeeeKTKSLNKLKNKQEAVIADLEERLKREEQ 1066
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQA--------------LESELAISRQDYDGATAQLRAAQAAVKA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1067 GRLEQEKfkrrmESEAMEAQEQLSDLGMLSSElrgslaqkekeitslqgRLEEEGARRAEAQRSLREALSQVSELKEEVE 1146
Cdd:pfam00529 115 AQAQLAQ-----AQIDLARRRVLAPIGGISRE-----------------SLVTAGALVAQAQANLLATVAQLDQIYVQIT 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1988774931 1147 NE--------RGMRERAEKQRRDLSEELEALRTELEDT 1176
Cdd:pfam00529 173 QSaaenqaevRSELSGAQLQIAEAEAELKLAKLDLERT 210
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
991-1185 |
7.81e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.05 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 991 KVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLnkLKNKQEAVIADLEERLKReeqgrle 1070
Cdd:pfam04012 24 EKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAA--LTKGNEELAREALAEKKS------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774931 1071 QEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQR----SLREALSQVSELKEEVE 1146
Cdd:pfam04012 95 LEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTSlgslSTSSATDSFERIEEKIE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1988774931 1147 nERGMRERAEKQRR---DLSEELEALRTELEDTLDSTAAQQE 1185
Cdd:pfam04012 175 -EREARADAAAELAsavDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| |
