|
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: 1457.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGrkkeAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTMDSMA 348
Cdd:cd14920 157 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 349 IMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTK 428
Cdd:cd14920 237 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 429 EQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 508
Cdd:cd14920 317 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 509 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEAD 588
Cdd:cd14920 397 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 589 FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSSGessaPVTFGAAGLKTKKGMF 668
Cdd:cd14920 477 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGM----TETAFGSAYKTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 669 RTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEI 748
Cdd:cd14920 553 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2414917124 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: 1307.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKeavQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKK---KGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLL-GTADQYRFLSGGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLtGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 348 AIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQT 427
Cdd:cd01377 238 DILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 428 KEQADFAVEALAKATYERLFRWLVHRINRALDRrQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFI 507
Cdd:cd01377 318 KEQVVFSVGALAKALYERLFLWLVKRINKTLDT-KSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 508 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFF-KSKQPRGE 586
Cdd:cd01377 397 LEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFkKPKPKKSE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 587 ADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGldqvssgessapvtfGAAGLKTKKG 666
Cdd:cd01377 475 AHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGG---------------GGGKKKKKGG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 667 MFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 746
Cdd:cd01377 540 SFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRY 619
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2414917124 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 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTMDSMA 348
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 349 IMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTK 428
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 429 EQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 508
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 509 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEAD 588
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 589 FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSSGESSAPVTFgaaglKTKKGMF 668
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHGAF-----KTRKGMF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 669 RTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEI 748
Cdd:cd14932 556 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2414917124 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: 1156.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQ-----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 263
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVNpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 264 FDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQT 343
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 344 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQ 423
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 424 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 503
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 504 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQp 583
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDF- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 584 RGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDrIVGLDQVSSGESsapvTFGAaglKT 663
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQALTDT----QFGA---RT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 664 KKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 743
Cdd:cd14911 549 RKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2414917124 744 QRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14911 629 QRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| 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: 1126.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 866 TRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGEL 945
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 946 ETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEER 1025
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1026 LNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSDLRGSLAQ 1105
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1106 KEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQE 1185
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1186 LRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASR 1265
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1266 SESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDE 1345
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1346 SRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQR 1425
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1426 ERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLA 1505
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1506 LSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERTRRTLETEAQNLRIQTQELEEELSEAENSRLRLEV 1585
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1586 TLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQL 1665
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1666 RRLQGQMKEVLRELDEAKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVL 1745
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1746 SEEKRRLDARVNQLEEDLEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGA 1825
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1826 VRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLE 1905
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 2414917124 1906 EVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQL 1946
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| 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: 1125.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVASSHKGgtlgRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKG----KKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTMDSMA 348
Cdd:cd14921 157 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 349 IMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTK 428
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 429 EQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 508
Cdd:cd14921 317 EQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 509 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEAD 588
Cdd:cd14921 397 EQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 589 FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSS-GESSAPvtfgaAGLKTKKGM 667
Cdd:cd14921 477 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKmTESSLP-----SASKTKKGM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 668 FRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 747
Cdd:cd14921 552 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2414917124 748 ILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14921 632 ILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| 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: 1125.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVASSHKGgtlgrKKEavQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKS-----KKD--QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTMDSMA 348
Cdd:cd14919 154 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 349 IMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTK 428
Cdd:cd14919 234 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 429 EQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 508
Cdd:cd14919 314 EQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 509 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEAD 588
Cdd:cd14919 394 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKAD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 589 FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSS-GESSAPVTFgaaglKTKKGM 667
Cdd:cd14919 474 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGmSETALPGAF-----KTRKGM 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 668 FRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 747
Cdd:cd14919 549 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 628
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2414917124 748 ILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14919 629 ILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| 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: 1115.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTMDSMA 348
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 349 IMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTK 428
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 429 EQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 508
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 509 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEAD 588
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 589 FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVsSGESSAPVTFgaaglKTKKGMF 668
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKV-SGMSEMPGAF-----KTRKGMF 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 669 RTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEI 748
Cdd:cd15896 555 RTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 634
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2414917124 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: 1103.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 97 VEDMADLTCLNEASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSML 176
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 177 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRkkeavqgeLERQLLQANPILEAFGNAKTVKNDNSSRF 256
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVGR--------LEEQILQSNPILEAFGNAKTVRNNNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 257 GKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQS 335
Cdd:pfam00063 153 GKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSqSGCYTIDGID 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 336 DSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRI 415
Cdd:pfam00063 233 DSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 416 KVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNE 495
Cdd:pfam00063 313 KTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 496 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHP 575
Cdd:pfam00063 393 KLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 576 KFFKSKQpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSSGESSAPvt 655
Cdd:pfam00063 470 HFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTPK-- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 656 fgaaglKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPN 735
Cdd:pfam00063 547 ------RTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPN 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 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 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVASSHKGgtlgRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKG----RKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQsDSENFTQTMDSMA 348
Cdd:cd14930 157 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ-ERELFQETLESLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 349 IMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTK 428
Cdd:cd14930 236 VLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 429 EQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 508
Cdd:cd14930 316 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 509 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEAD 588
Cdd:cd14930 396 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQAD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 589 FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSSGESSAPvtfgaaGLKTKKGMF 668
Cdd:cd14930 476 FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPP------GGRPRRGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 669 RTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEI 748
Cdd:cd14930 550 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2414917124 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: 1018.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 90 NPPRFSKVEDMADLTCLNEASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISE 169
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 170 AAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGtlgrkkeavqGELERQLLQANPILEAFGNAKTVK 249
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV----------GSVEDQILESNPILEAFGNAKTLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 250 NDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGS 328
Cdd:smart00242 151 NNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNqGGC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 329 IPVPGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFT 407
Cdd:smart00242 231 LTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 408 RAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQgASFIGILDIAGFEIFQLNSFEQ 487
Cdd:smart00242 311 KALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 488 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATDRSFVEKL 567
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 568 SGEQGSHPKFFKSKQpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdrivgldqvss 647
Cdd:smart00242 467 NQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG----------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 648 gessapvtfgaAGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIR 727
Cdd:smart00242 535 -----------VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIR 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 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: 900.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 46 VWVPSEKQGFESASIREERGDEVEVELTDSQRRVTLSREEVQ-----RMNPPRFSKVEDMADLTCLNEASVLHNLRERYY 120
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEGKKEDGESVSVKKKvlgndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 121 SGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGESGAGKTENTKK 200
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 201 VIQYLAHVASSHkggtlgrkkEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLL 280
Cdd:COG5022 172 IMQYLASVTSSS---------TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 281 EKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSMAIMGFTPEELMS 359
Cdd:COG5022 243 EKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSqGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 360 MLKVISAVLQFGNISFMKEKNhDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALA 439
Cdd:COG5022 323 IFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 440 KATYERLFRWLVHRINRALDRRQRQGaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE 519
Cdd:COG5022 402 KALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 520 WNFIDFgLDLQPCIDLIERpANPPGVLALLDEECWFPRATDRSFVEKLSG--EQGSHPKFFKSKQprGEADFSIIHYAGK 597
Cdd:COG5022 481 WSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRF--RDNKFVVKHYAGD 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 598 VDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVgldqvssgessapvtfgaaglktKKGMFRTVGQLYKE 677
Cdd:COG5022 557 VEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-----------------------SKGRFPTLGSRFKE 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 678 SLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPNAIPRT 757
Cdd:COG5022 614 SLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTG 693
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 758 ----FMDGKQASELMISALELDKNLFRVGQSKVFFRAGVLAHLEEERDLKITDTIIRFQSAARGFLSRKAFLKKQQQLSA 833
Cdd:COG5022 694 eytwKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKK 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 834 LRVMQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQDEEIQTREAALQKAKEQLTR---AEQDYTELDKKHAQLLEEKAVL 910
Cdd:COG5022 774 IQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKRekkLRETEEVEFSLKAEVLIQKFGR 853
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 911 ADQLQAEAELFAEAEEMRarlasrkqeleevlgeletrleeeeergVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLE 990
Cdd:COG5022 854 SLKAKKRFSLLKKETIYL----------------------------QSAQRVELAERQLQELKIDVKSISSLKLVNLELE 905
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 991 KVTLEtKVKSLETDLATAVE-QRERLGKEKKQLEERlnEVTDQLTEEEEKTKSLNKL---KNKQEAVIADLEERLKREEQ 1066
Cdd:COG5022 906 SEIIE-LKKSLSSDLIENLEfKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLhevESKLKETSEEYEDLLKKSTI 982
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1067 GRLEQEKFKRRMESEAMEAQEQLSDLGMLSSDLRgSLAQKEKEITSLQgrleeegarrtEAQRSLREALSQVSELKEEVE 1146
Cdd:COG5022 983 LVREGNKANSELKNFKKELAELSKQYGALQESTK-QLKELPVEVAELQ-----------SASKIISSESTELSILKPLQK 1050
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1147 NERGMreraEKQRRDLSEELEALRTELEDTLDSTaAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAAldsl 1226
Cdd:COG5022 1051 LKGLL----LLENNQLQARYKALKLRRENSLLDD-KQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQ---- 1121
|
1210 1220 1230
....*....|....*....|....*....|....*
gi 2414917124 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 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRH-EMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 188 GESGAGKTENTKKVIQYLAHVASSHKGgtlgrKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 267
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSS-----KSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 268 GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFL-----SGGSIPVPGQSDSENFTQ 342
Cdd:cd00124 156 GRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 343 TMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKN--HDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGRE 420
Cdd:cd00124 236 LLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEdeDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 421 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALD-RRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 499
Cdd:cd00124 316 TITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSpTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 500 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFK 579
Cdd:cd00124 396 FFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 580 SKQPRGEAdFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDhfvselwkevdrivgldqvssgessapvtfgaa 659
Cdd:cd00124 473 KKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ--------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 660 glktkkgmfrtvgqlYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPF 739
Cdd:cd00124 519 ---------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPF 583
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2414917124 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: 791.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVASshKGGTLGRKKEAVQ----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 264
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAA--LGDGPGKKAQFLAtktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 265 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRaDLLLGTAD--QYRFLSGGSIPVPGQSDSENFTQ 342
Cdd:cd14927 159 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEELMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 343 TMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 422
Cdd:cd14927 238 TDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 423 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRR-QRQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 501
Cdd:cd14927 318 TKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKlPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 502 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFK- 579
Cdd:cd14927 396 NHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKp 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 580 --SKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivglDQVSSGESSAPVTFG 657
Cdd:cd14927 473 rpDKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---------ENYVGSDSTEDPKSG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 658 AAGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRI 737
Cdd:cd14927 544 VKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRI 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 2414917124 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: 772.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 190 SGAGKTENTKKVIQYLAHVASShkgGTLGRKKEA-VQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAAT---GDLAKKKDSkMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETrADLLLGTADQYR--FLSGGSIPVPGQSDSENFTQTMDS 346
Cdd:cd14913 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEILVASIDDAEELLATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 347 MAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKA 425
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKF-KQKQREEQAEPDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 426 QTKEQADFAVEALAKATYERLFRWLVHRINRALDRR-QRQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 504
Cdd:cd14913 317 QTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKlPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 505 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKSKQP 583
Cdd:cd14913 395 MFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKVV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 584 RG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivgldqVSSGESSAPVTFGaAGL 661
Cdd:cd14913 472 KGraEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY-----------ATFATADADSGKK-KVA 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 662 KTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 741
Cdd:cd14913 540 KKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGD 619
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2414917124 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: 757.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKeavqGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSK----GSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGT-ADQYRFLSGGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd14909 157 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDnIYDYYIVSQGKVTVPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 348 AIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQT 427
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 428 KEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFI 507
Cdd:cd14909 317 VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKR-QHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 508 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKSKQPRG- 585
Cdd:cd14909 396 LEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKPg 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 586 --EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEvdrivgldqvSSGESSAPVtfGAAGLKT 663
Cdd:cd14909 473 qqAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD----------HAGQSGGGE--QAKGGRG 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 664 KKGM-FRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEF 742
Cdd:cd14909 541 KKGGgFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDF 620
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2414917124 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: 748.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGrkkeavQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDG------KGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLL-GTADQYRFLSGGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd14934 155 KLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQGVTVVDNMDDGEELQITDVAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 348 AIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQT 427
Cdd:cd14934 235 DVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 428 KEQADFAVEALAKATYERLFRWLVHRINRALDRR-QRQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 506
Cdd:cd14934 315 MEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKmQRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 507 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKSKQPRG 585
Cdd:cd14934 393 VLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 586 ---EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSdHFVSELWKEvdrivgldqvssgESSAPvtfgAAGLK 662
Cdd:cd14934 470 kgpEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS-LGLLALLFK-------------EEEAP----AGSKK 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 663 TKKGM-FRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 741
Cdd:cd14934 532 QKRGSsFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPE 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2414917124 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: 727.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSG-LIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVASSHKGGTlgrkkeavqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET----------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd01380 152 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNqGGSPVIDGVDDAAEFEETRKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 348 AIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQT 427
Cdd:cd01380 232 TLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 428 KEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 506
Cdd:cd01380 312 LQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 507 ILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPRATDRSFVEKLSGE-QGSHPKFFKSkqPR- 584
Cdd:cd01380 392 KLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQhLKKPNKHFKK--PRf 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 585 GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHfvselwkevdrivgldqvssgessapvtfgaaglktK 664
Cdd:cd01380 466 SNTAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR------------------------------------K 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 665 KgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 744
Cdd:cd01380 510 K----TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFS 585
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2414917124 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 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVASShkggTLGRKKeavQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAM----IESKKK---LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEetRADLLLGTAD--QYRFLSGGSIPVPGQSDSENFTQTMDS 346
Cdd:cd14929 154 MLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEELLATEQA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 347 MAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQ 426
Cdd:cd14929 232 MDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 427 TKEQADFAVEALAKATYERLFRWLVHRINRALDRR-QRQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 505
Cdd:cd14929 312 NIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKlSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHM 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 506 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKSKQPR 584
Cdd:cd14929 390 FVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 585 G--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKevdrivglDQVSSGESSapvTFGAAglK 662
Cdd:cd14929 467 KkfEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFE--------NYISTDSAI---QFGEK--K 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 663 TKKGM-FRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 741
Cdd:cd14929 534 RKKGAsFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYAD 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2414917124 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: 703.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 190 SGAGKTENTKKVIQYLAHVASShkGGTLGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 269
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAI--GDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 270 IVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETrADLLLGTAD--QYRFLSGGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 348 AIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASmPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQ 426
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 427 TKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 505
Cdd:cd14917 318 NVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQpRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 506 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKL-SGEQGSHPKFFKSKQPR 584
Cdd:cd14917 396 FVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLfDNHLGKSNNFQKPRNIK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 585 G--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivgldqVSSGESSAPVTFGAAglK 662
Cdd:cd14917 473 GkpEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLF-----------ANYAGADAPIEKGKG--K 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 663 TKKG-MFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 741
Cdd:cd14917 540 AKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGD 619
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2414917124 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: 696.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 111 VLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGES 190
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 191 GAGKTENTKKVIQYLAHVASShkggtlGRKKE----AVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 266
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVT------GEKKKeesgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 267 AGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTAD-QYRFLSGGSIPVPGQSDSENFTQTMD 345
Cdd:cd14918 157 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMATDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 346 SMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQK 424
Cdd:cd14918 237 AIDILGFTPEEKVSIYKLTGAVMHYGNMKF-KQKQREEQAEPDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 425 AQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 503
Cdd:cd14918 316 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 504 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKSKQ 582
Cdd:cd14918 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 583 PRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKevdrivgldQVSSGESSAPVTFGAag 660
Cdd:cd14918 471 VKGkaEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFS---------TYASAEADSGAKKGA-- 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 661 lKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 740
Cdd:cd14918 540 -KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYG 618
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2414917124 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: 691.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 190 SGAGKTENTKKVIQYLAHVASshkggTLGRKKEAV-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 264
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAV-----TGEKKKEEAtsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 265 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTAD-QYRFLSGGSIPVPGQSDSENFTQT 343
Cdd:cd14910 157 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 344 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 422
Cdd:cd14910 237 DSAIEILGFTSDERVSIYKLTGAVMHYGNMKF-KQKQREEQAEPDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 423 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 501
Cdd:cd14910 316 TKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 502 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKS 580
Cdd:cd14910 394 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 581 KQPRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivgldqvsSGESSAPVTFGA 658
Cdd:cd14910 471 KPAKGkvEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF-------------SGAAAAEAEEGG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 659 A--GLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNR 736
Cdd:cd14910 538 GkkGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 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: 691.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 190 SGAGKTENTKKVIQYLAHVASSHKggtlgRKKEA----VQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 265
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGD-----KKKEQqpgkMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 266 VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETrADLLLGTADQYR--FLSGGSIPVPGQSDSENFTQT 343
Cdd:cd14923 157 ATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELLAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 344 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 422
Cdd:cd14923 236 DNAIDILGFSSEEKVGIYKLTGAVMHYGNMKF-KQKQREEQAEPDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 423 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 501
Cdd:cd14923 315 TKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 502 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSK 581
Cdd:cd14923 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 582 QP---RGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdriVGLDQVSSGESSapvtfga 658
Cdd:cd14923 470 KPakgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSK------- 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 659 AGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIP 738
Cdd:cd14923 540 KGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRIL 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2414917124 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: 686.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 190 SGAGKTENTKKVIQYLAHVASShkgGTLGRKKEA--VQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 267
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAI---GDRSKKENPnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 268 GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETrADLLLGTAD--QYRFLSGGSIPVPGQSDSENFTQTMD 345
Cdd:cd14916 159 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPEL-LDMLLVTNNpyDYAFVSQGEVSVASIDDSEELLATDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 346 SMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNTA-AQKLCHLLGVNVLEFTRAILTPRIKVGREYVQK 424
Cdd:cd14916 238 AFDVLGFTAEEKAGVYKLTGAIMHYGNMKF-KQKQREEQAEPDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 425 AQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 503
Cdd:cd14916 317 GQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQpRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 504 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKL-SGEQGSHPKFFKSKQ 582
Cdd:cd14916 395 HMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLyDNHLGKSNNFQKPRN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 583 PRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdriVGLDQVSSGESSapvtfgaaG 660
Cdd:cd14916 472 VKGkqEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY---ASADTGDSGKGK--------G 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 661 LKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 740
Cdd:cd14916 541 GKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2414917124 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: 685.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 190 SGAGKTENTKKVIQYLAHVASSHKggtlgRKKE-----AVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 264
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGE-----KKKEeitsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 265 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTAD-QYRFLSGGSIPVPGQSDSENFTQT 343
Cdd:cd14912 157 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPyDYPFVSQGEISVASIDDQEELMAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 344 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 422
Cdd:cd14912 237 DSAIDILGFTNEEKVSIYKLTGAVMHYGNLKF-KQKQREEQAEPDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 423 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 501
Cdd:cd14912 316 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 502 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKS 580
Cdd:cd14912 394 NHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 581 KQPRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdrivgldQVSSGESSApvtfGA 658
Cdd:cd14912 471 KVVKGkaEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGA-------QTAEGASAG----GG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 659 A--GLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNR 736
Cdd:cd14912 540 AkkGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSR 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 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: 678.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 190 SGAGKTENTKKVIQYLAHVASSHKggtlGRKKEA----VQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 265
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGE----KKKEEAasgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 266 VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETrADLLLGTADQYRF--LSGGSIPVPGQSDSENFTQT 343
Cdd:cd14915 158 ATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 344 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 422
Cdd:cd14915 237 DSAVDILGFSADEKVAIYKLTGAVMHYGNMKF-KQKQREEQAEPDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 423 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 501
Cdd:cd14915 316 TKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 502 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKS 580
Cdd:cd14915 394 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 581 KQPRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSdhfvselWKEVDRIVGLDQVSSGESSApvtfGA 658
Cdd:cd14915 471 KPAKGkaEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSG-------MKTLAFLFSGGQTAEAEGGG----GK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 659 AGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIP 738
Cdd:cd14915 540 KGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2414917124 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: 673.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 190 SGAGKTENTKKVIQYLAHVASSHKggtlgrkkeavqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 269
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 270 IVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGA--SEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDS 346
Cdd:cd14883 149 IKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAkhSKELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 347 MAIMGFTPEELMSMLKVISAVLQFGNISFMK-EKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKA 425
Cdd:cd14883 229 MNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 426 QTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 505
Cdd:cd14883 309 LKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 506 FILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRG 585
Cdd:cd14883 388 FKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRW 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 586 EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVD--RIVGLDQVSSGESSApvtfgaagLKT 663
Cdd:cd14883 465 KTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDllALTGLSISLGGDTTS--------RGT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 664 KKGMfRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 743
Cdd:cd14883 537 SKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFV 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2414917124 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: 663.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 190 SGAGKTENTKKVIQYLAHVASSHkggtlgrkkeavQGELER---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 266
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGS------------ESEVERvkdMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 267 AGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMD 345
Cdd:cd01378 150 KGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSkSGCFDVDGIDDAADFKEVLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 346 SMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREY---V 422
Cdd:cd01378 230 AMKVIGFTEEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 423 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFn 502
Cdd:cd01378 309 EVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 503 hTMFIL--EQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-RATDRSFVEKLSGEQGSHPKFFK 579
Cdd:cd01378 388 -IELTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFEC 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 580 SKQPR--GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDrivgldqvssgessapvtfg 657
Cdd:cd01378 464 PSGHFelRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGV-------------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 658 aagLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRI 737
Cdd:cd01378 524 ---DLDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQ 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2414917124 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 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRgkKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 190 SGAGKTENTKKVIQYLAHVAsshkGGTLGrkkeavqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 269
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALG----GGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 270 IVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSG-GSIPVPGQSDSENFTQTMDSMA 348
Cdd:cd01383 147 ICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQsNCLTIDGVDDAKKFHELKEALD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 349 IMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTK 428
Cdd:cd01383 227 TVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 429 EQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 508
Cdd:cd01383 307 QQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 509 EQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRgead 588
Cdd:cd01383 387 EQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGERGGA---- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 589 FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLhQSSDHFVSELWKEVDRIVGLDQVSSgessapvtfgaAGLKTKKGMF 668
Cdd:cd01383 460 FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQLFASKMLDASRKALPL-----------TKASGSDSQK 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 669 RTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEI 748
Cdd:cd01383 528 QSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGF 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2414917124 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 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 188 GESGAGKTENTKKVIQYLAHVASshKGGTLGRKkeavqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 267
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGG--RAVTEGRS-------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 268 GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDS 346
Cdd:cd01384 152 GRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNqSKCFELDGVDDAEEYRATRRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 347 MAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKL---CHLLGVNVLEFTRAILTPRIKVGREYVQ 423
Cdd:cd01384 232 MDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDALCKRVIVTPDGIIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 424 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 503
Cdd:cd01384 312 KPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 504 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQP 583
Cdd:cd01384 391 HVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPKLS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 584 RgeADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRivgldqvsSGESSApvtfgaaglkT 663
Cdd:cd01384 468 R--TDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR--------EGTSSS----------S 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 664 KkgmFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 743
Cdd:cd01384 528 K---FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2414917124 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 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVASSHKggtlgrkkeavqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS-------------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd01381 148 VIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTqGNCLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 348 AIMGFTPEELMSMLKVISAVLQFGNISFMK--EKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKA 425
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 426 QTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAS--FIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 503
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 504 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQ 582
Cdd:cd01381 388 HIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 583 pRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFvselwkeVDRIVGLDQVSSGESSApvtfgaaglK 662
Cdd:cd01381 464 -DLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKF-------LKQLFNEDISMGSETRK---------K 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 663 TKkgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEF 742
Cdd:cd01381 527 SP-----TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEF 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2414917124 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 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVASSHKGgtlgrkkeavqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLllGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd14872 148 RICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGW--GSSAAYGYLSlSGCIEVEGVDDVADFEEVVLAM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 348 AIMGFTPEELMSMLKVISAVLQFGNISF---MKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKV-GREYVQ 423
Cdd:cd14872 226 EQLGFDDADINNVMSLIAAILKLGNIEFasgGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 424 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 503
Cdd:cd14872 306 IPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 504 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQP 583
Cdd:cd14872 386 YTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 584 RGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivgldqvssgessaPVTFGAAglKT 663
Cdd:cd14872 463 TSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF-------------------PPSEGDQ--KT 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 664 KKGmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 743
Cdd:cd14872 522 SKV---TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFL 598
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2414917124 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 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 188 GESGAGKTENTKKVIQYLAHVasshkGGTLGrkkeavqGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 267
Cdd:cd01382 81 GESGAGKTESTKYILRYLTES-----WGSGA-------GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 268 GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGtadqyrflsggsipvPGQSDSENFTQTMDSM 347
Cdd:cd01382 149 SSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKD---------------PLLDDVGDFIRMDKAM 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 348 AIMGFTPEELMSMLKVISAVLQFGNISFmkEKNHDQA---SMPDNTAAQKL---CHLLGVNVLEF-----TRAILTPRIK 416
Cdd:cd01382 214 KKIGLSDEEKLDIFRVVAAVLHLGNIEF--EENGSDSgggCNVKPKSEQSLeyaAELLGLDQDELrvsltTRVMQTTRGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 417 VGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRrqRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 496
Cdd:cd01382 292 AKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPF--ETSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 497 LQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPRATDRSFVEKLSGEQGSH-- 574
Cdd:cd01382 370 LQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHfr 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 575 ---PKFFKSKQPRGEAD---FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKevdrivglDQVSSG 648
Cdd:cd01382 447 lsiPRKSKLKIHRNLRDdegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFE--------SSTNNN 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 649 ESSAPvtfgaaglKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRI 728
Cdd:cd01382 519 KDSKQ--------KAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDL 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2414917124 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 |
1.59e-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: 1.59e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQ----DREDQS 183
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 184 ILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQ------GELERQLLQANPILEAFGNAKTVKNDNSSRFG 257
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 258 KFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDS 337
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 338 ENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFmkEKNHDQASMPDNTAAQKLCH---LLGVNVLEFTRAILTPR 414
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDF--ESENDTTVLEDATTLQSLKLaaeLLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 415 IKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQgASFIGILDIAGFEIFQLNSFEQLCINYTN 494
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 495 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPRAT--DRSFVEKL---- 567
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLhasf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 568 ---------SGEQGSHPKFFkskQPRGEAD--FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDhfvselwkev 636
Cdd:cd14890 476 grksgsggtRRGSSQHPHFV---HPKFDADkqFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRR---------- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 637 drivGLDQVSsgessapvtfgaaglktkkgmfrtVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQ 716
Cdd:cd14890 543 ----SIREVS------------------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQ 594
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2414917124 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 |
1.51e-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: 1.51e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVAsshkggtlgRKKEAVQGElerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvAG 268
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN---------QRRNNLVTE---QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd01387 148 VIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNqGGNCEIAGKSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 348 AIMGFTPEELMSMLKVISAVLQFGNISFMK---EKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQK 424
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNVYFHKrqlRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 425 AQTKEQADFAVEALAKATYERLFRWLVHRINrALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 504
Cdd:cd01387 308 PLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKH 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 505 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKskqPR 584
Cdd:cd01387 387 VFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSK---PR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 585 -GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKevdrivgldQVSSGESSAPVTFGAAGLKT 663
Cdd:cd01387 461 mPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFS---------SHRAQTDKAPPRLGKGRFVT 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 664 KKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 743
Cdd:cd01387 532 MKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFI 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2414917124 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 |
2.51e-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: 2.51e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLahVASSHKGGTLGrkkeavqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKGYGSG---------VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd01385 150 MVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFERLKQAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 348 AIMGFTPEELMSMLKVISAVLQFGNISFMKEK-NHDQASMPDNTAAQKL-CHLLGVNVLEFTRAILTPRIKVGREYVQKA 425
Cdd:cd01385 230 EMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVGETLILP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 426 QTKEQADFAVEALAKATYERLFRWLVHRINRAL----DRRQRQGASfIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 501
Cdd:cd01385 310 YKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 502 NHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPkfFKSK 581
Cdd:cd01385 389 NQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNK--YYEK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 582 QPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELwkevdriVGLDQV---------------- 645
Cdd:cd01385 464 PQVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVavfrwavlrafframa 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 646 ---------------SSGESSAPVTFGAAGL-KTKKGMfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLS 709
Cdd:cd01385 537 afreagrrraqrtagHSLTLHDRTTKSLLHLhKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFD 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 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 |
1.52e-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: 1.52e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEM---PPHIYAISEAAYRSMLQDR----ED 181
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 182 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 261
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 262 INFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGS-IPVPGQSDSENF 340
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 341 TQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFmkEKNHDQ----ASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIK 416
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 417 VGR-EYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQ---------GASFIGILDIAGFEIFQLNSFE 486
Cdd:cd14892 319 TARgSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 487 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPR-ATDRSFVE 565
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKRkTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 566 KLSGEQGSHPKFFksKQPRGEAD-FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDhfvselwkevdrivgldq 644
Cdd:cd14892 476 IYHQTHLDKHPHY--AKPRFECDeFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 645 vssgessapvtfgaaglktkkgmFRTvgqlykeSLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLE 724
Cdd:cd14892 536 -----------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLE 585
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2414917124 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 |
2.49e-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: 2.49e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMY------RGKKRHEMPPHIYAISEAAYRSMLQDRE-- 180
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 181 --DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQgeleRQLLQANPILEAFGNAKTVKNDNSSRFGK 258
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVR----DRVLESNPILEAFGNARTNRNNNSSRFGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 259 FIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFL--SGGSIPVPGQSD 336
Cdd:cd14901 157 FIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 337 SENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFM-KEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRI 415
Cdd:cd14901 237 SVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVkKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 416 KVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAS-FIGILDIAGFEIFQLNSFEQLCINYTN 494
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 495 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSH 574
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 575 PKFFKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSElwkevdrivgldqvssgessapv 654
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 655 tfgaaglktkkgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFP 734
Cdd:cd14901 531 ---------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYP 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 2414917124 735 NRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNL-----FRVGQSKVF 787
Cdd:cd14901 596 VRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIehlppFQVGKTKVF 653
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
110-789 |
1.14e-170 |
|
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: 1.14e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 190 SGAGKTENTKKVIQYLAHvasshkggtLGRkkeAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 269
Cdd:cd01379 82 SGAGKTESANLLVQQLTV---------LGK---ANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 270 IVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETR-ADLLLGTADQYRFLSGGSIPVPG----QSDSENFTQTM 344
Cdd:cd01379 150 VTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDivnnSGNREKFEEIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 345 DSMAIMGFTPEELMSMLKVISAVLQFGNISF----MKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAiLTPRIKVGR- 419
Cdd:cd01379 230 QCFKVIGFTKEEVDSVYSILAAILHIGDIEFteveSNHQTDKSSRISNPEALNNVAKLLGIEADELQEA-LTSHSVVTRg 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 420 EYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL--DRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKL 497
Cdd:cd01379 309 ETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 498 QQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPRATDRSFVEKLsgEQGSHPK 576
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKF--HNNIKSK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 577 FFkSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSElwkevdrivgldqvssgessapvtf 656
Cdd:cd01379 463 YY-WRPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 657 gaaglktkkgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNR 736
Cdd:cd01379 517 -------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHR 583
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 2414917124 737 IPFQEFRQRYEILTPNAIPRTFMDgKQASELMISALELDKnlFRVGQSKVFFR 789
Cdd:cd01379 584 ILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
109-789 |
1.19e-170 |
|
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: 1.19e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 188 GESGAGKTENTKKVIQYLAHVASSHKGGTLgrkkeavqgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 267
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLNDSTI------------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 268 GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRadLLLGTADQYRFL-SGGSIPVPGQSDSENFTQTMDS 346
Cdd:cd14903 149 GTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEER--LFLDSANECAYTgANKTIKIEGMSDRKHFARTKEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 347 MAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASM--PDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQK 424
Cdd:cd14903 227 LSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 425 AQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 504
Cdd:cd14903 307 PLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 505 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPRATDRSFVEKLSG---EQGSHPKFfksk 581
Cdd:cd14903 386 VFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLSSihkDEQDVIEF---- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 582 qPR-GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSSGESSAPVTFGAAG 660
Cdd:cd14903 458 -PRtSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 661 LKtkkgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 740
Cdd:cd14903 537 TT-------TVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHE 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2414917124 741 EFRQRYEILTPNAiPRTFMDGKQASELMISALELDK-NLFRVGQSKVFFR 789
Cdd:cd14903 610 EFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
109-789 |
2.74e-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: 2.74e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKK-RHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 188 GESGAGKTENTKKVIQYLAHVASShkggtlgrkkeaVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 267
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS------------DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTEN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 268 GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSEN-------F 340
Cdd:cd14897 149 GQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDSEEleyyrqmF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 341 TQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGRE 420
Cdd:cd14897 229 HDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 421 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL----DRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 496
Cdd:cd14897 309 RIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNER 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 497 LQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPK 576
Cdd:cd14897 389 LQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 577 FfkSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKevdrivgldqvssgessapvtf 656
Cdd:cd14897 466 Y--VASPGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT---------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 657 gaaglktkkgmfrtvgQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNR 736
Cdd:cd14897 522 ----------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIR 585
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 2414917124 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 |
5.43e-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: 5.43e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 188 GESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVqgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 267
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCV----EQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 268 GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDS 346
Cdd:cd14873 157 GNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 347 MAIMGFTPEELMSMLKVISAVLQFGNISFMkekNHDQASMPDNTAAQKLCHLLGVNVLEFTRAiLTPRIKVGR-EYVQKA 425
Cdd:cd14873 237 MEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQRSMFLRgEEILTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 426 QTKEQADFAVEALAKATYERLFRWLVHRINRALdrRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 505
Cdd:cd14873 313 LNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 506 FILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKskqPR- 584
Cdd:cd14873 391 FSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVK---PRv 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 585 GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDrivgldqvSSGESSAPVTfgaaGLKTK 664
Cdd:cd14873 464 AVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVS--------SRNNQDTLKC----GSKHR 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 665 KgmfRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 744
Cdd:cd14873 532 R---PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYK 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2414917124 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 |
2.50e-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: 516.94 E-value: 2.50e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRgKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 188 GESGAGKTENTKKVIQYLAHVASSHKggtlgRKKEAVqgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-- 265
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDI-----KKRSLV----EAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSkl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 266 -------VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLlCGASEETR-ADLLLGTADQYRFLSGGSIPV------ 331
Cdd:cd14888 151 kskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQL-CAAAREAKnTGLSYEENDEKLAKGADAKPIsidmss 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 332 ------------------PGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQ 393
Cdd:cd14888 230 fephlkfryltksschelPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 394 KL---CHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIG 470
Cdd:cd14888 310 DLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 471 ILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLD 550
Cdd:cd14888 390 VLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 551 EECWFPRATDRSFVEKLSGEQGSHPKF--FKSKQprgeADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHF 628
Cdd:cd14888 467 EECFVPGGKDQGLCNKLCQKHKGHKRFdvVKTDP----NSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPF 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 629 VSELWKE-VDRIVgldqvssgessapvtfgaaGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGK 707
Cdd:cd14888 543 ISNLFSAyLRRGT-------------------DGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDL 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2414917124 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 |
2.53e-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: 472.59 E-value: 2.53e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRH--------EMPPHIYAISEAAYRSMLQDR 179
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 180 EDQSILCTGESGAGKTENTKKVIQYL----AHVASSHKGGTLGRKKEA---VQGELERQLLQANPILEAFGNAKTVKNDN 252
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLtqlsQQEQNSEEVLTLTSSIRAtskSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 253 SSRFGKFIRINFD-VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLL---GTADQYRFLS-GG 327
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLknqLSGDRYDYLKkSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 328 SIPVPGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEK-NHDQASMPDNTAA-QKLCHLLGVNVLE 405
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTlDDNSPCCVKNKETlQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 406 FTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL------DRRQRQGASF-IGILDIAGFE 478
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYLsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 479 IFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFP 556
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 557 RATDRSFVEKLSGEQGSHPKFFKSKQPRGEAdFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkev 636
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF--- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 637 driVGLDQVSSGESSAPVtfgaaglKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQ 716
Cdd:cd14907 554 ---SGEDGSQQQNQSKQK-------KSQKKD-KFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQ 622
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2414917124 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 |
3.95e-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: 3.95e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMY-----------RGKKRHEMPPHIYAISEAAYRSM-- 175
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 176 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQgeLERQLLQANPILEAFGNAKTVKNDNS 253
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSG--IAAKVLQTNILLESFGNARTLRNDNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 254 SRFGKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRAdlllgtadqyrflsggsipvpg 333
Cdd:cd14900 160 SRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK---------------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 334 qsdSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISF-MKEKNHDQASMPDNTAAQKL------CHLLGVNVLEF 406
Cdd:cd14900 218 ---RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFeHDENSDRLGQLKSDLAPSSIwsrdaaATLLSVDATKL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 407 TRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL---DRRQRQGAS-FIGILDIAGFEIFQL 482
Cdd:cd14900 295 EKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVFPK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 483 NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATDRS 562
Cdd:cd14900 375 NSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSDTT 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 563 FVEKLSGEQGSHPKFFKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDplndnvasLLHQSSdhfvselwkeVDrivgl 642
Cdd:cd14900 452 LASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------VD----- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 643 dqvssgessapvtfgaaglktkkgMFRTVGQlYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGV 722
Cdd:cd14900 509 ------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGV 563
|
650 660 670
....*....|....*....|....*....|....
gi 2414917124 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 |
2.22e-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: 2.22e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 111 VLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSML----QDREDQSILC 186
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 187 TGESGAGKTENTKKVIQYLAHVAsshKGGTlgrkkeavqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDv 266
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---RGNS----------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 267 AGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSipvpGQSDS-----ENFT 341
Cdd:cd14889 149 NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGA----GCKREvqywkKKYD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 342 QTMDSMAIMGFTPEELMSMLKVISAVLQFGNISF-MKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAiLTPRIKVGR- 419
Cdd:cd14889 225 EVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFeMDDDEALKVENDSNGWLKAAAGQFGVSEEDLLKT-LTCTVTFTRg 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 420 EYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQG--ASFIGILDIAGFEIFQLNSFEQLCINYTNEKL 497
Cdd:cd14889 304 EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 498 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIerPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKF 577
Cdd:cd14889 384 QYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 578 FKSKqpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEvdRIVGLDQVSSGESSAPVTFG 657
Cdd:cd14889 461 GKSR--SKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTA--TRSRTGTLMPRAKLPQAGSD 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 658 AAGLKTKKgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRI 737
Cdd:cd14889 537 NFNSTRKQ----SVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRP 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 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 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYR--GKKRHE-------MPPHIYAISEAAYRSMLQD- 178
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 179 REDQSILCTGESGAGKTENTKKVIQYLAHVASShKGGTLGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGK 258
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNG-EEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 259 FIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRA-----DLLLGT---ADQYRFLSGGSIP 330
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyefhDGITGGlqlPNEFHYTGQGGAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 331 VPGQ-SDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNTAAQK----LCHLLGVNVLE 405
Cdd:cd14908 240 DLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEF-ESKEEDGAAEIAEEGNEKclarVAKLLGVDVDK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 406 FTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL--DRRQRQGASfIGILDIAGFEIFQLN 483
Cdd:cd14908 319 LLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFECFAHN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 484 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP-RATDRS 562
Cdd:cd14908 398 SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGSDAN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 563 FVEKL--------SGEQGSHPKFFKSKQPRGEADFSIIHYAGKVDYKA-NDWLVKNMDPLNdnvasllhqssdhfvselw 633
Cdd:cd14908 475 YASRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIP------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 634 kevdrivgldqvssgessapvtfgaaglKTKKGMFRTvGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLV 713
Cdd:cd14908 536 ----------------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRV 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 714 LDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPnAIPRT----FMDGKQASEL-----------------MISAL 772
Cdd:cd14908 587 TEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVvlswSMERLDPQKLcvkkmckdlvkgvlspaMVSMK 665
|
730
....*....|....*..
gi 2414917124 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 |
1.71e-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: 1.71e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 188 GESGAGKTENTKKVIQYLAHVASSHKGGTLGRkkeavqgelerqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 267
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTIAK------------VIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 268 GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGG--SIPVPGQSDSENFTQTMD 345
Cdd:cd14904 149 GKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSlaQMQIPGLDDAKLFASTQK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 346 SMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMpDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKA 425
Cdd:cd14904 229 SLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRIS-NGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 426 QTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 505
Cdd:cd14904 308 LAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 506 FILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPRATDRSFVEKL---SGEQGSHP--KFFKS 580
Cdd:cd14904 388 FKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNEsiDFPKV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 581 KQPRgeadFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivgldqvSSGESSAPVTFGAAG 660
Cdd:cd14904 464 KRTQ----FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF------------GSSEAPSETKEGKSG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 661 LKTKKGmfRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 740
Cdd:cd14904 528 KGTKAP--KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPK 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2414917124 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 |
1.54e-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: 1.54e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERyySGLI----YTYSGLFCVVVNPYKNLPiytESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDRE---D 181
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 182 QSILCTGESGAGKTENTKKVIQYLAH--VASSHKGGT----LGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSR 255
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTraVGGKKASGQdieqSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 256 FGKFIRINFDVAGY-IVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPG 333
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 334 QSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEK----NHDQASMPDNTAAQKLCHLLGVNVLEFTRA 409
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDtsegEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 410 ILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrRQRQGASFIGILDIAGFEIFQL-NSFEQL 488
Cdd:cd14891 316 ITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLG-HDPDPLPYIGVLDIFGFESFETkNDFEQL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 489 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATDRSFVEKLS 568
Cdd:cd14891 395 LINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNETLH 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 569 GEQGSHPKFFKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSsdhfvselwkevdrivgldqvssg 648
Cdd:cd14891 472 KTHKRHPCFPRPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS------------------------ 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 649 essapvtfgaaglktkkgmfrtvgQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRI 728
Cdd:cd14891 528 ------------------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEV 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2414917124 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 |
1.08e-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: 1.08e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPiytesivEMYRGKKRHE-------MPPHIYAISEAAYRSMLQ----- 177
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 178 --DREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQGElerQLLQANPILEAFGNAKTVKNDNSSR 255
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISGS---ELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 256 FGKFIRINF-----DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEE--TRADLLLGTADQYRFLSGGS 328
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmkLELQLELLSAQEFQYISGGQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 329 IPV--PGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHD---------------QASMPDNTA 391
Cdd:cd14895 232 CYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 392 AQKL---CHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ------ 462
Cdd:cd14895 312 QQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpn 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 463 ----RQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIEr 538
Cdd:cd14895 392 kaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 539 pANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVA 618
Cdd:cd14895 470 -QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELF 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 619 SLLHQSSDHFVSELWKEVDRIVgldqvssgesSAPVTFGAAGLKTKKGMFRTV--GQLYKESLTKLMATLRNTNPNFLRC 696
Cdd:cd14895 549 SVLGKTSDAHLRELFEFFKASE----------SAELSLGQPKLRRRSSVLSSVgiGSQFKQQLASLLDVVQQTQTHYIRC 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 697 IIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELdk 776
Cdd:cd14895 619 IKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL-- 696
|
730
....*....|...
gi 2414917124 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 |
1.47e-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: 433.44 E-value: 1.47e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAhvasshkggTLGRKKEAVQGeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvAG 268
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLS---------SLYQDQTEDRL---RQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd14896 148 VIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNqGGACRLQGKEDAQDFEGLLKAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 348 AIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQ--ASMPDNTAAQKLCHLLGVNVlEFTRAILTPRIKV---GReyV 422
Cdd:cd14896 228 QGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPP-ERLEGAVTHRVTEtpyGR--V 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 423 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALD-RRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 501
Cdd:cd14896 305 SRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLApPGEAESDATIGVVDAYGFEALRVNGLEQLCINLASERLQLFS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 502 NHTMFILEQEEYQREGIEWNFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSK 581
Cdd:cd14896 385 SQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQ 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 582 QPRgeADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQvssgessapvtfGAAGL 661
Cdd:cd14896 462 LPL--PVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQ------------GKPTL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 662 KTKkgmfrtvgqlYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 741
Cdd:cd14896 528 ASR----------FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQA 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2414917124 742 FRQRYEILTPNAIPrTFMDGKQASELMISALELDKNLFRVGQSKVFFR 789
Cdd:cd14896 598 FLARFGALGSERQE-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
99-800 |
6.08e-129 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 426.37 E-value: 6.08e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 99 DMADLTCLNEASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHE-MPPHIYAISEAAYRSMLQ 177
Cdd:PTZ00014 100 DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 178 DREDQSILCTGESGAGKTENTKKVIQYLAhvasSHKGGTLGRKkeavqgeLERQLLQANPILEAFGNAKTVKNDNSSRFG 257
Cdd:PTZ00014 180 VKKSQTIIVSGESGAGKTEATKQIMRYFA----SSKSGNMDLK-------IQNAIMAANPVLEAFGNAKTIRNNNSSRFG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 258 KFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDS 337
Cdd:PTZ00014 249 RFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 338 ENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFM-KEKN-HDQASM--PDNTAA-QKLCHLLGVNVLEFTRAILT 412
Cdd:PTZ00014 329 KDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEgKEEGgLTDAAAisDESLEVfNEACELLFLDYESLKKELTV 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 413 PRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAsFIGILDIAGFEIFQLNSFEQLCINY 492
Cdd:PTZ00014 409 KVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINI 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 493 TNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPRATDRSFVEKLSGEQG 572
Cdd:PTZ00014 488 TNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLK 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 573 SHPKFFKSKQpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdrivgldQVSSGessa 652
Cdd:PTZ00014 565 NNPKYKPAKV-DSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGV-------EVEKG---- 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 653 pvtfgaaglKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQG 732
Cdd:PTZ00014 633 ---------KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLG 701
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2414917124 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 |
1.01e-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: 1.01e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYR--------GKKRHEMPPHIYAISEAAYRSMLQ-D 178
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 179 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHkggTLGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGK 258
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQ---SSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 259 FIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFL-----SGGSIPVPG 333
Cdd:cd14902 158 FIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLnsygpSFARKRAVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 334 QSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDqasmpDNTAAQKLC--------HLLGVNVLE 405
Cdd:cd14902 238 DKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQE-----DATAVTAASrfhlakcaELMGVDVDK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 406 FTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALD--------RRQRQGASFIGILDIAGF 477
Cdd:cd14902 313 LETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 478 EIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPR 557
Cdd:cd14902 393 ESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 558 ATDRSFVEklsgeqgshpKFFKSKQPRGEadFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELwkevd 637
Cdd:cd14902 470 GSNQALST----------KFYRYHGGLGQ--FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAI----- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 638 rivGLDqvssGESSAPVTFGAAGLKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLD 715
Cdd:cd14902 533 ---GAD----ENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVE 605
|
650 660 670
....*....|....*....|....*....|....*.
gi 2414917124 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 |
9.45e-126 |
|
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: 412.86 E-value: 9.45e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAvqgelerqllqANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNA-----------ALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLG--TADQYRFLSGGSIPVPGQSDSENFTQTMDS 346
Cdd:cd01386 150 QLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNqlAESNSFGIVPLQKPEDKQKAAAAFSKLQAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 347 MAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAI------------LTPR 414
Cdd:cd01386 230 MKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 415 IKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASfIGILDIAGfeiFQLN---------SF 485
Cdd:cd01386 310 GQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPG---FQNPahsgsqrgaTF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 486 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERP---ANPP---------GVLALLDEEC 553
Cdd:cd01386 386 EDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLLDEEA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 554 WFPRATDRSFVEKLS---GEQGS---HPKFFKSKQPRgeaDFSIIHYAGK--VDYKANDWLVK-NMDPLNDNVASLLHQS 624
Cdd:cd01386 466 LYPGSSDDTFLERLFshyGDKEGgkgHSLLRRSEGPL---QFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQES 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 625 SDHFvselwkevdrivgldqvssgessapvtfgaAGLKtKKGMFRTVgqlyKESLTKLMATLRNTNPNFLRCIIPNHE-- 702
Cdd:cd01386 543 QKET------------------------------AAVK-RKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHNag 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 703 ----KRAGKLSPHLVLD------QLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTP-----NAIPRTFMDGKQASEL 767
Cdd:cd01386 588 kderSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkkLGLNSEVADERKAVEE 667
|
730 740
....*....|....*....|..
gi 2414917124 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 |
3.59e-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: 3.59e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRH-EMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 188 GESGAGKTENTKKVIQYLAhvaSSHKGGTLGRKKEAVqgelerqlLQANPILEAFGNAKTVKNDNSSRFGKFIRInfDVA 267
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRIQTAI--------MAANPVLEAFGNAKTIRNNNSSRFGRFMQL--DVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 268 --GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTMD 345
Cdd:cd14876 148 seGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 346 SMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKnhdQASMPDntAA----------QKLCHLLGVNVLEFTRAILTPRI 415
Cdd:cd14876 228 SLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKT---EQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 416 KVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAsFIGILDIAGFEIFQLNSFEQLCINYTNE 495
Cdd:cd14876 303 KAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINITNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 496 KLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPRATDRSFVEKLSGEQGSHP 575
Cdd:cd14876 382 MLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 576 KFFKSKQpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdrivgldqvssgessaPVT 655
Cdd:cd14876 459 KFKPAKV-DSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGV----------------VVE 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 656 FGaaglKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPN 735
Cdd:cd14876 522 KG----KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSY 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2414917124 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 |
1.47e-122 |
|
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: 404.75 E-value: 1.47e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKR-HEMPPHIYAISEAAYRSMLQDREDQSILC 186
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 187 TGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEavQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 266
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNNNNN--NNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 267 AGYIV-GANIETYLLEKSRAT-RQAKDERTFHIFYQLLCGASEETRADLLLGT-ADQYRFL--------------SGGSI 329
Cdd:cd14906 159 SDGKIdGASIETYLLEKSRIShRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqsSNKNS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 330 PVPGQSDS-ENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQAS--MPDNTAA-QKLCHLLGVNVLE 405
Cdd:cd14906 239 NHNNKTESiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 406 FTRAILTPRIKVGREYVQKAQTKE--QADFAVEALAKATYERLFRWLVHRINRALDR----RQRQGAS------FIGILD 473
Cdd:cd14906 319 FKQALLNRNLKAGGRGSVYCRPMEvaQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsNDLAGGSnkknnlFIGVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 474 IAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEEC 553
Cdd:cd14906 399 IFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDEC 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 554 WFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEadFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELW 633
Cdd:cd14906 476 IMPKGSEQSLLEKYNKQYHNTNQYYQRTLAKGT--LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 634 kevdrivgldqvSSGESSAPVTfgaaglKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLV 713
Cdd:cd14906 554 ------------QQQITSTTNT------TKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHV 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 714 LDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALEL------------------- 774
Cdd:cd14906 616 LSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSklktmgisnnkkknnsnsn 695
|
730
....*....|....*...
gi 2414917124 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 |
5.13e-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: 5.13e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKR-HEMPPHIYAISEAAYRSMLQDRE--DQSI 184
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 185 LCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEavqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 264
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAE----RIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 265 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLsggsiPVPGQS-DSENFTQT 343
Cdd:cd14880 157 NRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL-----PNPERNlEEDCFEVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 344 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTA---AQKLCHLLGVNVLEFTRAILTPRIKVGRE 420
Cdd:cd14880 232 REAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRAGKQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 421 YV--QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 498
Cdd:cd14880 312 QQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 499 QLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATD----RSFVEK-LSGEQG- 572
Cdd:cd14880 392 QHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSaaqlQTRIESaLAGNPCl 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 573 SHPKFfkSKQPrgeaDFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVsSGESSA 652
Cdd:cd14880 469 GHNKL--SREP----SFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEP-SGQSRA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 653 PVTfgaaglktkkgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQG 732
Cdd:cd14880 542 PVL--------------TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAG 607
|
650
....*....|....*....
gi 2414917124 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 |
3.23e-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: 387.63 E-value: 3.23e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYS-GLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRG-KKRHEMPPHIYAISEAAYRSM-LQDREDQSIL 185
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 186 CTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKkeaVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 265
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRS---IADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 266 -VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADL-LLGTADQYRFLSGGSI----PVPGQ--SDS 337
Cdd:cd14875 158 pTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDGKtlDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 338 ENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILtprIKV 417
Cdd:cd14875 238 HEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEF-ESDQNDKAQIADETPFLTACRLLQLDPAKLRECFL---VKS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 418 GREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQR-QGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 496
Cdd:cd14875 314 KTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDcSGCKYIGLLDIFGFENFTRNSFEQLCINYANES 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 497 LQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPK 576
Cdd:cd14875 394 LQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 577 FF---KSKQPRgeaDFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELwkevdrivgldqvssgessap 653
Cdd:cd14875 471 YFvlpKSTIPN---QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL--------------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 654 vtfgaagLKTKKGMFR---TVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICR 730
Cdd:cd14875 527 -------LSTEKGLARrkqTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKR 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2414917124 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 |
5.15e-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: 374.99 E-value: 5.15e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRH-----EMPPHIYAISEAAYRSMLQDREDQ 182
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 183 SILCTGESGAGKTENTKKVIQYLAHVASSHkggtlgrkkeavQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 262
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTS------------STDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 263 NFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSI-PVPGQSDSENFT 341
Cdd:cd14886 149 LVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGIDDQKEFA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 342 QTMDSMAIMgFTPEELMSMLKVISAVLQFGNISFMKEKNH---DQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVG 418
Cdd:cd14886 229 PVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMgviNAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVIN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 419 REYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALdRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 498
Cdd:cd14886 308 NETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 499 QLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPRATDRSFVEKLSgeqgSHPK-- 576
Cdd:cd14886 387 QYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSSCK----SKIKnn 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 577 -FFKSKQprGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLdqvssgessapvt 655
Cdd:cd14886 460 sFIPGKG--SQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 656 fgaaglktKKGMFrtVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPN 735
Cdd:cd14886 525 --------MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAY 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 2414917124 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 |
1.94e-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: 1.94e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMY----------RGKKRHEMPPHIYAISEAAYRSMLQ 177
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 178 DREDQSILCTGESGAGKTENTKKVIQYLAhvASSHKGGTLGRKKEAVQGE-------LERQLLQANPILEAFGNAKTVKN 250
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFA--VHCGTGNNNLTNSESISPPaspsrttIEEQVLQSNPILEAFGNARTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 251 DNSSRFGKFIRINF-DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLL-----CGASEETRADLLLGTADQYRFL 324
Cdd:cd14899 159 DNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLsadnnCVSKEQKQVLALSGGPQSFRLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 325 SGG--SIPVPGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISF--MKEKNHDQASMPDNTAAQ------- 393
Cdd:cd14899 239 NQSlcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqIPHKGDDTVFADEARVMSsttgafd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 394 ---KLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRR--------- 461
Cdd:cd14899 319 hftKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 462 -----QRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLI 536
Cdd:cd14899 399 sdvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 537 ERpaNPPGVLALLDEECWFPRATDRSFVEKLSGE---QGSHPKFFKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPL 613
Cdd:cd14899 478 EH--RPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 614 NDNVASLLHQSSDHFVSELWKEvdrivGLDQVSSGESSAPVTFGAAGLKTKKGMFR-TVGQLYKESLTKLMATLRNTNPN 692
Cdd:cd14899 556 CESAAQLLAGSSNPLIQALAAG-----SNDEDANGDSELDGFGGRTRRRAKSAIAAvSVGTQFKIQLNELLSTVRATTPR 630
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 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 |
1.27e-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: 1.27e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYS--------GLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDRE 180
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 181 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGgtlgrkkeAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFI 260
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHG--------ADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKML 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 261 RINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFlsggsipvpgqsDSENF 340
Cdd:cd14887 153 LLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST------------DLRRI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 341 TQTMDSMAIMGFTPEELmsmLKVISAVLQFGNISFMKEKNHDQASMPDNTA--------AQKLCHLL------------- 399
Cdd:cd14887 221 TAAMKTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssglkvte 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 400 -----------------GVNVLEFTRAILTprIKVGREyVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDR-- 460
Cdd:cd14887 298 asrkhlktvarllglppGVEGEEMLRLALV--SRSVRE-TRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRsa 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 461 -----------RQRQGASFIGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI--D 524
Cdd:cd14887 375 kpsesdsdedtPSTTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsA 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 525 FGLDLQPCIDLIERPAN---------------------PPGVLALLDE------ECWFPRATDRSFVEKLSGEQGSHPKF 577
Cdd:cd14887 455 FPFSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSAKY 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 578 FKSKQ--PRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLhQSSDHFVSElwkevdriVGLDQVSsgessapvt 655
Cdd:cd14887 535 KNITPalSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRL--------VGSKKNS--------- 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 656 fgaaGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPN 735
Cdd:cd14887 597 ----GVRAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPC 672
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 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 |
7.08e-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: 7.08e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNlpIYTESIVEMYRGKKRHeMPPHIYAISEAAYRSMLQdREDQSILCTGE 189
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 190 SGAGKTENTKKVIQYLAHvasshkgGTLGRKKeavqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvaGY 269
Cdd:cd14898 78 SGSGKTENAKLVIKYLVE-------RTASTTS------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 270 IVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLlgtadQYRFLSGGSIPVPgqSDSENFTQTMDSMAI 349
Cdd:cd14898 143 ITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI-----DTSSTAGNKESIV--QLSEKYKMTCSAMKS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 350 MGFTpeELMSMLKVISAVLQFGNISFMkekNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKE 429
Cdd:cd14898 216 LGIA--NFKSIEDCLLGILYLGSIQFV---NDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 430 QADFAVEALAKATYERLFRWLVHRINRALdrrQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILE 509
Cdd:cd14898 291 QARTIRNSMARLLYSNVFNYITASINNCL---EGSGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAK 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 510 QEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLsgeqgshpKFFKSKQPRGEADF 589
Cdd:cd14898 368 QGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI--------KKYLNGFINTKARD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 590 SII--HYAGKVDYKANDWLVKNMdplndnvasllhqssdhfvselwkevdrivgldqvssgESSAPVTFGAAGLKTkKGM 667
Cdd:cd14898 436 KIKvsHYAGDVEYDLRDFLDKNR--------------------------------------EKGQLLIFKNLLIND-EGS 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 668 FRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 747
Cdd:cd14898 477 KEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYR 556
|
....*.
gi 2414917124 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 |
2.19e-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: 326.81 E-value: 2.19e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 106 LNEASVLHNLRERYYSGLIYTY---SGLfcVVVNPYKNLPIYTESIVEMYR-------GKKRHEMPPHIYAISEAAYRSM 175
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 176 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTlgrkkeavqgELERQLLQANPILEAFGNAKTVKNDNSSR 255
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGT----------KLSSQISAAEFVLDSFGNAKTLTNPNASR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 256 FGKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFL-SGGSIPV--- 331
Cdd:cd14879 149 FGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLaSYGCHPLplg 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 332 PGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFM--KEKNHDQASMpDNTAA-QKLCHLLGV--NVLEf 406
Cdd:cd14879 229 PGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTydHEGGEESAVV-KNTDVlDIVAAFLGVspEDLE- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 407 trAILTPRIK-VGRE----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEifQ 481
Cdd:cd14879 307 --TSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQ--N 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 482 L-----NSFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIERPanPPGVLALLDE 551
Cdd:cd14879 379 RsstggNSLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGK--PGGLLGILDD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 552 EC-WFPRATDRSFVEKLSGEQGSHPKF---FKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLndnvasllhqSSDh 627
Cdd:cd14879 451 QTrRMPKKTDEQMLEALRKRFGNHSSFiavGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVL----------SPD- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 628 FVSelwkevdrivgldqvssgessapvtfgaaglktkkgMFRTVGQLyKESLTKLMATLRNTNPNFLRCIIPNHEKRAGK 707
Cdd:cd14879 520 FVN------------------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNS 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 708 LSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPnaiprtFMDGKQASELMISALELDKNLFRVGQSKVF 787
Cdd:cd14879 563 FDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVF 636
|
.
gi 2414917124 788 F 788
Cdd:cd14879 637 L 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
109-749 |
2.95e-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: 2.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYR---GKKRHEMPPHIYAISEAAYRSMLQDREDQSIL 185
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 186 CTGESGAGKTENTKKVIQYLAHVASSHKGgtlgrkkeavqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF- 264
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT------------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFc 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 265 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGG----SIPVPGQSDSENF 340
Cdd:cd14878 149 ERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmredVSTAERSLNREKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 341 TQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGRE 420
Cdd:cd14878 229 AVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 421 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAS---FIGILDIAGFEIFQLNSFEQLCINYTNEKL 497
Cdd:cd14878 309 MIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtlDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 498 QQLFNHTMFILEQEEYQREGIewnfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECWFPRATDRSFVEK 566
Cdd:cd14878 389 HHYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVEPNLPKK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 567 LSG---EQGSHPKFFKSKQPRGE-------ADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEv 636
Cdd:cd14878 456 LQSlleSSNTNAVYSPMKDGNGNvalkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 637 drivgldqvssgessapvtfgaaglktkkgMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQ 716
Cdd:cd14878 535 ------------------------------KLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQ 584
|
650 660 670
....*....|....*....|....*....|...
gi 2414917124 717 LRCNGVLEGIRICRQGFPNRIPFQEFRQRYEIL 749
Cdd:cd14878 585 LQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL 617
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
109-789 |
4.04e-92 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 313.88 E-value: 4.04e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLpiytESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHvasshkggtlGRKKEavqGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14937 77 ESGSGKTEASKLVIKYYLS----------GVKED---NEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTMDSMA 348
Cdd:cd14937 144 NIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 349 IMGftpeelMSMLK-----VISAVLQFGNISFM---KEKNHDQASMPDNT--AAQKLCHLLGVNVLEFTRAILTPRIKVG 418
Cdd:cd14937 224 KMN------MHDMKddlflTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 419 REYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 498
Cdd:cd14937 298 NQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLN-NNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIH 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 499 QLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFF 578
Cdd:cd14937 377 SIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 579 KSKQPRGEaDFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdrivgldQVSSgessapvTFGA 658
Cdd:cd14937 453 STKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDV-------EVSE-------SLGR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 659 AGLKTKKgmfrtvgqlYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRIcRQGFPNRIP 738
Cdd:cd14937 518 KNLITFK---------YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYT 587
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2414917124 739 FQEFRQRYEILTPNAIPRTFMDGKQASELMISAlELDKNLFRVGQSKVFFR 789
Cdd:cd14937 588 FDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
109-741 |
6.66e-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: 288.34 E-value: 6.66e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHE-------MPPHIYAISEAAYRSMLQDRE 180
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 181 DQSILCTGESGAGKTENTKKVIQYLAHVASshkggtlgrkkEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFI 260
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQT-----------DSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRIN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 261 RINFD---------VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRAD-----------LLLGTADQ 320
Cdd:cd14884 150 LLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARrnlvrncgvygLLNPDESH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 321 YRFLSGGSIPVPG----------QSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFmkeknhdqasmpdnt 390
Cdd:cd14884 230 QKRSVKGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAY--------------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 391 aaQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGA---- 466
Cdd:cd14884 295 --KAAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdne 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 467 -------SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERp 539
Cdd:cd14884 373 diysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 540 anppgVLALLDE-----ECWFPRATDRSFVEKLSGE-----QGSHPKFFKS---------KQPRGEADFSIIHYAGKVDY 600
Cdd:cd14884 451 -----IFRRLDDitklkNQGQKKTDDHFFRYLLNNErqqqlEGKVSYGFVLnhdadgtakKQNIKKNIFFIRHYAGLVTY 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 601 KANDWLVKNMDPLNDNVASLLHQSSDHFVSElwkevdrivgldqvssgessapvtfgaAGLKTKKGMFRTVGQLYKESLT 680
Cdd:cd14884 526 RINNWIDKNSDKIETSIETLISCSSNRFLRE---------------------------ANNGGNKGNFLSVSKKYIKELD 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2414917124 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 |
1.80e-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: 1.80e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYknlpiytesiveMYRGKKRH-------EMPPHIYAISEAAYRSMLQDREDQ 182
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 183 SILCTGESGAGKTENTKKVIQYLAHVAsshkGGtlGRKKEAVqgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 262
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVA----GG--GPETDAF-----KHLAAAFTVLRSLGSAKTATNSESSRIGHFIEV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 263 NFdVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLG--TADQYRFLSGGSIPVPGQSDSENF 340
Cdd:cd14881 139 QV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYLSHGDTRQNEAEDAARF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 341 TQTMDSMAIMGFtpeELMSMLKVISAVLQFGNISFMkEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAiLTPRIK-VGR 419
Cdd:cd14881 218 QAWKACLGILGI---PFLDVVRVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRG-LTTRTHnARG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 420 EYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALdrrqRQGAS--------FIGILDIAGFEIFQLNSFEQLCIN 491
Cdd:cd14881 293 QLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSLK----RLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCIN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 492 YTNEKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPRATDRSFVEKLSGE 570
Cdd:cd14881 369 LCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQ 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 571 QGSHPKFFKSKQPRGEAdFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSdhfvselwkevdrivgldqvssges 650
Cdd:cd14881 445 HRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN------------------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 651 sapVTFGaaglktkkgmFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICR 730
Cdd:cd14881 499 ---CNFG----------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMA 565
|
650 660
....*....|....*....|....*.
gi 2414917124 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 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYrgKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAHVasshkggTLGRKKEavqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 268
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTT-------DLSRSKY-----LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 269 YIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSM 347
Cdd:cd14905 148 EIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNqGGSISVESIDDNRVFDRLKMSF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 348 AIMGFTPEELMSMLKVISAVLQFGNISFMKEKNhdQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAqt 427
Cdd:cd14905 228 VFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 428 keqadfavEALAKATYERLFRWLVHRINRALdrRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFI 507
Cdd:cd14905 304 --------DSLARSLYSALFHWIIDFLNSKL--KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 508 LEQEEYQREGIEW-NFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFfkSKQPRge 586
Cdd:cd14905 374 QEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLF--GKKPN-- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 587 aDFSIIHYAGKVDYKANDWLVKNMDPLNDNvASLLHQSS--DHFVSE--LWKEVDRIVGLDQVSSGESSA---PVTF--- 656
Cdd:cd14905 443 -KFGIEHYFGQFYYDVRGFIIKNRDEILQR-TNVLHKNSitKYLFSRdgVFNINATVAELNQMFDAKNTAkksPLSIvkv 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 657 --------------------GAAGLKTKKGMFRTVGQLYKE-SLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLD 715
Cdd:cd14905 521 llscgsnnpnnvnnpnnnsgGGGGGGNSGGGSGSGGSTYTTySSTNKAINNSNCDFHFIRCIKPNSKKTHLTFDVKSVNE 600
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2414917124 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 |
9.67e-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: 248.25 E-value: 9.67e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYrgkkrhemppHIYAISEAAYRSMLQDRED-QSILCT 187
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 188 GESGAGKTENTKKVIQYLAhvaSSHKGGTLGRKKEAVQGelerqllqanpILEAFGNAKTVKNDNSSRFGKFIRINFDvA 267
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPKSKVTTKHSSAIES-----------VFKSFGCAKTLKNDEATRFGCSIDLLYK-R 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 268 GYIVGANIE-TYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTMDS 346
Cdd:cd14874 136 NVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 347 MAIMGFTPEELMSMLKVISAVLQFGNISFMKEKN----HDQASMPDNTAAQKLCHLLGVNVLEFTrAILTPRIKVGREYv 422
Cdd:cd14874 216 LHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnveQDVVEIGNMSEVKWVAFLLEVDFDQLV-NFLLPKSEDGTTI- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 423 qkaqTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAsfIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 502
Cdd:cd14874 294 ----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 503 HTMFILEQEEYQREGIEWNF-IDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSK 581
Cdd:cd14874 368 KHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKAR 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 582 QpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELwkevdrivgldqVSSGESSApvtfgaagl 661
Cdd:cd14874 446 N-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLL------------FESYSSNT--------- 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 662 ktkKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 741
Cdd:cd14874 504 ---SDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTT 580
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2414917124 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 |
2.23e-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: 2.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 112 LHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKR----------HEMPPHIYAISEAAYRSMLQDRED 181
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 182 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 261
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 262 INFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEET--RADLLLG-TADQYRFLSGGSIPVPGQS-DS 337
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPtlRDSLEMNkCVNEFVMLKQADPLATNFAlDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 338 ENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFM------KEKN-------HDQASMPDNTAAQKL--CHLLGVN 402
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVpdpeggKSVGgansttvSDAQSCALKDPAQILlaAKLLEVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 403 --VLE---FTRAILTpriKVGREYVQ--KAQTKEQADFAVEALAKATYERLFRWLVHRINRAL----DRR-------QRQ 464
Cdd:cd14893 324 pvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYeksniviNSQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 465 GasfIGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQPCIDL 535
Cdd:cd14893 401 G---VHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 536 IERPanPPGVLALLDEECWFPRATDRSFVEKL-SGEQGSHpkffKSKQPRGEAD---------------FSIIHYAGKVD 599
Cdd:cd14893 478 FEDK--PFGIFDLLTENCKVRLPNDEDFVNKLfSGNEAVG----GLSRPNMGADttneylapskdwrllFIVQHHCGKVT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 600 YKANDWLVKNMDPLNDNVASLLHQSSDhfvselwkEVDRIVGLDQVSSGESSAPVTfGAAGLKTKKGMFRTVGQLYKESL 679
Cdd:cd14893 552 YNGKGLSSKNMLSISSTCAAIMQSSKN--------AVLHAVGAAQMAAASSEKAAK-QTEERGSTSSKFRKSASSARESK 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 680 T--------------KLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQR 745
Cdd:cd14893 623 NitdsaatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRR 702
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 2414917124 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 |
6.80e-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: 236.95 E-value: 6.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 190 SGAGKTENTKKVIQYLAHvasshkggtLGRKKEAVQGELERqllqANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 269
Cdd:cd14882 82 SYSGKTTNARLLIKHLCY---------LGDGNRGATGRVES----SIKAILALVNAGTPLNADSTRCILQYQLTFGSTGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 270 IVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETR-ADLLLGTADQYRFLsggSIP--VPG----------QSD 336
Cdd:cd14882 149 MSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRlKEYNLKAGRNYRYL---RIPpeVPPsklkyrrddpEGN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 337 SENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMkeKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIK 416
Cdd:cd14882 226 VERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFR--QNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 417 VGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALD-RRQRQGASF-IGILDIAGFEIFQLNSFEQLCINYTN 494
Cdd:cd14882 304 KGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfPRAVFGDKYsISIHDMFGFECFHRNRLEQLMVNTLN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 495 EKLQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQPCIdlierpANPPGVLALLDEECWfPRATDRSFVEKLSGEQ 571
Cdd:cd14882 384 EQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVDQLM------TKPDGLFYIIDDASR-SCQDQNYIMDRIKEKH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 572 GSHPKffkskqPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEvdrivglDQVSSgess 651
Cdd:cd14882 457 SQFVK------KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRN---- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 652 apvtfgaagLKTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRI 728
Cdd:cd14882 520 ---------MRTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKA 584
|
650 660
....*....|....*....|.
gi 2414917124 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 2414917124 131 FCVVVNPYKNLPIYTESIV-EMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 209
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 210 SSHKGGT---LGRKKEAVQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAT 286
Cdd:cd01363 81 FNGINKGeteGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGFEIINESLNTLMNVLRAT 160
|
.
gi 2414917124 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 |
4.13e-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: 206.61 E-value: 4.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYR-GKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 189 ESGAGKTENTKKVIQYLAH-VASSHKGGTLGRKKEAV----------QGELERQLLQANPILEAFGNAKTVKNDNSSRFG 257
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYqVKGSRRLPTNLNDQEEDnihneentdyQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 258 KFIRINFDvAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDS 337
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 338 ENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKE--------------------------KNHDQASMPDNTA 391
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAfrkksllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 392 AQKL-CHLLGVNVLEFTRAILTPRIkVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQR--QGASF 468
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 469 IGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANppGVLAL 548
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 549 LDEECWFPRATDRSFVEKLSGEQGSH-PKFFKSKQPRG-EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSD 626
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSIIRKFSRnSKYIKKDDITGnKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 627 HFVSEL-----WKEVDRIVGLDQVSSGESSapvtfgaagLKTKKGMFRTVGQ----LYKESLTKLMATLRNTNPNFLRCI 697
Cdd:cd14938 558 EYMRQFcmfynYDNSGNIVEEKRRYSIQSA---------LKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCM 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 698 IPNHEKRA-GKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEIltPNAiprtfmDGKQASELMISALELDK 776
Cdd:cd14938 629 KPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI--KNE------DLKEKVEALIKSYQISN 700
|
730
....*....|.
gi 2414917124 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 |
2.55e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 131.33 E-value: 2.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 987 LLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKreeq 1066
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ---- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1067 grlEQEKFKRRMESEAMEAQEQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVE 1146
Cdd:TIGR02168 306 ---ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1147 NERGMRERAEKQRRDLSEELEALRTELEdtlDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSL 1226
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1227 QEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRsESERGRKRADNQLQELSARLAQADREREDREERMHKLQCE 1306
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ-ENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1307 IES-LSGNLSSSDSKSLRLAKE-ISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQI 1384
Cdd:TIGR02168 539 IEAaLGGRLQAVVVENLNAAKKaIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1385 QTHSQQL---------TELRKQSEEVNSAV-EAGDEIRRK--LQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTI 1452
Cdd:TIGR02168 619 SYLLGGVlvvddldnaLELAKKLRPGYRIVtLDGDLVRPGgvITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEK 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1453 ALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRL--- 1529
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEela 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1530 ----EMEQLVNQQDDVGKNVHELERTRRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEReISTNEEKG 1605
Cdd:TIGR02168 779 eaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE-LSEDIESL 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1606 EEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDEAKVT 1685
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 2414917124 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 |
9.18e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 129.79 E-value: 9.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1122 ARRTEAQRSLREA---LSQV----SELKEEVENERGMRERAEKQRrDLSEELEALRTELEdTLDSTAAQQELRsRREAEL 1194
Cdd:TIGR02168 172 ERRKETERKLERTrenLDRLedilNELERQLKSLERQAEKAERYK-ELKAELRELELALL-VLRLEELREELE-ELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1195 SELQRCVEEETRR---HETQLSELRVKHS---AALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSES 1268
Cdd:TIGR02168 249 KEAEEELEELTAElqeLEEKLEELRLEVSeleEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1269 ERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQ 1348
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1349 KMALASRVRALEEEKNGLmeRLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAiqrerq 1428
Cdd:TIGR02168 409 LERLEDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA------ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1429 keeekERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKF---DQCLAE--------EKAVSARLAEERDRAEADSR 1497
Cdd:TIGR02168 481 -----ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgiLGVLSElisvdegyEAAIEAALGGRLQAVVVENL 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1498 EKETRCLAlsrALQEAQDQK-----EELERANKQLRLEMEQLVNQQDDVGKN---VHELERTRRTLETEAQNLRIQTQEL 1569
Cdd:TIGR02168 556 NAAKKAIA---FLKQNELGRvtflpLDSIKGTEIQGNDREILKNIEGFLGVAkdlVKFDPKLRKALSYLLGGVLVVDDLD 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1570 EEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEA 1649
Cdd:TIGR02168 633 NALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1650 QVETANRGKEEAMKQLRRLQGQMKEVLRELDEAKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERD 1729
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1730 EIADEMVSSSSGKNVLSEEKRRLDARVNQLEEDLEEEQTN-------NELLTERLRKTALQVETLTVQLQGERTLAQKAE 1802
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRiaaterrLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1803 AA-------REQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQ 1875
Cdd:TIGR02168 873 SEleallneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT 952
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1876 AEDERRHADQYREQLDKSMVRLKQLKRQL-----------EEVEEENSRS---SAQKRKLQRELEELTDSSQTMNREISS 1941
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnlaaiEEYEELKERYdflTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
.
gi 2414917124 1942 L 1942
Cdd:TIGR02168 1033 R 1033
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
115-730 |
9.18e-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: 116.00 E-value: 9.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 115 LRERYYSGLIYTYSGLFCV-VVNPYKNL------PIYTESIVEMYRGKKRHE--MPPHIYAISE---------------- 169
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 170 ----AAYRSMLQDReDQSILCTGESGAGKTENTKKVIQYLAHVA---------------------------SSHKGGTLG 218
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetckvsgstrqpkiklftSSTKSTIQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 219 RKKEA------------------------------------------VQG------------ELERQL------------ 232
Cdd:cd14894 166 RTEEArtialleakgvekyeivlldlhperwdemtsvsrskrlpqvhVDGlffgfyeklehlEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 233 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVAGY---IVGANIETYLLEKSRATRQA------KDERTFHI 297
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 298 FYQLLCGASEETRADLL----------------LGTADqYRFLSGGSIPVPGQSDSENFTQTMDSMAIMGFTPEELMSML 361
Cdd:cd14894 326 LYAMVAGVNAFPFMRLLakelhldgidcsaltyLGRSD-HKLAGFVSKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 362 KVISAVLQFGNISFMKEKNHDQASMPDN---TAAQKLCHLLGVNVLE-FTRAILTPRIKV--GREYVQKAQTKEQADFAV 435
Cdd:cd14894 405 KVLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEkLERMLMTKSVSLqsTSETFEVTLEKGQVNHVR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 436 EALAKATYERLFRWLVHRINRAL-------DRRQRQ---------GASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQq 499
Cdd:cd14894 485 DTLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY- 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 500 lfnhtmfileQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATD--------------RSFVE 565
Cdd:cd14894 564 ----------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENmnaqqeekrnklfvRNIYD 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 566 KLSGEQGSHPKFFKSKQPRGEA-----DFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRI- 639
Cdd:cd14894 634 RNSSRLPEPPRVLSNAKRHTPVllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQLg 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 640 ----VGLDQVSSGESSapvtfgAAGLKTKKGMFRTVGQLYKESLTKLMatlrntnPNFLRCIIPNHEKRAGKLSPHLVLD 715
Cdd:cd14894 714 wspnTNRSMLGSAESR------LSGTKSFVGQFRSHVNVLTSQDDKNM-------PFYFHCIRPNAKKQPSLVNNDLVEQ 780
|
810
....*....|....*
gi 2414917124 716 QLRCNGVLEGIRICR 730
Cdd:cd14894 781 QCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1678 |
3.55e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.77 E-value: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 847 LRNWQWWRLftkvkpLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEAELFAEAEE 926
Cdd:TIGR02168 222 LRELELALL------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 927 MRARLASRKQeleevlgeletrleeeeergvQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLA 1006
Cdd:TIGR02168 296 EISRLEQQKQ---------------------ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1007 TAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQgrlEQEKFKRRMESEAMEAQ 1086
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED---RRERLQQEIEELLKKLE 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1087 E-QLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEE 1165
Cdd:TIGR02168 432 EaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1166 LE----------------------------ALRTELEDTLDSTAAQQ------------------ELRSRREAELSELQR 1199
Cdd:TIGR02168 512 LKnqsglsgilgvlselisvdegyeaaieaALGGRLQAVVVENLNAAkkaiaflkqnelgrvtflPLDSIKGTEIQGNDR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1200 CVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRA---RQSLEKAKATLEEERqnLTSELKSLQASRSESERGRKRAD 1276
Cdd:TIGR02168 592 EILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVddlDNALELAKKLRPGYR--IVTLDGDLVRPGGVITGGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1277 NQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRV 1356
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1357 RALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDsaiqrerqkeeekerv 1436
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT---------------- 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1437 erqrerlreeieDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQ 1516
Cdd:TIGR02168 814 ------------LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1517 KEELERANKQLRLEMEQLVNQQDDVGKNVHELERTRRTLETEAQNLRIQTQeleeelseaensrlRLEVTLQALKAQF-- 1594
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE--------------GLEVRIDNLQERLse 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1595 -----EREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQ 1669
Cdd:TIGR02168 948 eysltLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
....*....
gi 2414917124 1670 GQMKEVLRE 1678
Cdd:TIGR02168 1028 REARERFKD 1036
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
962-1816 |
1.78e-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: 99.28 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 962 EKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTK 1041
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1042 SLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEg 1121
Cdd:pfam02463 255 SSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1122 arrteaqrslreaLSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCV 1201
Cdd:pfam02463 334 -------------KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1202 EEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQE 1281
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1282 LSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDAREL-LQDESRQKMALASRVRALE 1360
Cdd:pfam02463 481 KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENyKVAISTAVIVEVSATADEV 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1361 EEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQR 1440
Cdd:pfam02463 561 EERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKES 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1441 ERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEEL 1520
Cdd:pfam02463 641 AKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1521 ERANKQLRLEM----EQLVNQQDDVGKNVHELERTRRTLETEaQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFER 1596
Cdd:pfam02463 721 ELLADRVQEAQdkinEELKLLKQKIDEEEEEEEKSRLKKEEK-EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1597 EISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVL 1676
Cdd:pfam02463 800 EEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEEL 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1677 RELDEAKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVL-SEEKRRLDAR 1755
Cdd:pfam02463 880 EEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKeKEENNKEEEE 959
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2414917124 1756 VNQLEEDLEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELK 1816
Cdd:pfam02463 960 ERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
864-1402 |
2.82e-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: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 864 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLG 943
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 944 ELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLE 1023
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1024 ERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSDLRGSL 1103
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1104 AQKEKEITSLQGRLEEEGARRTEA-QRSLREALSQVSELKEEVENERGMRERAEKQR--RDLSEELEALRTELEDTLDST 1180
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAgLRGLAGAVAVLIGVEAAYEAALEAALAAALQNivVEDDEVAAAAIEYLKAAKAGR 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1181 AAQQEL---RSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQnLTSE 1257
Cdd:COG1196 574 ATFLPLdkiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE-VTLE 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1258 LKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIEslsgnlsssdskslRLAKEISSLESQLHD 1337
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE--------------EEERELAEAEEERLE 718
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2414917124 1338 ARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVN 1402
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVN 783
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1036-1749 |
7.16e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 97.45 E-value: 7.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1036 EEEKTKSLNKLK------NKQEAVIADLEERLKREEQGRLEQEKFK----RRMESEAMEAQEQLSDLGMLSSDLRGSLAQ 1105
Cdd:TIGR02169 169 DRKKEKALEELEeveeniERLDLIIDEKRQQLERLRREREKAERYQallkEKREYEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1106 KEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENE-RGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQ 1184
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1185 ELRSRREAELSELQRCVEEETRRhetqlselRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQAS 1264
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKR--------RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1265 RSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQD 1344
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1345 ESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVE--AGDEI----------- 1411
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaAGNRLnnvvveddava 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1412 --------RRKLQREldSAIQRERQKEEEKERVERQRERLREEIEDMtIALQRERQNCTA-------------------- 1463
Cdd:TIGR02169 561 keaiellkRRKAGRA--TFLPLNKMRDERRDLSILSEDGVIGFAVDL-VEFDPKYEPAFKyvfgdtlvvedieaarrlmg 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1464 -----------LEK--------RQKKFDQCLA-EEKAVSARLAE-------ERDRAEADSREKETRCLALSRALQEAQDQ 1516
Cdd:TIGR02169 638 kyrmvtlegelFEKsgamtggsRAPRGGILFSrSEPAELQRLRErleglkrELSSLQSELRRIENRLDELSQELSDASRK 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1517 KEELERANKQLRLEMEQLVNQQDDVGKNVHELERTRRTLETEAQNLRiqtQELEEELSEAENSRLRLEVTLQALKAQFER 1596
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE---ARIEELEEDLHKLEEALNDLEARLSHSRIP 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1597 EISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQ-------VETANRGKEEAMKQLRRLQ 1669
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQiksiekeIENLNGKKEELEEELEELE 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1670 GQMKEVLRELDEAKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVS-SSSGKNVLSEE 1748
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdEEIPEEELSLE 954
|
.
gi 2414917124 1749 K 1749
Cdd:TIGR02169 955 D 955
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1324-1939 |
1.58e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1324 LAKEISSLESQ---LHDARELLQD-ESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSE 1399
Cdd:COG1196 198 LERQLEPLERQaekAERYRELKEElKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1400 EVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEK 1479
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1480 AVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERTRRTLETEA 1559
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1560 QNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREistnEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQ 1639
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL----EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1640 LEAELQEAEAQVETANRGKEEAMKQLR--RLQGQMKEVLRELDEAkvtRDDVISQSKDSEKKIQTLEAEVLHLTEELAVS 1717
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALeaALAAALQNIVVEDDEV---AAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1718 ERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEDLEEEQTNNELLTERLRKTALQVETLTVQLQGERTL 1797
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1798 AQKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKE--VMMQ 1875
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEeeLLEE 750
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2414917124 1876 AEDERRHADQYREQLDKsmvRLKQLKRQL--------------EEVEEENSRSSAQKRKLQRELEELTDSSQTMNREI 1939
Cdd:COG1196 751 EALEELPEPPDLEELER---ELERLEREIealgpvnllaieeyEELEERYDFLSEQREDLEEARETLEEAIEEIDRET 825
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
990-1551 |
2.05e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 95.49 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 990 EKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLknkqEAVIADLEERLKREEQgrl 1069
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETL----EAEIEDLRETIAETER--- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1070 EQEKFKRRMEseamEAQEQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENER 1149
Cdd:PRK02224 273 EREELAEEVR----DLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1150 GMRERAEKQRRDLSEELEALRTELEDTldstaaqQELRSRREAELSELqrcvEEETRRHETQLSELRVKHSAALDSLQEQ 1229
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEA-------REAVEDRREEIEEL----EEEIEELRERFGDAPVDLGNAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1230 LDNSKRARQSLEKAKATLEEERQNLTSELKSLQASR----------SESERGRKRADNQLQELSARLAQADREREDREER 1299
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1300 MHKLQcEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKE 1379
Cdd:PRK02224 498 LERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1380 LSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQ 1459
Cdd:PRK02224 577 LNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKE 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1460 NC-TALEKRQKKFDQCLAEEKAVSARL-AEERDRAEADS-REKETRCLALSRALQEAQDQKEELERANKQLRLEMEQlvn 1536
Cdd:PRK02224 657 RAeEYLEQVEEKLDELREERDDLQAEIgAVENELEELEElRERREALENRVEALEALYDEAEELESMYGDLRAELRQ--- 733
|
570
....*....|....*
gi 2414917124 1537 qqddvgKNVHELERT 1551
Cdd:PRK02224 734 ------RNVETLERM 742
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
946-1563 |
8.70e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.46 E-value: 8.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 946 ETRLEeeeergvQLANEKKKMQ--QNIQDLEEQLEeeesaRQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLE 1023
Cdd:COG1196 199 ERQLE-------PLERQAEKAEryRELKEELKELE-----AELLLLKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1024 ERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRleqekfkrrmeseameaqeqlsdlgmlsSDLRGSL 1103
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----------------------------RELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1104 AQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELedtLDSTAAQ 1183
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL---LEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1184 QELRSRREAELSELQRCVEEETRRHETQLSEL--RVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSL 1261
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEeaLAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1262 QASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDAREL 1341
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1342 LQDESRQ----KMALASRVRALEEEKnglmeRLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQR 1417
Cdd:COG1196 556 DEVAAAAieylKAAKAGRATFLPLDK-----IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1418 ELDSAIQRERQKEEEKERVERQRERLREEIEdmtIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSR 1497
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGS---LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2414917124 1498 EKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERTRRTLETEAQNLR 1563
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1203-1947 |
1.12e-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: 93.58 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1203 EETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQ------SLEKAKATLEEERQNltSELKSLQASRSESERGRKRAD 1276
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAERYKElkaelrELELALLVLRLEELR--EELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1277 NQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRV 1356
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1357 RALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVeagdeirRKLQRELDSAiqrerqkeeekerv 1436
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV-------AQLELQIASL-------------- 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1437 erqrerlreeiedmTIALQRERQNCTALEKRQKKFDQCLAEekavsarlaEERDRAEADSREKETRCLALSRALQEAQDQ 1516
Cdd:TIGR02168 399 --------------NNEIERLEARLERLEDRRERLQQEIEE---------LLKKLEEAELKELQAELEELEEELEELQEE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1517 KEELERANKQLRLEMEQLVNQQDDVGKNVHELERTRRTLETEAQNLriqtQELEEELSEAENSRLRLEVTLQAL------ 1590
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL----EGFSEGVKALLKNQSGLSGILGVLselisv 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1591 KAQFEREIST------------NEEKGEEKRRALSK----QVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETA 1654
Cdd:TIGR02168 532 DEGYEAAIEAalggrlqavvveNLNAAKKAIAFLKQnelgRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFD 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1655 NRGK----------------EEAMKQLRRLQGQMKEVlrELDEAKVTRDDVIS-QSKDSEKKIQTLEAEVLHLTEELAVS 1717
Cdd:TIGR02168 612 PKLRkalsyllggvlvvddlDNALELAKKLRPGYRIV--TLDGDLVRPGGVITgGSAKTNSSILERRREIEELEEKIEEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1718 ERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEDLEEEQTNNELLTERLRKTALQVETLTVQLQGERTL 1797
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1798 AQKAEAAREQLEKQNKELKARLGEMEGAVrGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAE 1877
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEEL-KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1878 DERRHADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLS 1947
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1009-1728 |
3.85e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.13 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1009 VEQRERLGKEKKQLE--ERLNEVTDQLTEEEEKtkslnKLKNKQEAVIADLEERLKREEQGRlEQEKFKRRMESEAMEAQ 1086
Cdd:PTZ00121 1066 VGQDEGLKPSYKDFDfdAKEDNRADEATEEAFG-----KAEEAKKTETGKAEEARKAEEAKK-KAEDARKAEEARKAEDA 1139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1087 EQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREaLSQVSELK--EEV---------ENERGMRE-- 1153
Cdd:PTZ00121 1140 RKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEE-VRKAEELRkaEDArkaeaarkaEEERKAEEar 1218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1154 ------------RAEKQRRDLSE--------ELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLS 1213
Cdd:PTZ00121 1219 kaedakkaeavkKAEEAKKDAEEakkaeeerNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKA 1298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1214 ElRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNqlQELSARLAQADRER 1293
Cdd:PTZ00121 1299 E-EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA--AEEKAEAAEKKKEE 1375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1294 EDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRAlEEEKNGLMERLEEE 1373
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA-EEAKKADEAKKKAE 1454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1374 EERGKELSRQIQTHSQQLTELRKQSEEVNSAveagDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIA 1453
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKA----DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1454 LQRERQNCTALEKRQKKFDQClaeEKAVSARLAEERDRAEADSREKETRCLALSRAlQEAqdQKEELERANKQLRLEMEQ 1533
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADEL---KKAEELKKAEEKKKAEEAKKAEEDKNMALRKA-EEA--KKAEEARIEEVMKLYEEE 1604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1534 LVNQQDDVGKNVHELERTRRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRRALS 1613
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1614 KQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEaQVETANRGKEEAMKQLRRLQGQMKEVLRELDEAKVTRDDVISQS 1693
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE-ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK 1763
|
730 740 750
....*....|....*....|....*....|....*
gi 2414917124 1694 KDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQER 1728
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1152-1826 |
7.90e-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: 7.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1152 RERAEKQRRDLSEELE---ALRTELEDTLDSTAAQQElRSRREAELSElqrcvEEETRRHETQLSELRvkhsaaldslqe 1228
Cdd:COG1196 174 KEEAERKLEATEENLErleDILGELERQLEPLERQAE-KAERYRELKE-----ELKELEAELLLLKLR------------ 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1229 qldnskrarqSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIE 1308
Cdd:COG1196 236 ----------ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1309 SLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKnglmerleeeeergkelsrqiqthS 1388
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL------------------------A 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1389 QQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQ 1468
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1469 KKfdqcLAEEKAVSARLAEERDRAEADSREKETRcLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHEL 1548
Cdd:COG1196 442 EA----LEEAAEEEAELEEEEEALLELLAELLEE-AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1549 ERTRRtLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERS 1628
Cdd:COG1196 517 AGLRG-LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARG 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1629 QRSQSVSSKKQLEAELQEAEAQVETANRGkeEAMKQLRRLQGQMKEVLRELDEAKVTRDDVISQSKDSEKKIQTLEAEVL 1708
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLG--RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1709 HLTEELAVSERQKRQAQQERDEIADEMvssssgknvLSEEKRRLDARVNQLEEDLEEEQTNNELLTERLRKTALQVETLT 1788
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALL---------AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
650 660 670
....*....|....*....|....*....|....*....
gi 2414917124 1789 VQLQGERTLAQKAEAA-REQLEKQNKELKARLGEMeGAV 1826
Cdd:COG1196 745 EELLEEEALEELPEPPdLEELERELERLEREIEAL-GPV 782
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1389-1946 |
2.89e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.46 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1389 QQLTELRKQSEEVNSAVEAGDEIR-----------RKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRE 1457
Cdd:COG1196 200 RQLEPLERQAEKAERYRELKEELKeleaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1458 RQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQ 1537
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1538 QDDVGKNVHELERTRRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFER------EISTNEEKGEEKRRA 1611
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERleeeleELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1612 LSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETAnRGKEEAMKQLRRLQGQMKEVLRELDEAKVTRDDVIS 1691
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL-LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1692 QSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKN--------VLSEEKRRLDARVNQLEEDL 1763
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKagratflpLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1764 EEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAV--RGKHRMSVAALEAKI 1841
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSltGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1842 ETMEEQLEQerqeraiANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKL 1921
Cdd:COG1196 679 AELEELAER-------LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570 580
....*....|....*....|....*
gi 2414917124 1922 QRELEELTDSSQTMNREISSLRNQL 1946
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1127-1942 |
1.48e-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: 86.28 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1127 AQRSLREALSQVSELKEEVENERGMRERAEKQR-------RDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQR 1199
Cdd:TIGR02169 154 ERRKIIDEIAGVAEFDRKKEKALEELEEVEENIerldliiDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1200 CVEEETRRHETQLSELRvKHSAALDSLQEQL-DNSKRARQSLE----KAKATLEEERQNLTSELKSLQASRSESERGRKR 1274
Cdd:TIGR02169 234 ALERQKEAIERQLASLE-EELEKLTEEISELeKRLEEIEQLLEelnkKIKDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1275 ADNQLQELSARLAQADREredreerMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDES----RQKM 1350
Cdd:TIGR02169 313 KERELEDAEERLAKLEAE-------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDkefaETRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1351 ALASRVRALE---EEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRER 1427
Cdd:TIGR02169 386 ELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1428 QKEEEkerverqrerlreeiedmtiaLQRERQNCTALEKRQKKFDQCLAEEKAvSARLAEERDRAEADSREketrclALS 1507
Cdd:TIGR02169 466 KYEQE---------------------LYDLKEEYDRVEKELSKLQRELAEAEA-QARASEERVRGGRAVEE------VLK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1508 RALQEAQDQKEELERANKQLRLEME--------QLVNQQDDVGKNVHELERTRRTLETEAQNLRIQTQELEEELSEAENS 1579
Cdd:TIGR02169 518 ASIQGVHGTVAQLGSVGERYATAIEvaagnrlnNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDG 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1580 RLRLEVTLQALKAQFEREI-----STNEEKGEEKRRALSKQVR--ELEIQLEEE-------RSQRSQSVSSKKQLEAELQ 1645
Cdd:TIGR02169 598 VIGFAVDLVEFDPKYEPAFkyvfgDTLVVEDIEAARRLMGKYRmvTLEGELFEKsgamtggSRAPRGGILFSRSEPAELQ 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1646 EAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDEAKvtrddviSQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQ 1725
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS-------RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1726 QERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEDLEEEQTNN-----ELLTERLRKTALQVETLTVQLQGERTLAQK 1800
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1801 AEAAREQLEKQNKELKARLGEMEGAvrgkhrmsVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDER 1880
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKE--------IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2414917124 1881 RHADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKLQRE------LEELTDSSQTMNREISSL 1942
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRAL 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
987-1757 |
1.58e-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: 86.28 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 987 LLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEK------------TKSLNKLKNKQ---E 1051
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlgeeeqlrvKEKIGELEAEIaslE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1052 AVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSL 1131
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1132 REALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLdstAAQQELRSRREAelselqrcVEEETRRHETQ 1211
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE---AKINELEEEKED--------KALEIKKQEWK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1212 LSELRvkhsAALDSLQEQLdnsKRARQSLEKakatLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADR 1291
Cdd:TIGR02169 457 LEQLA----ADLSKYEQEL---YDLKEEYDR----VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHG 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1292 EREDREERMHKLQCEIESLSGN------------------------------LSSSDSKSLRLAKEISSLESQLHDAREL 1341
Cdd:TIGR02169 526 TVAQLGSVGERYATAIEVAAGNrlnnvvveddavakeaiellkrrkagratfLPLNKMRDERRDLSILSEDGVIGFAVDL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1342 LQDESRQKMALASR------VRALEE------------------EKNGLMERLEEEEERGKELSRQiqtHSQQLTELRKQ 1397
Cdd:TIGR02169 606 VEFDPKYEPAFKYVfgdtlvVEDIEAarrlmgkyrmvtlegelfEKSGAMTGGSRAPRGGILFSRS---EPAELQRLRER 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1398 SEEVNSAVEAGDEIRRKLQRELDSAiqrerqkeeekerverqrERLREEIEDMTIALQRERQnctALEKRQKKFDQCLAE 1477
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDEL------------------SQELSDASRKIGEIEKEIE---QLEQEEEKLKERLEE 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1478 EKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERanKQLRLEMEQLVNQQDDVGKNVHELERTRRTLET 1557
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1558 EAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFErEISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSK 1637
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE-NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1638 KQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDEakvtrddvISQSKDSEKKIQTLEAEVLHLTEELAVS 1717
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE--------DEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 2414917124 1718 ERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVN 1757
Cdd:TIGR02169 971 EPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIE 1010
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1115-1722 |
1.83e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.78 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1115 GRLEEEGARRTEAQRSLREALSQVSELKEEVENERgmrerAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAEL 1194
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQI-----EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETR 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1195 SELQRCVEEetrrHETQLSELRVKhSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKR 1274
Cdd:PRK02224 237 DEADEVLEE----HEERREELETL-EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1275 ADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALAS 1354
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1355 RVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGdeirrklQRELDSAIQRERQKEEEKE 1434
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA-------EALLEAGKCPECGQPVEGS 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1435 RVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSaRLAEERDRAEADSREKETRCLALSRALQEAQ 1514
Cdd:PRK02224 465 PHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE-RLEERREDLEELIAERRETIEEKRERAEELR 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1515 DQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERTRRTLETEAQNLRiqtqeleeelseaensRLRlevTLQALKAQF 1594
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE----------------RIR---TLLAAIADA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1595 EREIstneEKGEEKRRALSKQVRELEIQLEEersqrsqSVSSKKQLEAELQeaEAQVETANRGKEEAMKQLRRLQGQmke 1674
Cdd:PRK02224 605 EDEI----ERLREKREALAELNDERRERLAE-------KRERKRELEAEFD--EARIEEAREDKERAEEYLEQVEEK--- 668
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2414917124 1675 vLRELDEAkvtRDDVISQSKDSEKKIQTLEAevlhLTEEL-AVSERQKR 1722
Cdd:PRK02224 669 -LDELREE---RDDLQAEIGAVENELEELEE----LRERReALENRVEA 709
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
860-1707 |
3.59e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 78.47 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 860 KPLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEEKAVLAdQLQAEAELFAEAEEMRARLASRKQELE 939
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL-YLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 940 EVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEK 1019
Cdd:pfam02463 255 SSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1020 KQLEERLNEVTDQ-------LTEEEEKTKSLNKLKNKQEAVIA---DLEERLKREEQGRLEQEKFKRRMESEAMEAQEQL 1089
Cdd:pfam02463 335 EEIEELEKELKELeikreaeEEEEEELEKLQEKLEQLEEELLAkkkLESERLSSAAKLKEEELELKSEEEKEAQLLLELA 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1090 SDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEA---QRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEEL 1166
Cdd:pfam02463 415 RQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEElekQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1167 EALRTELEDTLDSTAAQQELRSRREAELSELQrcVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKAT 1246
Cdd:pfam02463 495 LEERSQKESKARSGLKVLLALIKDGVGGRIIS--AHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1247 LEEERQNLTSELKSLQASRS-----ESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKS 1321
Cdd:pfam02463 573 LPLGARKLRLLIPKLKLPLKsiavlEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGV 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1322 LRLAKEissLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTEL---RKQS 1398
Cdd:pfam02463 653 SLEEGL---AEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELladRVQE 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1399 EEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEE 1478
Cdd:pfam02463 730 AQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEE 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1479 KAVSARLAEERDRAEADSrEKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQddvgknvhELERTRRTLETE 1558
Cdd:pfam02463 810 LKEEAELLEEEQLLIEQE-EKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL--------LQELLLKEEELE 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1559 AQNLRIQTQELEEELSEAENSRLRLEVTLQALkaqfEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKK 1638
Cdd:pfam02463 881 EQKLKDELESKEEKEKEEKKELEEESQKLNLL----EEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE 956
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2414917124 1639 QLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDEAKVTRDDVI--SQSKDSEKKIQTLEAEV 1707
Cdd:pfam02463 957 EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIraIIEETCQRLKEFLELFV 1027
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
982-1563 |
6.15e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.80 E-value: 6.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 982 SARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIAdLEERL 1061
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-LKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1062 KREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSDLRgslaQKEKEITSLQGrLEEEGARRTEAQRSLREALSQVSEL 1141
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE----EKVKELKELKE-KAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1142 KEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQElrsrrEAELSELQRCVEEETRRHETQLSELrvkhsa 1221
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-----RHELYEEAKAKKEELERLKKRLTGL------ 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1222 aldslqeQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSEsergRKRADNQLQELSAR--LAQADREREDREER 1299
Cdd:PRK03918 385 -------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE----LKKAIEELKKAKGKcpVCGRELTEEHRKEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1300 MHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESrqkmaLASRVRALEEEKNGLMERLEEEEERGKE 1379
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE-----LAEQLKELEEKLKKYNLEELEKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1380 LSRQ-----------IQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELD----SAIQRERQKEEEKERVERQRERLR 1444
Cdd:PRK03918 529 KLKEkliklkgeiksLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfESVEELEERLKELEPFYNEYLELK 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1445 EEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAE-ERDRAEADSREKETRCLALSRALQEAQDQKEELERA 1523
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElEKKYSEEEYEELREEYLELSRELAGLRAELEELEKR 688
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2414917124 1524 NKQLRLEMEQLVNQQDDVGKNVHELERTRRTLEtEAQNLR 1563
Cdd:PRK03918 689 REEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELR 727
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
958-1261 |
6.36e-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: 77.80 E-value: 6.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 958 QLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEE 1037
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1038 EKTKSLNKLKNKQEAVIADLEERLKREEQgRLEQEKFKrrmeseamEAQEQLSDLGMLSSDLRGSLAQKEKEITSLQGRL 1117
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEA-RLSHSRIP--------EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1118 EEEGARRTEAQRSLREALSQVSELKEEVENERGmreraekQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSEL 1197
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG-------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2414917124 1198 QRCVEE---ETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKA--TLEEERQNLTSELKSL 1261
Cdd:TIGR02169 902 ERKIEEleaQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRAL 970
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1465-1943 |
6.69e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.79 E-value: 6.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1465 EKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANkQLRLEMEQLVNQQDDVGKN 1544
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKKK 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1545 VHELERTRRTLETEAqnlriqtqeleeelseaensrlrlEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLE 1624
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEA------------------------EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA 1393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1625 EERSQRSQSVSSKKQleaELQEAEAQVETANRGKEEAMKQLRRLQGQMK-EVLRELDEAKVTRDDVISQSKDSEKKIQTL 1703
Cdd:PTZ00121 1394 DEAKKKAEEDKKKAD---ELKKAAAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1704 EAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEDLEEEQTNNELLTERLRKTALQ 1783
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1784 VETLTVQLQGERTlaQKAEAAREQLEKQNKELkaRLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMR 1863
Cdd:PTZ00121 1551 LKKAEELKKAEEK--KKAEEAKKAEEDKNMAL--RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1864 KTE---KKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVE---EENSRSSAQKRK----LQRELEELTDSSQ 1933
Cdd:PTZ00121 1627 KAEeekKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKkkaEEAKKAEEDEKKaaeaLKKEAEEAKKAEE 1706
|
490
....*....|
gi 2414917124 1934 TMNREISSLR 1943
Cdd:PTZ00121 1707 LKKKEAEEKK 1716
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1106-1938 |
4.51e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.10 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1106 KEKEITSLQGRLEEEgARRTEAQRSlrEALSQVSELKEEVENERGMRE--RAEKQRRdlseELEALRTELEDTLDSTAAQ 1183
Cdd:PTZ00121 1088 RADEATEEAFGKAEE-AKKTETGKA--EEARKAEEAKKKAEDARKAEEarKAEDARK----AEEARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1184 QELRSRREAELSELQRCVEEETRRHET-QLSELRVKHSAALDSLQEQLDNSKRArqslEKAKATLEEERqnlTSELKSLQ 1262
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVrKAEELRKAEDARKAEAARKAEEERKA----EEARKAEDAKK---AEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1263 ASRSESERGRKRADNQLQELSARLAQADREREDREERMHKlqceieslsgnlsssdSKSLRLAKEISSLEsQLHDARELL 1342
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK----------------AEEARKADELKKAE-EKKKADEAK 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1343 QDESRQKMALASRvRALEEEKnglmerleeeeerGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSA 1422
Cdd:PTZ00121 1297 KAEEKKKADEAKK-KAEEAKK-------------ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1423 iqrerqkeeekerverqrerlreeiedmtialqRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETR 1502
Cdd:PTZ00121 1363 ---------------------------------EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE 1409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1503 CLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERTRRTLETEAQNLRIQTQELEEELSEAENSRLR 1582
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1583 LEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEam 1662
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE-- 1567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1663 kQLRRLQGQMKEVLRELDEAKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIademvssSSGK 1742
Cdd:PTZ00121 1568 -EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV-------EQLK 1639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1743 NVLSEEKRRldarvnqleedleeeqtnnellTERLRKTALQVETLTVQL-QGERTLAQKAEAAREQLEKQNKELKARLGE 1821
Cdd:PTZ00121 1640 KKEAEEKKK----------------------AEELKKAEEENKIKAAEEaKKAEEDKKKAEEAKKAEEDEKKAAEALKKE 1697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1822 MEGAvrgkhrmsvaaleakietmeeqleqerqeraianklmrkteKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLK 1901
Cdd:PTZ00121 1698 AEEA-----------------------------------------KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 2414917124 1902 RQLEEVE---EENSRSSAQKRKLQRELEELTDSSQTMNRE 1938
Cdd:PTZ00121 1737 KEAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1076-1266 |
7.19e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.10 E-value: 7.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1076 RRMESEAMEAQEQLSDLGMLSsDLRGSLAQKEKEITSLqgRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERA 1155
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIR-ELAERYAAARERLAEL--EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1156 EKQRRDLSEELEALR-----------TELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALD 1224
Cdd:COG4913 315 EARLDALREELDELEaqirgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2414917124 1225 SLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRS 1266
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
864-1422 |
8.40e-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: 70.97 E-value: 8.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 864 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEAELfaeaeemRARLASRKQELEEVLG 943
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEA-------KRNVERQLSTLQAQLS 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 944 ELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDL------------------ 1005
Cdd:pfam01576 528 DMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLdhqrqlvsnlekkqkkfd 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1006 ----------ATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFK 1075
Cdd:pfam01576 608 qmlaeekaisARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSK 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1076 RRMESEAMEAQEQLSDLG-----------MLSSDLRGSLAQKEKEitsLQGRLEEEGARRteaqrslREALSQVSELKEE 1144
Cdd:pfam01576 688 RALEQQVEEMKTQLEELEdelqatedaklRLEVNMQALKAQFERD---LQARDEQGEEKR-------RQLVKQVRELEAE 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1145 VENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQL-----SELRVKH 1219
Cdd:pfam01576 758 LEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILaqskeSEKKLKN 837
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1220 -SAALDSLQEQLDNSKRARQslekakaTLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREE 1298
Cdd:pfam01576 838 lEAELLQLQEDLAASERARR-------QAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLND 910
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1299 RMHKLQCEIESLSGNLSSSDSKS------------------LRLAKE-----------ISSLESQLHDARELLQDESRQK 1349
Cdd:pfam01576 911 RLRKSTLQVEQLTTELAAERSTSqksesarqqlerqnkelkAKLQEMegtvkskfkssIAALEAKIAQLEEQLEQESRER 990
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2414917124 1350 MALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSA 1422
Cdd:pfam01576 991 QAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDA 1063
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
928-1254 |
1.66e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.71 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 928 RARLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLAt 1007
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE- 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1008 avEQRERLGKEKKQLEERLNEVTDQLTEE-EEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQ 1086
Cdd:TIGR02169 769 --ELEEDLHKLEEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1087 EQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEEL 1166
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1167 EALRTELEDTLDSTAAQQELrsrREAELSElqRCVEEETRRHETQLSELRVKHSAALdslqEQLDNSKRARQSLEKAKAT 1246
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEI---PEEELSL--EDVQAELQRVEEEIRALEPVNMLAI----QEYEEVLKRLDELKEKRAK 997
|
....*...
gi 2414917124 1247 LEEERQNL 1254
Cdd:TIGR02169 998 LEEERKAI 1005
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
995-1679 |
1.90e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.71 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 995 ETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVT---DQLTEE-EEKTKSLNKLKNKQEAVIADLEERLKREEQGRLE 1070
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkrrDKLTEEyAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1071 QEKFKRRMES---EAMEAQEQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVEN 1147
Cdd:TIGR02169 394 LEKLKREINElkrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1148 ERGMRERAEKQRRDLSEELEALRTEL----EDTLDSTAAQQELRSRRE------AELSEL-------------------- 1197
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQAraseERVRGGRAVEEVLKASIQgvhgtvAQLGSVgeryataievaagnrlnnvv 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1198 -------QRCVEEETRRHETQ-----LSELRVKHS--------AALDSLQEQLDNSKRAR-------------QSLEKAK 1244
Cdd:TIGR02169 554 veddavaKEAIELLKRRKAGRatflpLNKMRDERRdlsilsedGVIGFAVDLVEFDPKYEpafkyvfgdtlvvEDIEAAR 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1245 ATLEEERQ-NLTSELKSLQASRSESERGRKRADNQLQELSARLAQadreredreermhkLQCEIESLSGNLSSsdskslr 1323
Cdd:TIGR02169 634 RLMGKYRMvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQR--------------LRERLEGLKRELSS------- 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1324 LAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNglmerleEEEERGKELSRQIQTHSQQLTELRKQSEEVNS 1403
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE-------KLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1404 AVEAGDEIRRKLQRELDSaiqrerqkeEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDqcLAEEKAVSA 1483
Cdd:TIGR02169 766 RIEELEEDLHKLEEALND---------LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT--LEKEYLEKE 834
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1484 RLAEERDRAEADSREKETRclalsRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERTRRTLETEAQNLR 1563
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIE-----KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1564 IQTQELEEELSeaensrlRLEVTLQALK---AQFEREISTNEE---------KGEEKRRALSKQVRELE------IQLEE 1625
Cdd:TIGR02169 910 AQIEKKRKRLS-------ELKAKLEALEeelSEIEDPKGEDEEipeeelsleDVQAELQRVEEEIRALEpvnmlaIQEYE 982
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 2414917124 1626 ERSQRSQSVSSKKQ-LEAELQEAEAQVETANRGKEEA-MKQLRRLQGQMKEVLREL 1679
Cdd:TIGR02169 983 EVLKRLDELKEKRAkLEEERKAILERIEEYEKKKREVfMEAFEAINENFNEIFAEL 1038
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
982-1750 |
2.45e-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: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 982 SARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEErlnevtdqltEEEEKTKSLNKLKNKQEaviadleerl 1061
Cdd:TIGR00618 191 SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE----------ALQQTQQSHAYLTQKRE---------- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1062 KREEQGRLEQEKFKRRMESEAMEAQEQlsdlgmlssdlRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSEL 1141
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELRAQEA-----------VLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1142 KEEVENERGMRERAEKQRRDLSEELEALRT---ELEDTLDSTAAQQELRSRREAELSELQRCVE-EETRRHETQLSELRV 1217
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsQEIHIRDAHEVATSIREISCQQHTLTQHIHTlQQQKTTLTQKLQSLC 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1218 KHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQnLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDRE 1297
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE-LQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1298 ERMHKLQCEIESLSGNLSSSDSKSLRLAKeisslESQLHDARELLQdeSRQKMALASRVRALEEEKNGLMERLEEEEERG 1377
Cdd:TIGR00618 479 EQIHLQETRKKAVVLARLLELQEEPCPLC-----GSCIHPNPARQD--IDNPGPLTRRMQRGEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1378 KELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSaIQRERQKEEEKERVERQRERLREEIEDMTIALQRE 1457
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR-LQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDV 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1458 RQNctalekrQKKFDQCLAEEKAVSARLAEERdraeadSREKETRCLALSRalqeaQDQKEELERanKQLRLEMEQlvnq 1537
Cdd:TIGR00618 631 RLH-------LQQCSQELALKLTALHALQLTL------TQERVREHALSIR-----VLPKELLAS--RQLALQKMQ---- 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1538 qddvgknvHELERTRRTLETEAQnlrIQTQELEEELSEAENSRLRLEVTLQALKAQfeREISTNEEKGEEKRRALSKQVR 1617
Cdd:TIGR00618 687 --------SEKEQLTYWKEMLAQ---CQTLLRELETHIEEYDREFNEIENASSSLG--SDLAAREDALNQSLKELMHQAR 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1618 ELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDEAKVTRDDVISQSKDS- 1696
Cdd:TIGR00618 754 TVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQf 833
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 2414917124 1697 ----EKKIQTLeAEVLHLTEELAVSERQKRQAQQERDEIAdEMVSSSSGKNVLSEEKR 1750
Cdd:TIGR00618 834 lsrlEEKSATL-GEITHQLLKYEECSKQLAQLTQEQAKII-QLSDKLNGINQIKIQFD 889
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
924-1731 |
2.64e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 924 AEEMRARLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQ--DLEEQLEEEESARQRLLLEKVTLETKVKSL 1001
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkaEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1002 ETDLATAVEQRERLGK--EKKQLEERlnEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRME 1079
Cdd:PTZ00121 1276 EARKADELKKAEEKKKadEAKKAEEK--KKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1080 SEAMEAQEqlsdlgmlssdlrgslAQKEKEITSLQgrlEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQR 1159
Cdd:PTZ00121 1354 AAADEAEA----------------AEEKAEAAEKK---KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1160 RDlSEELEALRTELEDTLDSTAAQQELRSRREAElsELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQS 1239
Cdd:PTZ00121 1415 AA-KKKADEAKKKAEEKKKADEAKKKAEEAKKAD--EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1240 LEKAKATLEEERQNLTSELKSLQASRSESergRKRADNQLQELSARLAQADREREDREErmhklqceieslsgnlsssdS 1319
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEE---AKKADEAKKAEEAKKADEAKKAEEKKK--------------------A 1548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1320 KSLRLAKEISSLEsQLHDARELLQDESRQKMAL--ASRVRALEEEK-NGLMERLEEEEERGKELSRQIQTHSQQLTELRK 1396
Cdd:PTZ00121 1549 DELKKAEELKKAE-EKKKAEEAKKAEEDKNMALrkAEEAKKAEEARiEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1397 QsEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQclA 1476
Cdd:PTZ00121 1628 A-EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK--A 1704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1477 EEkaVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKqlrlemeqlvnqqDDVGKNvhELERTRRTLE 1556
Cdd:PTZ00121 1705 EE--LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK-------------DEEEKK--KIAHLKKEEE 1767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1557 TEAQNLRIQTQELEEELSEAENSRLRLEV--TLQALKAQFEreistNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSV 1634
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVdkKIKDIFDNFA-----NIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQ 1842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1635 SSKKQlEAELQEAEAQVETANRGKEEA--MKQLRRLQGQMKEVLRELDEAKVTRDDVISQSKDSEKKIQTLEAevlhLTE 1712
Cdd:PTZ00121 1843 LEEAD-AFEKHKFNKNNENGEDGNKEAdfNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDI----IDD 1917
|
810
....*....|....*....
gi 2414917124 1713 ELAVSERQKRQAQQERDEI 1731
Cdd:PTZ00121 1918 KLDKDEYIKRDAEETREEI 1936
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1193-1942 |
3.28e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 68.99 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1193 ELSELQRCVEEETRRHETQLSELR---VKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELkslQASRSESE 1269
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRqsvIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHEL---EAAKCLKE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1270 RGRKRADNQLQEL-------SARLAQADREREDREERMHKLQCEIESLSG----NLSSSDSKSLR-LAKEISSLESQL-- 1335
Cdd:pfam15921 163 DMLEDSNTQIEQLrkmmlshEGVLQEIRSILVDFEEASGKKIYEHDSMSTmhfrSLGSAISKILReLDTEISYLKGRIfp 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1336 -HDARELLQDESRQKMAL-----ASRVRAL----EEEKNGLMERLEEEEERGKELSRQI-----QTHSQQLTELRKQSEE 1400
Cdd:pfam15921 243 vEDQLEALKSESQNKIELllqqhQDRIEQLisehEVEITGLTEKASSARSQANSIQSQLeiiqeQARNQNSMYMRQLSDL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1401 VNSAVEAGDEIRrKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTA-LEKRQKKfdqcLAEEK 1479
Cdd:pfam15921 323 ESTVSQLRSELR-EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAdLHKREKE----LSLEK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1480 AVSARLAEeRD----------RAEADSREKETRCL-ALSRALQ-EAQDQKEELERA--NKQLRLE-----MEQLVNQQDD 1540
Cdd:pfam15921 398 EQNKRLWD-RDtgnsitidhlRRELDDRNMEVQRLeALLKAMKsECQGQMERQMAAiqGKNESLEkvsslTAQLESTKEM 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1541 VGKNVHELERTRRTLETEAQNLR-----IQTQELEEELSEAENSRLRLEVTLQALKAQFEReistNEEkgeEKRRALSKQ 1615
Cdd:pfam15921 477 LRKVVEELTAKKMTLESSERTVSdltasLQEKERAIEATNAEITKLRSRVDLKLQELQHLK----NEG---DHLRNVQTE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1616 VRELEIQLEEERSQRSQSvssKKQLEAELQEAEAQVETANRGKEEAMKqlrrLQGQMKEVLRELDEAKVTRDDVISQSKD 1695
Cdd:pfam15921 550 CEALKLQMAEKDKVIEIL---RQQIENMTQLVGQHGRTAGAMQVEKAQ----LEKEINDRRLELQEFKILKDKKDAKIRE 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1696 SEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEKrrldarvnqleedleeeqtnnELLTE 1775
Cdd:pfam15921 623 LEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDY---------------------EVLKR 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1776 RLRKTALQVETLTVQLQgertlaQKAEAAREQLEKQNKELKArlgeMEGAvrGKHRMSVAALEAKIETmeeqlEQERQER 1855
Cdd:pfam15921 682 NFRNKSEEMETTTNKLK------MQLKSAQSELEQTRNTLKS----MEGS--DGHAMKVAMGMQKQIT-----AKRGQID 744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1856 AIANKLmrkteKKLKEVMMQAEDERRHadqyreqldksmvrlkqLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTM 1935
Cdd:pfam15921 745 ALQSKI-----QFLEEAMTNANKEKHF-----------------LKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRL 802
|
....*..
gi 2414917124 1936 NREISSL 1942
Cdd:pfam15921 803 KEKVANM 809
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1639-1928 |
7.20e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1639 QLEAELQEAEAQVETANRGKEeAMKQLRRLQGQMKevLRELDEAKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSE 1718
Cdd:COG1196 197 ELERQLEPLERQAEKAERYRE-LKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1719 RQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEDLEEEQTNNELLTERLRKTALQVETLTVQLQGERTLA 1798
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1799 QKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKK------LKEV 1872
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELeeleeaLAEL 433
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2414917124 1873 MMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKLQRELEEL 1928
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
862-1365 |
1.31e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.60 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 862 LLQVTRQDEEIQTREAalqkaKEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEV 941
Cdd:PRK02224 189 LDQLKAQIEEKEEKDL-----HERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 942 LGELETRLEeeeergvqlanEKKKMQQNIQDLEEQLEEEESARQRlLLEKVTLEtkvkslETDLATAVEQRERLGKEKKQ 1021
Cdd:PRK02224 264 RETIAETER-----------EREELAEEVRDLRERLEELEEERDD-LLAEAGLD------DADAEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1022 LEERLNEVTDQLTEEEEKTKSLNKlknkqeaVIADLEERL--KREEQGRLeqekfkrrmESEAMEAQEQLsdlgmlsSDL 1099
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLRE-------DADDLEERAeeLREEAAEL---------ESELEEAREAV-------EDR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1100 RGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALR-----TELE 1174
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1175 DT--LDSTAAQQELRSRREAELSELQRCVEEETRRHEtQLSELrVKHSAALDSLQEQLDNSKrarQSLEKAKATLEEERQ 1252
Cdd:PRK02224 463 GSphVETIEEDRERVEELEAELEDLEEEVEEVEERLE-RAEDL-VEAEDRIERLEERREDLE---ELIAERRETIEEKRE 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1253 NLTSELKSLQASRSESERGRKRAdnqlQELSARLAQADREREDREERMHKLQCEIESLsGNLSSSDSKSLRLAKEISSLE 1332
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAA----AEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLR 612
|
490 500 510
....*....|....*....|....*....|....
gi 2414917124 1333 SQLHDARElLQDESRQKMA-LASRVRALEEEKNG 1365
Cdd:PRK02224 613 EKREALAE-LNDERRERLAeKRERKRELEAEFDE 645
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1097-1323 |
1.38e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.56 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1097 SDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDT 1176
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1177 LDSTAAQ---QELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQN 1253
Cdd:COG4942 103 KEELAELlraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1254 LTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLR 1323
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
870-1276 |
1.43e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.60 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 870 EEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEaelfaeaeemRARLASRKQELEEVLGELETRL 949
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA----------REAVEDRREEIEELEEEIEELR 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 950 EEEEERGVQLANekkkmqqniqdleeqleeEESARQRLLLEKVTLETKVKSLETDLATAveqRERLGKEKKQLEERLNEV 1029
Cdd:PRK02224 398 ERFGDAPVDLGN------------------AEDFLEELREERDELREREAELEATLRTA---RERVEEAEALLEAGKCPE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1030 TDQLTEEEEKTKSLNKLKNKqeavIADLEERLkreEQGRLEQEKFKRRMES--EAMEAQEQLSDLGMLSSDLRGSLAQKE 1107
Cdd:PRK02224 457 CGQPVEGSPHVETIEEDRER----VEELEAEL---EDLEEEVEEVEERLERaeDLVEAEDRIERLEERREDLEELIAERR 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1108 KEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEAL---RTELEDTLDSTAAQQ 1184
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLeriRTLLAAIADAEDEIE 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1185 ELRSRREAeLSELQRCVEEETRRHETQLSELRVKH-SAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQA 1263
Cdd:PRK02224 610 RLREKREA-LAELNDERRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
410
....*....|...
gi 2414917124 1264 SRSESERGRKRAD 1276
Cdd:PRK02224 689 ELEELEELRERRE 701
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
41-86 |
1.44e-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: 1.44e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2414917124 41 AAKRLVWVPSEKQGFESASIREERGDEVEVElTDSQRRVTLSREEV 86
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVE-TEDGKTVTVKKDDV 45
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
864-1266 |
1.71e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 864 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEEKA----VLADQLQAEAELFAEAEEMR----ARLA--- 932
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAeeakKKADEAKKAAEAKKKADEAKkaeeAKKAdea 1527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 933 -----SRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLAT 1007
Cdd:PTZ00121 1528 kkaeeAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1008 AVEQrerlgkEKKQLEERLNevTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQE 1087
Cdd:PTZ00121 1608 KAEE------AKKAEEAKIK--AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1088 qlsdlgmlssdLRGSLAQKEKEITSLQgRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELE 1167
Cdd:PTZ00121 1680 -----------AKKAEEDEKKAAEALK-KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1168 ALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKhsaaldSLQEQLDNSKRARQSLEKAKATL 1247
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK------KIKDIFDNFANIIEGGKEGNLVI 1821
|
410
....*....|....*....
gi 2414917124 1248 EEERQNLTSELKSLQASRS 1266
Cdd:PTZ00121 1822 NDSKEMEDSAIKEVADSKN 1840
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1514-1947 |
2.15e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.81 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1514 QDQKEELERANKQLRLEMEQLvnqQDDVGKNVHELERTRRTLE-TEAQNLRIQTQELEEELSEAENSRL--RLEVTLQAL 1590
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKK---QQEINEKTTEISNTQTQLNqLKDEQNKIKKQLSEKQKELEQNNKKikELEKQLNQL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1591 KAQFEreiSTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQG 1670
Cdd:TIGR04523 294 KSEIS---DLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1671 QMKEVLRELDEAKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEKR 1750
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1751 RLDARVNQLEEDLEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAVR--- 1827
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEkle 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1828 ---GKHRMSVAALEAKIETMEEQLEQERQERAI------------ANKLMRKTEKKLKEVMMQAEDERrhaDQYREQLDK 1892
Cdd:TIGR04523 531 sekKEKESKISDLEDELNKDDFELKKENLEKEIdeknkeieelkqTQKSLKKKQEEKQELIDQKEKEK---KDLIKEIEE 607
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2414917124 1893 SMVRLKQLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLS 1947
Cdd:TIGR04523 608 KEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWP 662
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
867-1416 |
2.76e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 867 RQDEEIQTREAAlqKAKEQLTRAEQDYTELDKKHAQLL---------EEKAVLADQLQAEAELFAEAEEMRARLASR--- 934
Cdd:PTZ00121 1194 RKAEDARKAEAA--RKAEEERKAEEARKAEDAKKAEAVkkaeeakkdAEEAKKAEEERNNEEIRKFEEARMAHFARRqaa 1271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 935 -KQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRE 1013
Cdd:PTZ00121 1272 iKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1014 RLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLG 1093
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK 1431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1094 mlSSDLRGSLAQKEKEITSLQGRLEE-----------EGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDL 1162
Cdd:PTZ00121 1432 --KADEAKKKAEEAKKADEAKKKAEEakkaeeakkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1163 SEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEK 1242
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1243 AKATLEEERQNLTSE--LKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESL---SGNLSSS 1317
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEkkMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENkikAAEEAKK 1669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1318 DSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNG---LMERLEEEEERGKELSRQIQTHSQQLTEL 1394
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
570 580
....*....|....*....|..
gi 2414917124 1395 RKQSEEVNSAVEAGDEIRRKLQ 1416
Cdd:PTZ00121 1750 KKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
957-1730 |
2.85e-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: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 957 VQLANEKKKMQQNIQDLEEQLEEEESARQRLLL--EKVTLETKVKSLET-DLATAVEQRERLGKEKKQLEERLNEVTDQL 1033
Cdd:pfam05483 95 VSIEAELKQKENKLQENRKIIEAQRKAIQELQFenEKVSLKLEEEIQENkDLIKENNATRHLCNLLKETCARSAEKTKKY 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1034 TEEEEKTKSLN-KLKNKQEAVIADLEERLKREEQGRLEQEkFKRRMESEAMEAQEQlsdlgmlssDLRGSLAQKEKEITS 1112
Cdd:pfam05483 175 EYEREETRQVYmDLNNNIEKMILAFEELRVQAENARLEMH-FKLKEDHEKIQHLEE---------EYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1113 LQGRLEEEGARRTEAQRSLREALSQVSELKEEVE-NERGMRERAEKQRRdLSEELEALRTELEDTLDSTAAQQElrsrre 1191
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLLEESRDKANQLEEKTKlQDENLKELIEKKDH-LTKELEDIKMSLQRSMSTQKALEE------ 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1192 aELSELQRCVEEETRRHETQLSELrvkhsaaldslqeqldNSKRARQSLekakatLEEERQNLTSELKSLQasRSESERG 1271
Cdd:pfam05483 318 -DLQIATKTICQLTEEKEAQMEEL----------------NKAKAAHSF------VVTEFEATTCSLEELL--RTEQQRL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1272 RKRADnQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSsdskslrlakeisslesqlhdaRELLQDESRQKMA 1351
Cdd:pfam05483 373 EKNED-QLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE----------------------DEKLLDEKKQFEK 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1352 LASRVRALEEEKNGLMerleeeeergkelsrqiQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEE 1431
Cdd:pfam05483 430 IAEELKGKEQELIFLL-----------------QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1432 EKERVERQRERLREEIEDMTIALQRERQ---NCTALEKRQKKFDQCLaEEKAVSARLAEERDRAEADSREKETRClalsr 1508
Cdd:pfam05483 493 HCDKLLLENKELTQEASDMTLELKKHQEdiiNCKKQEERMLKQIENL-EEKEMNLRDELESVREEFIQKGDEVKC----- 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1509 ALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERTRRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQ 1588
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELA 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1589 ALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRL 1668
Cdd:pfam05483 647 SAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSE 726
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2414917124 1669 QGQMKEVLRELDEAKVTRddvisqskdsEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDE 1730
Cdd:pfam05483 727 LGLYKNKEQEQSSAKAAL----------EIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1015-1359 |
4.45e-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: 63.93 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1015 LGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEerlkreeqgrleQEKfKRRMESEAMEAQEQLSdlgm 1094
Cdd:pfam19220 1 IGQRNELLRVRLGEMADRLEDLRSLKADFSQLIEPIEAILRELP------------QAK-SRLLELEALLAQERAA---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1095 lSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQ-------RRDLSEELE 1167
Cdd:pfam19220 64 -YGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQlaaeteqNRALEEENK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1168 ALRTEL----EDTLDSTAAQQELRSRR---EAELSELQRCVEE---ETRRHETQLSEL---RVKHSAALDSLQEQLDNSK 1234
Cdd:pfam19220 143 ALREEAqaaeKALQRAEGELATARERLallEQENRRLQALSEEqaaELAELTRRLAELetqLDATRARLRALEGQLAAEQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1235 RARQsleKAKATLEEERQNLTSELKSLqasrsesergrkraDNQLQELSARLAQADREREDREERMHKLQCEIESLSGNL 1314
Cdd:pfam19220 223 AERE---RAEAQLEEAVEAHRAERASL--------------RMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRL 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2414917124 1315 SSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRAL 1359
Cdd:pfam19220 286 KEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEML 330
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1483-1947 |
8.26e-10 |
|
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: 64.43 E-value: 8.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1483 ARLAEERDRAEADSREKETrclaLSRALQEAQDQKEELERANKQLRLE----------MEQLVNQQDDVGKnvhELERTR 1552
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKK----MQQHIQDLEEQLDEEEAARQKLQLEkvtteakikkLEEDILLLEDQNS---KLSKER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1553 RTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKgEEKRRALSKQVRELEIQLEEERSQRSQ 1632
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQEL-EKAKRKLEGESTDLQEQIAELQAQIAE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1633 SVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDEAKVTRDDVISQSKDSEKKIQTLEAEVLHLTE 1712
Cdd:pfam01576 234 LRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1713 ELAVSERQKRQAQQERDEIademvssssgKNVLSEEKRRLDARVNQLEEDLEEEQtnnELLTERL----------RKTAL 1782
Cdd:pfam01576 314 TTAAQQELRSKREQEVTEL----------KKALEEETRSHEAQLQEMRQKHTQAL---EELTEQLeqakrnkanlEKAKQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1783 QVETLTVQLQGE-RTLAQ---KAEAAREQLEKQNKELKARLGEMEgAVRGKHRMSVAALEAKIETMEEQLEQERQERAIA 1858
Cdd:pfam01576 381 ALESENAELQAElRTLQQakqDSEHKRKKLEGQLQELQARLSESE-RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1859 NKLMRKTEKKLKEVMMQAEDERRHADQYREQLdksmvrlkqlkRQLEEveeensrssaQKRKLQRELEELTDSSQTMNRE 1938
Cdd:pfam01576 460 SKDVSSLESQLQDTQELLQEETRQKLNLSTRL-----------RQLED----------ERNSLQEQLEEEEEAKRNVERQ 518
|
....*....
gi 2414917124 1939 ISSLRNQLS 1947
Cdd:pfam01576 519 LSTLQAQLS 527
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
983-1423 |
1.16e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 983 ARQRLLLEKVTLETKvkslETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKtksLNKLKNKQEAVIADLEERLK 1062
Cdd:COG4913 272 AELEYLRAALRLWFA----QRRLELLEAELEELRAELARLEAELERLEARLDALREE---LDELEAQIRGNGGDRLEQLE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1063 REEQgRLEQEKfkRRMESEAMEAQEQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELK 1142
Cdd:COG4913 345 REIE-RLEREL--EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1143 EEVENERgmrERAEKQRRDLSEELEALRTELEDTLDST----------------------AAQQELRSRR------EAEL 1194
Cdd:COG4913 422 RELEAEI---ASLERRKSNIPARLLALRDALAEALGLDeaelpfvgelievrpeeerwrgAIERVLGGFAltllvpPEHY 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1195 SELQRCVEE------------ETRRHETQLS---------ELRVKHSAALDSLQ---------------EQLDNSKRA-- 1236
Cdd:COG4913 499 AAALRWVNRlhlrgrlvyervRTGLPDPERPrldpdslagKLDFKPHPFRAWLEaelgrrfdyvcvdspEELRRHPRAit 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1237 RQSLEKAKATL-------------------EEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADRERedre 1297
Cdd:COG4913 579 RAGQVKGNGTRhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA---- 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1298 ermhklqceieslsgNLSSSDSKSLRLAKEISSLESQLhdarELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERG 1377
Cdd:COG4913 655 ---------------EYSWDEIDVASAEREIAELEAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEI 715
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1378 KELSRQIQTHSQQLTELRKQSEEVNSAV--------------EAGDEIRRKLQRELDSAI 1423
Cdd:COG4913 716 GRLEKELEQAEEELDELQDRLEAAEDLArlelralleerfaaALGDAVERELRENLEERI 775
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
864-1275 |
1.20e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 864 QVTRQDEEIQTREAalqKAKEQLTRAEQDYTELDKKHAQLLEEKA---VLADQLQAE-AELFAEAEEMRARLASRKQELE 939
Cdd:PTZ00121 1346 EAAKAEAEAAADEA---EAAEEKAEAAEKKKEEAKKKADAAKKKAeekKKADEAKKKaEEDKKKADELKKAAAAKKKADE 1422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 940 EVLGELETRLEEEEERGVQLAN---------EKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLET----DLA 1006
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKkadeakkkaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAkkkaDEA 1502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1007 TAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEA-VIADLEERLKREEQGRLEQEKFKRRMESEAMEA 1085
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK 1582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1086 QEQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRE-----------R 1154
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEelkkaeeenkiK 1662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1155 AEKQRRDLSEE---LEALRTELEDtlDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLD 1231
Cdd:PTZ00121 1663 AAEEAKKAEEDkkkAEEAKKAEED--EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2414917124 1232 NSKRARQSLEKakatlEEERQNLTSELKSLQASRSESERGRKRA 1275
Cdd:PTZ00121 1741 EDKKKAEEAKK-----DEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1032-1809 |
1.27e-09 |
|
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: 63.83 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1032 QLTEEEEK--TKSLNKLKNKQEAVIADLEeRLKREEQGR---LEQEKFKRRMESEAMEAQEQLSDLgmLSSDLRGSLAQK 1106
Cdd:TIGR00618 108 QLYLEQKKgrGRILAAKKSETEEVIHDLL-KLDYKTFTRvvlLPQGEFAQFLKAKSKEKKELLMNL--FPLDQYTQLALM 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1107 EKEIT-SLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQE 1185
Cdd:TIGR00618 185 EFAKKkSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1186 LRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQ-------LDNSKRARQSLEKAKATLEEERQNLTSEL 1258
Cdd:TIGR00618 265 LRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQaqrihteLQSKMRSRAKLLMKRAAHVKQQSSIEEQR 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1259 KSLQASRSESERGRKRADNQLqelsARLAQaDREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDA 1338
Cdd:TIGR00618 345 RLLQTLHSQEIHIRDAHEVAT----SIREI-SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1339 RELlqdesRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEvnsaveagdEIRRKLQRE 1418
Cdd:TIGR00618 420 RDL-----QGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ---------TKEQIHLQE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1419 LDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRErQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSRE 1498
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG-PLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQ 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1499 ketrclalsraLQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERTRRTLETEAQNLRIQTQELEEELSEAEN 1578
Cdd:TIGR00618 565 -----------MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1579 SRlRLEVTLQALKAQFEREIstnEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGK 1658
Cdd:TIGR00618 634 LQ-QCSQELALKLTALHALQ---LTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1659 EEAMKQLRRLQGQMKEVLRELDEAKVTRDDVISQskdSEKKIQTLEAEVL-HLTEELAVSERQKRQAQQERDEIAD---- 1733
Cdd:TIGR00618 710 ETHIEEYDREFNEIENASSSLGSDLAAREDALNQ---SLKELMHQARTVLkARTEAHFNNNEEVTAALQTGAELSHlaae 786
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1734 -------EMVSSSSGKNVLSEEKRRLDARVNQLEEDLEEEQTNNELLTERLR-KTALQVETLTVQLQGERTLAQKAEAAR 1805
Cdd:TIGR00618 787 iqffnrlREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEeKSATLGEITHQLLKYEECSKQLAQLTQ 866
|
....
gi 2414917124 1806 EQLE 1809
Cdd:TIGR00618 867 EQAK 870
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
983-1729 |
1.45e-09 |
|
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: 63.53 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 983 ARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAV------IAD 1056
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIehnlskIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1057 LEERLKREEQGRLEQEKFKRRMESEAME----AQEQLSD----------------------LGMLSSDLRgSLAQKEKEI 1110
Cdd:TIGR00606 267 LDNEIKALKSRKKQMEKDNSELELKMEKvfqgTDEQLNDlyhnhqrtvrekerelvdcqreLEKLNKERR-LLNQEKTEL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1111 TSLQGRLEEEGARRTEAQR---SLREALSQVSEL---KEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQ 1184
Cdd:TIGR00606 346 LVEQGRLQLQADRHQEHIRardSLIQSLATRLELdgfERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1185 ELRSRREAELSELQRCVEEETRRHETQLSELRVKHSaALDSLQEQLDNSKRARQSLEKAKATLEEERQN-----LTSELK 1259
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIK-ELQQLEGSSDRILELDQELRKAERELSKAEKNsltetLKKEVK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1260 SLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHK---------------------------LQCEIESLSG 1312
Cdd:TIGR00606 505 SLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKdeqirkiksrhsdeltsllgyfpnkkqLEDWLHSKSK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1313 NLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRV------RALEEEKNGLMERLEEEEERGKELSRQIQT 1386
Cdd:TIGR00606 585 EINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAV 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1387 HSQQLTELRKQSEEVNSAVEAGDEIRRKLQrELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNctALEK 1466
Cdd:TIGR00606 665 YSQFITQLTDENQSCCPVCQRVFQTEAELQ-EFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQS--IIDL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1467 RQKKFDQCLAEEKAVSARLAEERDRAEADSREKET---------RCLALSRALQEAQDQKEELERANKQLRLEMeqlvnQ 1537
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTimpeeesakVCLTDVTIMERFQMELKDVERKIAQQAAKL-----Q 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1538 QDDVGKNVHELERTRRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQfEREISTNEEKG---EEKRRALSK 1614
Cdd:TIGR00606 817 GSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE-KLQIGTNLQRRqqfEEQLVELST 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1615 QVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAM----KQLRRLQGQMKEVLRELDEAKvtrDDvi 1690
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVndikEKVKNIHGYMKDIENKIQDGK---DD-- 970
|
810 820 830
....*....|....*....|....*....|....*....
gi 2414917124 1691 sQSKDSEKKIQTLEAEvlhlteelaVSERQKRQAQQERD 1729
Cdd:TIGR00606 971 -YLKQKETELNTVNAQ---------LEECEKHQEKINED 999
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
870-1541 |
1.55e-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: 63.55 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 870 EEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGELETRL 949
Cdd:TIGR02169 294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 950 EEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQrerlgkeKKQLEERLNEV 1029
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK-------INELEEEKEDK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1030 TDQLTEEEEKTKSLNKLKNKQEAVIADLeerlkREEQGRLEQEKFKRRMESEAMEAQEQLSDLG---------MLSSDLR 1100
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYEQELYDL-----KEEYDRVEKELSKLQRELAEAEAQARASEERvrggraveeVLKASIQ 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1101 ---GSLAQ----KEKEITSLQ----GRL-----EEEG--------ARRTEAQRS-------LREALSQVSELKEE----- 1144
Cdd:TIGR02169 522 gvhGTVAQlgsvGERYATAIEvaagNRLnnvvvEDDAvakeaielLKRRKAGRAtflplnkMRDERRDLSILSEDgvigf 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1145 ----VENERGMRERAEKQRRD--LSEELEALRTELED----TLDS--------------TAAQQELRSRRE-AELSELQR 1199
Cdd:TIGR02169 602 avdlVEFDPKYEPAFKYVFGDtlVVEDIEAARRLMGKyrmvTLEGelfeksgamtggsrAPRGGILFSRSEpAELQRLRE 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1200 CVEEETRRHETQLSELRvKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQL 1279
Cdd:TIGR02169 682 RLEGLKRELSSLQSELR-RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1280 QELSARLAQadreredREERMHKLQCEIESLSGNLSSSDSKSLRlaKEISSLESQLHDARELLQDESRQKMALASRVRAL 1359
Cdd:TIGR02169 761 KELEARIEE-------LEEDLHKLEEALNDLEARLSHSRIPEIQ--AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1360 EEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQ 1439
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1440 RERLREEIEDMTIALQRERQNCTALEkRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLA-------LSRALQE 1512
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLaiqeyeeVLKRLDE 990
|
730 740
....*....|....*....|....*....
gi 2414917124 1513 AQDQKEELERANKQLRLEMEQLVNQQDDV 1541
Cdd:TIGR02169 991 LKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
821-1289 |
1.69e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 821 RKAFLKKQQQLSALRVMQRNCAAYLKLRNWQwwRLFTKVKPLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKH 900
Cdd:COG4913 241 HEALEDAREQIELLEPIRELAERYAAARERL--AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 901 AQLLEEKAVLADQL-----QAEAELFAEAEEMRARLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEE 975
Cdd:COG4913 319 DALREELDELEAQIrgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 976 QLEEEESARQRLLLEKVTLETKVKSLETDLAtAVEQR-----ERLGKEKKQLEERLNEVTD---------QLTEEEEK-- 1039
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIA-SLERRksnipARLLALRDALAEALGLDEAelpfvgeliEVRPEEERwr 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1040 ------------------------TKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGML 1095
Cdd:COG4913 478 gaiervlggfaltllvppehyaaaLRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAELGR 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1096 SSDLR-----GSLAQKEKEIT-----SLQGRLEEEGARRTEAQRSL--REALSQVSELKEEvenergmRERAEKQRRDLS 1163
Cdd:COG4913 558 RFDYVcvdspEELRRHPRAITragqvKGNGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAE-------LAELEEELAEAE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1164 EELEALRTELEDTLDSTAAQQELRSRREAELSELQrcVEEETRRHETQLSELRvKHSAALDSLQEQLDNSKRARQSLEKA 1243
Cdd:COG4913 631 ERLEALEAELDALQERREALQRLAEYSWDEIDVAS--AEREIAELEAELERLD-ASSDDLAALEEQLEELEAELEELEEE 707
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2414917124 1244 KATLEEERQNLTSELKSLQASRSESER-----GRKRADNQLQELSARLAQA 1289
Cdd:COG4913 708 LDELKGEIGRLEKELEQAEEELDELQDrleaaEDLARLELRALLEERFAAA 758
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1096-1674 |
3.95e-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: 61.69 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1096 SSDLRGSLAQKEKeiTSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRdlsEELEALRTELED 1175
Cdd:pfam07111 52 SLELEGSQALSQQ--AELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQ---AEAEGLRAALAG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1176 tldSTAAQQELRSRREAELSELQRCveeetrrHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEE----- 1250
Cdd:pfam07111 127 ---AEMVRKNLEEGSQRELEEIQRL-------HQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQlaeaq 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1251 ------RQNLTSELKSLQASRSESERGRKRADNQL-------------QELSARLAQADREREDREERMHKLQCEIESLS 1311
Cdd:pfam07111 197 keaellRKQLSKTQEELEAQVTLVESLRKYVGEQVppevhsqtwelerQELLDTMQHLQEDRADLQATVELLQVRVQSLT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1312 GNLSSSDSKSLRLAKEISSLESQL-HDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKElsrQIQTHSQQ 1390
Cdd:pfam07111 277 HMLALQEEELTRKIQPSDSLEPEFpKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQE---QVTSQSQE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1391 LTELRKQSEEVNSAVEAGDEIRRKLQRELDSAiqrerqkeeeKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKK 1470
Cdd:pfam07111 354 QAILQRALQDKAAEVEVERMSAKGLQMELSRA----------QEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTR 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1471 FDQCLAEEKAVSARLAEERdRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQ------------- 1537
Cdd:pfam07111 424 VEQAVARIPSLSNRLSYAV-RKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREErnrldaelqlsah 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1538 --QDDVGKNVHELERTRRTLETEAQNLRiqtQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKR---RAL 1612
Cdd:pfam07111 503 liQQEVGRAREQGEAERQQLSEVAQQLE---QELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEiygQAL 579
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2414917124 1613 SKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKE 1674
Cdd:pfam07111 580 QEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARK 641
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1132-1701 |
9.95e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 9.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1132 REALSQVSELKEEVENERGMRERAEKQRR---------DLSEELEALRTELE------DTLDSTAAQQELR------SRR 1190
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqiellepirELAERYAAARERLAeleylrAALRLWFAQRRLElleaelEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1191 EAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESER 1270
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1271 G-----------RKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSL----RLAKEISSLESQL 1335
Cdd:COG4913 381 EfaalraeaaalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLalrdALAEALGLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1336 HDARELLQ---DESRQKMAL-----------------ASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLtelr 1395
Cdd:COG4913 461 PFVGELIEvrpEEERWRGAIervlggfaltllvppehYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSL---- 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1396 kqSEEVNSAV-EAGDEIRRKLQRELD--------------SAIQRERQKEEEKERVERQRERLREEI-------EDMTIA 1453
Cdd:COG4913 537 --AGKLDFKPhPFRAWLEAELGRRFDyvcvdspeelrrhpRAITRAGQVKGNGTRHEKDDRRRIRSRyvlgfdnRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1454 LQRERQNCTA-LEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRclALSRALQEAQDQKEELERAN---KQLRL 1529
Cdd:COG4913 615 LEAELAELEEeLAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA--SAEREIAELEAELERLDASSddlAALEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1530 EMEQLVNQQDDVGKNVHELERTRRTLETEAQnlRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREIStnEEKGEEKR 1609
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELE--QAEEELDELQDRLEAAEDLARLELRALLEERFAAALG--DAVERELR 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1610 RALSKQVRELEIQLEEERSQRSQSVSS-KKQLEAELQEAEAQVETAnrgkEEAMKQLRRLQG--------QMKEVLRELD 1680
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESL----PEYLALLDRLEEdglpeyeeRFKELLNENS 844
|
650 660
....*....|....*....|.
gi 2414917124 1681 EAKVTrdDVISQSKDSEKKIQ 1701
Cdd:COG4913 845 IEFVA--DLLSKLRRAIREIK 863
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
864-1406 |
1.11e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 864 QVTRQDEEIQTREAALQKAKEQLTRAEqdytELDKKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKqeleevlg 943
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAA----EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK-------- 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 944 eletrleeeeergvqlANEKKKMQQniqdleeqleeeesarqrllLEKVTLETKVKSLEtdLATAVEQRERLGKEKKQLE 1023
Cdd:PTZ00121 1387 ----------------AEEKKKADE--------------------AKKKAEEDKKKADE--LKKAAAAKKKADEAKKKAE 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1024 ERlnEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSDLRGSL 1103
Cdd:PTZ00121 1429 EK--KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1104 AQKEKeitSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQ 1183
Cdd:PTZ00121 1507 EAKKK---ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1184 QELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAAldslqEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQA 1263
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-----EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1264 SRSESERGRKRADNQLQElsARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQ 1343
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKK--AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2414917124 1344 DESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQltELRKQSEEVNSAVE 1406
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVD 1797
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
854-1417 |
1.33e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 854 RLFTKVKPLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLAS 933
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 934 RKQELEEVlgeletrleeeeergVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRE 1013
Cdd:PRK03918 274 EIEELEEK---------------VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1014 RLGKekkqLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAViadleERLKREEQGrLEQEKFKRRMES---EAMEAQEQLS 1090
Cdd:PRK03918 339 RLEE----LKKKLKELEKRLEELEERHELYEEAKAKKEEL-----ERLKKRLTG-LTPEKLEKELEElekAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1091 DLGMLSSDLRGSLAQKEKEITSLQ---------GRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRD 1161
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKkakgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1162 LSEELEALRteLEDTLDS-TAAQQELRSRREAELSElqrcVEEETRRHETQLSELRVKHSAALDSLqEQLDNSKRARQSL 1240
Cdd:PRK03918 489 LKKESELIK--LKELAEQlKELEEKLKKYNLEELEK----KAEEYEKLKEKLIKLKGEIKSLKKEL-EKLEELKKKLAEL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1241 EKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSK 1320
Cdd:PRK03918 562 EKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1321 SLRLAKEISSLESQLHDarELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQThsqqLTELRKQSEE 1400
Cdd:PRK03918 642 LEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE----REKAKKELEK 715
|
570
....*....|....*..
gi 2414917124 1401 VNSAVEAGDEIRRKLQR 1417
Cdd:PRK03918 716 LEKALERVEELREKVKK 732
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1056-1930 |
1.72e-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: 59.85 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1056 DLEERLKREEQGR-LEQEKFKRRMESEAMEAQ------EQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQ 1128
Cdd:pfam12128 213 PPKSRLNRQQVEHwIRDIQAIAGIMKIRPEFTklqqefNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1129 RSLREALSQV--------SELKEEVENERGMRERAEKQ-RRDLSEELEALRTELEDtLDSTAAQQELRSRREAELSELQR 1199
Cdd:pfam12128 293 RTLDDQWKEKrdelngelSAADAAVAKDRSELEALEDQhGAFLDADIETAAADQEQ-LPSWQSELENLEERLKALTGKHQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1200 CVEEETRRHETQLSElrvKHSAALDSLQEQLDNSKRARqslEKAKATLEEERQNLTSELKS-LQASRSESERGRKRADNQ 1278
Cdd:pfam12128 372 DVTAKYNRRRSKIKE---QNNRDIAGIKDKLAKIREAR---DRQLAVAEDDLQALESELREqLEAGKLEFNEEEYRLKSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1279 LQELSARLAQADREREDREERMHKlQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRA 1358
Cdd:pfam12128 446 LGELKLRLNQATATPELLLQLENF-DERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1359 LEEeknglmerleeeeergkelsrQIQTHSQQLTE-LRKQseevnsAVEAGDEIRRKLQRELdsaiqreRQKEEEKERVE 1437
Cdd:pfam12128 525 LEL---------------------QLFPQAGTLLHfLRKE------APDWEQSIGKVISPEL-------LHRTDLDPEVW 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1438 RQRERLREEIEDMTIALQRERQNctalekrqkkfdQCLAEEKAVSARLAeerdraeadsreketrclALSRALQEAQDQK 1517
Cdd:pfam12128 571 DGSVGGELNLYGVKLDLKRIDVP------------EWAASEEELRERLD------------------KAEEALQSAREKQ 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1518 EELErankqlrlemEQLVNQQDDVGKNVHELERTRRTLETEAQNLRiqtqeleeelseaensrlRLEVTLQALKAQFERE 1597
Cdd:pfam12128 621 AAAE----------EQLVQANGELEKASREETFARTALKNARLDLR------------------RLFDEKQSEKDKKNKA 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1598 ISTNEEKGEEKRRALSKQVRELEIQL--------EEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKqlRRLQ 1669
Cdd:pfam12128 673 LAERKDSANERLNSLEAQLKQLDKKHqawleeqkEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAK--AELK 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1670 GQMKEVLRELDEAKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEK 1749
Cdd:pfam12128 751 ALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQL 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1750 RRLDARVNQLeedleeeqtNNELLTERLRKTALQVEtLTVQLQGERTLAQKAeaAREQLEKQNKELKARLGEMEGAV--- 1826
Cdd:pfam12128 831 ARLIADTKLR---------RAKLEMERKASEKQQVR-LSENLRGLRCEMSKL--ATLKEDANSEQAQGSIGERLAQLedl 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1827 RGKHRMSVAALEAKIETMEEQLEQERQERAIANKL-MRKTEKKLKEVMMQAEDERRHAdQYREQLDKSMVR-----LKQL 1900
Cdd:pfam12128 899 KLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWEsLREEDHYQNDKGIRLLDYRKLV-PYLEQWFDVRVPqsimvLREQ 977
|
890 900 910
....*....|....*....|....*....|....*...
gi 2414917124 1901 KRQLEEVEEE--------NSRSSAQKRKLQRELEELTD 1930
Cdd:pfam12128 978 VSILGVDLTEfydvladfDRRIASFSRELQREVGEEAF 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
827-1170 |
2.06e-08 |
|
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: 59.69 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 827 KQQQLSALRVMQRNCAAYLKLRNWQWWRLFTKVKPL-LQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLE 905
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 906 EKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEqleeeESARQ 985
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE-----QIEEL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 986 RLLLEKVTLEtkVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLteeEEKTKSLNKLKNKQEAVIADLEERLKREE 1065
Cdd:TIGR02168 851 SEDIESLAAE--IEELEELIEELESELEALLNERASLEEALALLRSEL---EELSEELRELESKRSELRRELEELREKLA 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1066 QGRLEQEKFkrrmESEAMEAQEQLSDLGMLSSDLrgsLAQKEKEITSLQGRLEEEgarrteaQRSLREALSQVSELK--- 1142
Cdd:TIGR02168 926 QLELRLEGL----EVRIDNLQERLSEEYSLTLEE---AEALENKIEDDEEEARRR-------LKRLENKIKELGPVNlaa 991
|
330 340
....*....|....*....|....*....
gi 2414917124 1143 -EEVENERGMRERAEKQRRDLSEELEALR 1170
Cdd:TIGR02168 992 iEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
867-1285 |
4.68e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 867 RQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEaelfaeaeemRARLasrkqeleevlgele 946
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAA----------SDHL--------------- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 947 trleeeeergvQLANEKKKMQQNIQdleeqleeeesaRQRLLLEKvtLETKVKSLETDLATAVEQRERLGKEKKQLEERL 1026
Cdd:PRK04863 338 -----------NLVQTALRQQEKIE------------RYQADLEE--LEERLEEQNEVVEEADEQQEENEARAEAAEEEV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1027 NEVTDQLTE-----EEEKTKSLnklkNKQEAVIAdLEERLKREEQGRLEQEKFKRRMesEAMEAQEQLSDLGMLSSDLRG 1101
Cdd:PRK04863 393 DELKSQLADyqqalDVQQTRAI----QYQQAVQA-LERAKQLCGLPDLTADNAEDWL--EEFQAKEQEATEELLSLEQKL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1102 SLAQKEKE--------ITSLQGRLEeegarRTEAQRSLREALSQVSELKEEVENERGMR------ERAEKQRRDLSEELE 1167
Cdd:PRK04863 466 SVAQAAHSqfeqayqlVRKIAGEVS-----RSEAWDVARELLRRLREQRHLAEQLQQLRmrlselEQRLRQQQRAERLLA 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1168 ALRTELEDTLDSTAAQQELRSRREAELSELQRCVEE------ETRRHETQLSELRVKHSA----------ALDSLQEQLD 1231
Cdd:PRK04863 541 EFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEarerrmALRQQLEQLQARIQRLAArapawlaaqdALARLREQSG 620
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 1232 NSKRARQSlekakatLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSAR 1285
Cdd:PRK04863 621 EEFEDSQD-------VTEYMQQLLERERELTVERDELAARKQALDEEIERLSQP 667
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1050-1560 |
6.44e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1050 QEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLsdlgmlssdlRGSLAQKEKEITSLQGRLEEEGARRTEAQR 1129
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEE----------LKEAEEKEEEYAELQEELEELEEELEELEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1130 SLREALSQVSELKEEVENERGMRER--AEKQRRDLSEELEALRTELEDTLDstaaQQELRSRREAELSELQrcveeetRR 1207
Cdd:COG4717 110 ELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQ-------EE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1208 HETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLqasrsESERGRKRADNQLQELSARLA 1287
Cdd:COG4717 179 LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL-----ENELEAAALEERLKEARLLLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1288 QADReredreermhklqceIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNgLM 1367
Cdd:COG4717 254 IAAA---------------LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE-LE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1368 ERLEEEEERGKELSRQIQTHsqQLTELRKQSEEVNSAVEAGDEIRRKLQREldsaiqrerqkeEEKERVERQRERLREEI 1447
Cdd:COG4717 318 EEELEELLAALGLPPDLSPE--ELLELLDRIEELQELLREAEELEEELQLE------------ELEQEIAALLAEAGVED 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1448 EDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKEtrclaLSRALQEAQDQKEELERANKQL 1527
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE-----LEEELEELEEELEELREELAEL 458
|
490 500 510
....*....|....*....|....*....|...
gi 2414917124 1528 RLEMEQLVNqQDDVGKNVHELERTRRTLETEAQ 1560
Cdd:COG4717 459 EAELEQLEE-DGELAELLQELEELKAELRELAE 490
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
827-1400 |
1.01e-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: 57.29 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 827 KQQQLSALRVMQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEE 906
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 907 KAVLADQLQAEAELFAEAEEMRARLASR-------KQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEE 979
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSKMRSRAKLLmkraahvKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 980 EESARQR---LLLEKVTLETKVKSLETDLATAVE---QRERLGK------------EKKQLEERLNEVTDQLTEEEEKTK 1041
Cdd:TIGR00618 380 HIHTLQQqktTLTQKLQSLCKELDILQREQATIDtrtSAFRDLQgqlahakkqqelQQRYAELCAAAITCTAQCEKLEKI 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1042 SLNKLKNKQEAVI---ADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLG--MLSSDLRGSLAQKEKEITSLQGR 1116
Cdd:TIGR00618 460 HLQESAQSLKEREqqlQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNpaRQDIDNPGPLTRRMQRGEQTYAQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1117 LEEEGArRTEAQrsLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQqelrsrreaelSE 1196
Cdd:TIGR00618 540 LETSEE-DVYHQ--LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL-----------SE 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1197 LQRCVEEETRRHETQLSELRVKHSAALDSLQEQldnskrarQSLEKAKATLEEERQNLTSE--LKSLQASRSESERGRKR 1274
Cdd:TIGR00618 606 AEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS--------QELALKLTALHALQLTLTQErvREHALSIRVLPKELLAS 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1275 ADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQD-ESRQKMALA 1353
Cdd:TIGR00618 678 RQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLK 757
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2414917124 1354 SRV----RALEEEKNGLMERLEEE--EERGKELSRQIQTHSQQLTELRKQSEE 1400
Cdd:TIGR00618 758 ARTeahfNNNEEVTAALQTGAELShlAAEIQFFNRLREEDTHLLKTLEAEIGQ 810
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
985-1194 |
1.25e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.55 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 985 QRLLLEKVTLETKVKSLETdlataveQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKRe 1064
Cdd:COG1579 6 LRALLDLQELDSELDRLEH-------RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1065 eqgrleqekfkrrmeseameAQEQLSDlgmlssdlrgslAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEE 1144
Cdd:COG1579 78 --------------------YEEQLGN------------VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEE 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2414917124 1145 VENERGMRERAEKQRRDLSEELEALRTELEDTLDS-TAAQQELRSRREAEL 1194
Cdd:COG1579 126 LAELEAELAELEAELEEKKAELDEELAELEAELEElEAEREELAAKIPPEL 176
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1127-1340 |
1.62e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1127 AQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETR 1206
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1207 RHETQLSEL--------RVKHSAALDSL--QEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRAD 1276
Cdd:COG4942 98 ELEAQKEELaellralyRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 1277 NQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARE 1340
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
962-1418 |
2.23e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 962 EKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLA--TAVEQRERLGKEKKQLEERLNEVTDQLteeeek 1039
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERL------ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1040 tkslnklknkqeaviadleERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLgmlssdLRGSLAQKEKEITSLQGRLEE 1119
Cdd:COG4717 149 -------------------EELEERLEELRELEEELEELEAELAELQEELEEL------LEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1120 EGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEE-----------LEALRTELEDTLDSTAA------ 1182
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1183 ------------QQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKA-----KA 1245
Cdd:COG4717 284 gllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAeeleeEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1246 TLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLqceieslsgnlsSSDSKSLRLA 1325
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL------------LEALDEEELE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1326 KEISSLESQLHDARELLQDESRQKMALASRVRALEEEKnglmerleeeeeRGKELSRQIQTHSQQLTELRKQSEEVNSAV 1405
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQLEEDG------------ELAELLQELEELKAELRELAEEWAALKLAL 499
|
490
....*....|...
gi 2414917124 1406 EAGDEIRRKLQRE 1418
Cdd:COG4717 500 ELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1220-1423 |
2.44e-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: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1220 SAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREER 1299
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1300 MHKLQCEIESL------SGNLSS-----SDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLME 1368
Cdd:COG4942 99 LEAQKEELAELlralyrLGRQPPlalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2414917124 1369 RLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAI 1423
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1306-1825 |
2.53e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1306 EIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQ 1385
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1386 THSQQLTELRKQSEEVNSAVEAGDEIRR--KLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTA 1463
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEYIKlsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1464 LEKRQ---KKFDQCLAEEKAVSARLAEERDRAEADSREKetrclaLSRALQEAQDQKEELERANKQLRLEMEQLVNQQDD 1540
Cdd:PRK03918 350 LEKRLeelEERHELYEEAKAKKEELERLKKRLTGLTPEK------LEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1541 VGKNVHELERTRRTLETeaqnlriqtqeleeelseaeNSRLRLEVTLQALKAQFEREISTNEE---KGEEKRRALSKQVR 1617
Cdd:PRK03918 424 LKKAIEELKKAKGKCPV--------------------CGRELTEEHRKELLEEYTAELKRIEKelkEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1618 ELEIQLEEERSQRSQSVSSK--KQLEAELQEAEAQ-VETANRGKEEAMKQLRRLQGQMKEVLRELDEAKvtrdDVISQSK 1694
Cdd:PRK03918 484 ELEKVLKKESELIKLKELAEqlKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE----ELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1695 DSEKKIQTLE---AEVLHLTEELAVSERQKRQAQ-QERDEIADEMVSSSSGKNVLSEEKRRLD-ARVNQLEEDLEEEQTN 1769
Cdd:PRK03918 560 ELEKKLDELEeelAELLKELEELGFESVEELEERlKELEPFYNEYLELKDAEKELEREEKELKkLEEELDKAFEELAETE 639
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1770 NELLTERLRKTALQVE--------------TLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGA 1825
Cdd:PRK03918 640 KRLEELRKELEELEKKyseeeyeelreeylELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
864-1287 |
3.33e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 864 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEAELFAEAEEmRARLASRKQELEevlg 943
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-EAELAELPERLE---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 944 eletrleeeeergvQLANEKKKMQQNIQDLEEQLEEEESARQRL--LLEKVTLETkvkslETDLATAVEQRERLGKEKKQ 1021
Cdd:COG4717 150 --------------ELEERLEELRELEEELEELEAELAELQEELeeLLEQLSLAT-----EEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1022 LEERLNEVTDQLTEEEEKTKSLnklknKQEAVIADLEERLKREEQ------GRLEQEKFKRRMESEAMEAQEQLSDLGML 1095
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQL-----ENELEAAALEERLKEARLllliaaALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1096 SSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQ-----------VSELKEEVENERGMRERAEKQRRDLse 1164
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlspeeLLELLDRIEELQELLREAEELEEEL-- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1165 ELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAAL-----DSLQEQLDNSKRARQS 1239
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLealdeEELEEELEELEEELEE 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1240 LEKAKATLEEERQNLTSELKSLQASR--SESERGRKRADNQLQELSARLA 1287
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEEWA 493
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1488-1930 |
3.33e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1488 ERDRAEAdsREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLvNQQDDVGKNVHELERTRRTLETEAQNLRiQTQ 1567
Cdd:COG4717 77 EEELKEA--EEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLE-ELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1568 ELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEA 1647
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1648 EAQVETANrgKEEAMKQLRRLQGQMKEVLreldeAKVTRDDVISQSKDSEKKIQTLEAEVLHLteELAVSERQKRQAQQE 1727
Cdd:COG4717 233 ENELEAAA--LEERLKEARLLLLIAAALL-----ALLGLGGSLLSLILTIAGVLFLVLGLLAL--LFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1728 RDEIADEMVSSSSGKNVLSEEKRRLDArvnqleedleeeqtNNELLTERLRKTALQVETLTVQLQGERTLaqKAEAAREQ 1807
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGL--------------PPDLSPEELLELLDRIEELQELLREAEEL--EEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1808 LEKQNKELKARLG-EMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEvmmQAEDERRHADQY 1886
Cdd:COG4717 368 LEQEIAALLAEAGvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE---ELEELEEELEEL 444
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2414917124 1887 REQLDKSMVRLKQLKRQLEEVEEENsRSSAQKRKLQRELEELTD 1930
Cdd:COG4717 445 EEELEELREELAELEAELEQLEEDG-ELAELLQELEELKAELRE 487
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1455-1946 |
3.80e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1455 QRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEAdsrEKETRCLALSRAlQEAQDQKEELERANKQLRLEMEQL 1534
Cdd:PRK02224 195 QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE---TRDEADEVLEEH-EERREELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1535 VNQQDDVGKNVHELERTRRTLETEAQNLRIQTQELEEELSeaensrlrlevTLQALKAQFEREISTNEEKGEEKRRALSK 1614
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAE-----------AVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1615 QVRELEIQLEEERSQRSQSVSSKKQ---LEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDEAKVTRDDVIS 1691
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEaaeLESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1692 QSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQ-------QERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEDLE 1764
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1765 EEqtnnelltERLRKTALQVETLTVQLQG-ERTLAQKAEAAREQLEKQnKELKARLGEMEGAVRGKHRMSVAALEAKIET 1843
Cdd:PRK02224 500 RA--------EDLVEAEDRIERLEERREDlEELIAERRETIEEKRERA-EELRERAAELEAEAEEKREAAAEAEEEAEEA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1844 MEEQLEQERQERAIANKLMRKteKKLKEVMMQAEDERRHADQYREQL-------DKSMVRLKQL---KRQLEEVEEENSR 1913
Cdd:PRK02224 571 REEVAELNSKLAELKERIESL--ERIRTLLAAIADAEDEIERLREKRealaelnDERRERLAEKrerKRELEAEFDEARI 648
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2414917124 1914 SSAQKRKLQRE---------LEELTDSSQTMNREISSLRNQL 1946
Cdd:PRK02224 649 EEAREDKERAEeyleqveekLDELREERDDLQAEIGAVENEL 690
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1510-1928 |
4.71e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.34 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1510 LQEAQDQKEELERANKQLRLEMEQLVNQQDDVGknvhELERTRRTLETEAQnlriqtqeleeelseAENSRLRLevTLQA 1589
Cdd:COG3096 284 SERALELRRELFGARRQLAEEQYRLVEMARELE----ELSARESDLEQDYQ---------------AASDHLNL--VQTA 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1590 LKAQfereistneEKGEEKRRALSkqvrELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRG---KEEAMKQLR 1666
Cdd:COG3096 343 LRQQ---------EKIERYQEDLE----ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQladYQQALDVQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1667 RLQGQMKEVLRELDEAK-------VTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSE---RQKRQAQQERDEIADEMV 1736
Cdd:COG3096 410 TRAIQYQQAVQALEKARalcglpdLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADaarRQFEKAYELVCKIAGEVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1737 SS---SSGKNVLSE--EKRRLDARVNQLEEDLEEEqtnnELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQ 1811
Cdd:COG3096 490 RSqawQTARELLRRyrSQQALAQRLQQLRAQLAEL----EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQ 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1812 NKELKARLGEmEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLmrktekklkevmmqaederrhADQYREQLD 1891
Cdd:COG3096 566 LEELEEQAAE-AVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERL---------------------REQSGEALA 623
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2414917124 1892 KS---MVRLKQLKRQLEEVEEENSRSSAQKRKLQRELEEL 1928
Cdd:COG3096 624 DSqevTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1503-1743 |
7.60e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1503 CLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERTRRTLETEAQNLRIQTQELEEELSEAENSRLR 1582
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1583 LEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEiQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAM 1662
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFL-DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1663 KQLRRLQGQMKEVLRELDEAKVTRDDVISQskdSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGK 1742
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
.
gi 2414917124 1743 N 1743
Cdd:COG4942 251 L 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1508-1973 |
1.05e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1508 RALQEAQDQKEELE--RANKQLRLEMEQLVNQQDDVGK--NVHELERTRRTLETEAQNLRIQTQELEEELSEAENSRLRL 1583
Cdd:COG4913 242 EALEDAREQIELLEpiRELAERYAAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1584 EVTLQALKAQ-----------FEREISTNEEKGEEKRRA---LSKQVRELEIQLEEErsqrsqsvssKKQLEAELQEAEA 1649
Cdd:COG4913 322 REELDELEAQirgnggdrleqLEREIERLERELEERERRrarLEALLAALGLPLPAS----------AEEFAALRAEAAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1650 QVETANRGKEEAMKQLRRLQGQMKEVLRELDEAKVTRDDVISQSKDSEKKIQTLEAEvlhLTEELAVSERQKR------- 1722
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA---LAEALGLDEAELPfvgelie 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1723 -QAQQERDEIADEMVSSSSGKNVLSEEKRRLDA----------------RVNQLEEDLEEEQTNNELLTERL-------- 1777
Cdd:COG4913 469 vRPEEERWRGAIERVLGGFALTLLVPPEHYAAAlrwvnrlhlrgrlvyeRVRTGLPDPERPRLDPDSLAGKLdfkphpfr 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1778 ---------RKTALQVE------------TLTVQLQGERTLAQK---------------AEAAREQLEKQNKELKARLge 1821
Cdd:COG4913 549 awleaelgrRFDYVCVDspeelrrhpraiTRAGQVKGNGTRHEKddrrrirsryvlgfdNRAKLAALEAELAELEEEL-- 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1822 megavrgkhrmsvAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKevMMQAEDERRHADQYREQLDKSMVRLKQLK 1901
Cdd:COG4913 627 -------------AEAEERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERLDASSDDLAALE 691
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2414917124 1902 RQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLSFPEWRPDIRAALPLSMRGRRALVDDL 1973
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1054-1243 |
1.20e-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: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1054 IADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLS----SDLRgsLAQKEKEITSLQGRLEEegarrteaqr 1129
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeyswDEID--VASAEREIAELEAELER---------- 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1130 sLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDS-TAAQQELRSRREAELSELQRCVEEetRRH 1208
Cdd:COG4913 680 -LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEElDELQDRLEAAEDLARLELRALLEE--RFA 756
|
170 180 190
....*....|....*....|....*....|....*.
gi 2414917124 1209 ETQLSELRVKHSAALDSLQEQLDNSK-RARQSLEKA 1243
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLnRAEEELERA 792
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1382-1947 |
1.41e-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: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1382 RQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNC 1461
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1462 TA-LEKRQKKFDQCLAEEKAVSARLAEERDRAEAdsrEKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDD 1540
Cdd:TIGR02169 250 EEeLEKLTEEISELEKRLEEIEQLLEELNKKIKD---LGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1541 VGKNVHELERTRRTLETEAQNLRIQtqeleeelseaensRLRLEVTLQALKAQFE---REISTNEEKGEEKRRALSKQVR 1617
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKR--------------RDKLTEEYAELKEELEdlrAELEEVDKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1618 ELEI---QLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDEAKVTRDDVISQSK 1694
Cdd:TIGR02169 393 KLEKlkrEINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1695 DSEKKIQTLEAEVLHLTEELAVSERQKRQAQQE-RDEIADEMVSSSSGKNV--LSEEKRRLDARVNQLEEDLEEEQTNN- 1770
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELAEAEAQARASEERvRGGRAVEEVLKASIQGVhgTVAQLGSVGERYATAIEVAAGNRLNNv 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1771 ------------ELLTER---------LRKTAL-------------------------QVETLTVQLQGERTLAQKAEAA 1804
Cdd:TIGR02169 553 vveddavakeaiELLKRRkagratflpLNKMRDerrdlsilsedgvigfavdlvefdpKYEPAFKYVFGDTLVVEDIEAA 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1805 REQLEK-----QNKELKARLGEMEG-AVRGKHRMSVAA---------------LEAKIETMEEQLEQERQERAIANKLMR 1863
Cdd:TIGR02169 633 RRLMGKyrmvtLEGELFEKSGAMTGgSRAPRGGILFSRsepaelqrlrerlegLKRELSSLQSELRRIENRLDELSQELS 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1864 KTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEEN-------SRSSAQKRKLQRELEELTDSS---- 1932
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELkeleariEELEEDLHKLEEALNDLEARLshsr 792
|
650
....*....|....*.
gi 2414917124 1933 -QTMNREISSLRNQLS 1947
Cdd:TIGR02169 793 iPEIQAELSKLEEEVS 808
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
867-1258 |
1.42e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 867 RQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLE-EKAVLADQLQAEAELFAEAEEMRA----RLASRKQELEEV 941
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaEEKKKADELKKAEELKKAEEKKKAeeakKAEEDKNMALRK 1582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 942 LGELETRLEEEEERGVQLANEKKKMQ-------QNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLE------------ 1002
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKaeeakkaEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEelkkaeeenkik 1662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1003 -TDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESE 1081
Cdd:PTZ00121 1663 aAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED 1742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1082 AMEAQEqlsdlgmlssdlrgslAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQvSELKEEVENERGMRERAEKQRRD 1161
Cdd:PTZ00121 1743 KKKAEE----------------AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE-EELDEEDEKRRMEVDKKIKDIFD 1805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1162 LSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLE 1241
Cdd:PTZ00121 1806 NFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIE 1885
|
410
....*....|....*..
gi 2414917124 1242 KAKATLEEERQNLTSEL 1258
Cdd:PTZ00121 1886 EADEIEKIDKDDIEREI 1902
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1098-1534 |
1.51e-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: 53.80 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1098 DLRGSLAQKEKEITSLQGRLEE---EGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRrdlsEELEALRTELE 1174
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEmarELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQ----EDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1175 DTLDSTAAQQELRSRREAELSElqrcVEEETRRHETQLSELRvkhsAALDSLQEQLDNSKRARQSLEKAKATLEEERQNL 1254
Cdd:COG3096 365 EQEEVVEEAAEQLAEAEARLEA----AEEEVDSLKSQLADYQ----QALDVQQTRAIQYQQAVQALEKARALCGLPDLTP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1255 TSELKSLQASRSESERgrkrADNQLQELSARLAQADreredreerMHKLQCE-----IESLSGNLSSSDSKSlrlakeis 1329
Cdd:COG3096 437 ENAEDYLAAFRAKEQQ----ATEEVLELEQKLSVAD---------AARRQFEkayelVCKIAGEVERSQAWQ-------- 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1330 slesqlhDARELLQDESRQKmALASRVRALEeeknglmerleeeeergkelsrqiqthsQQLTELRKQSEEVNSAVEAGD 1409
Cdd:COG3096 496 -------TARELLRRYRSQQ-ALAQRLQQLR----------------------------AQLAELEQRLRQQQNAERLLE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1410 EIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMtIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEER 1489
Cdd:COG3096 540 EFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQR-SELRQQLEQLRARIKELAARAPAWLAAQDALERLREQS 618
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2414917124 1490 DRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQL 1534
Cdd:COG3096 619 GEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1079-1289 |
1.53e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1079 ESEAMEAQEQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENER---GMRERA 1155
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReelGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1156 EKQRRDLSEELEAL--RTELEDTLDSTAAQQELRSRREAELSELQRcVEEETRRHETQLSELRVKHSAALDSLQEQLDNS 1233
Cdd:COG3883 95 LYRSGGSVSYLDVLlgSESFSDFLDRLSALSKIADADADLLEELKA-DKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2414917124 1234 KRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQA 1289
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1018-1701 |
2.01e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1018 EKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQgrlEQEKFKRRMESEAMEAQEQLSDLGMLSS 1097
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQ---QIKDLNDKLKKNKDKINKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1098 DLRGSLAQK---EKEITSLQGRLEEEgarrteaQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELE 1174
Cdd:TIGR04523 111 EIKNDKEQKnklEVELNKLEKQKKEN-------KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1175 DTLDSTAAQQELRSRREAELSELQRCVEEEtrrhetqlselrvkhsaalDSLQEQLDNSKRARQSLEKAKATLEEERQNL 1254
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKKIQKN-------------------KSLESQISELKKQNNQLKDNIEKKQQEINEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1255 TSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLR-----LAKEIS 1329
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKselknQEKKLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1330 SLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGD 1409
Cdd:TIGR04523 325 EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1410 EIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTialqrerQNCTALEKRQKKFDQCLAEEKAVSARLAEER 1489
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT-------NQDSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1490 DRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERTRRTLETEaqnlrIQTQEL 1569
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE-----LNKDDF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1570 EEELSEAENSRLRLEVTLQALKAQFEREISTNEEKgEEKRRALSKQVRELEIQLEEersqrsqSVSSKKQLEAELQEAEA 1649
Cdd:TIGR04523 553 ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEK-QELIDQKEKEKKDLIKEIEE-------KEKKISSLEKELEKAKK 624
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2414917124 1650 QVETANRGKEEAMKQLRRLQGQMKEVLRELDEAKVTRDDVISQSKDSEKKIQ 1701
Cdd:TIGR04523 625 ENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1637-1982 |
2.09e-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: 53.15 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1637 KKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQ------MKEVLRELDEAKVTrdDVISQSKDSEKKIQTLEAEVLHL 1710
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRRErekaerYQALLKEKREYEGY--ELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1711 TEELAvserqkrQAQQERDEIADEMVSSssgKNVLSEEKRRLDARVNQLEEDleeeqtnnelLTERLRKTALQVETLtvq 1790
Cdd:TIGR02169 250 EEELE-------KLTEEISELEKRLEEI---EQLLEELNKKIKDLGEEEQLR----------VKEKIGELEAEIASL--- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1791 lqgERTLAQKAEAArEQLEKQNKELKARLGEMEGAVRGkhrmsvaaLEAKIETMEEQLEQERQERAIANKLMRKTEKKLK 1870
Cdd:TIGR02169 307 ---ERSIAEKEREL-EDAEERLAKLEAEIDKLLAEIEE--------LEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1871 EVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLSFPE 1950
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
330 340 350
....*....|....*....|....*....|....*.
gi 2414917124 1951 WR----PDIRAALPLSMRGRRALVDDLSLENSDSEE 1982
Cdd:TIGR02169 455 WKleqlAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1465-1906 |
2.20e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1465 EKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQ-DQKEELERANKQLRLEMEQLVNQQDDVGK 1543
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1544 NVHELE----RTRRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQF---EREI-------STNEEKGEEKR 1609
Cdd:COG4913 367 LLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELrelEAEIaslerrkSNIPARLLALR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1610 RALSK----------------QVRELE----------------------------------------IQLEEERSQRSQS 1633
Cdd:COG4913 447 DALAEalgldeaelpfvgeliEVRPEEerwrgaiervlggfaltllvppehyaaalrwvnrlhlrgrLVYERVRTGLPDP 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1634 VSSKKQ------------------LEAELQEAE--AQVETanrgkEEAMKQLRR---LQGQMKE--VLRELD-EAKVTRD 1687
Cdd:COG4913 527 ERPRLDpdslagkldfkphpfrawLEAELGRRFdyVCVDS-----PEELRRHPRaitRAGQVKGngTRHEKDdRRRIRSR 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1688 DVISQskDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEmvssssgKNVLSEEKRRLDARVNQLEEDLEEEQ 1767
Cdd:COG4913 602 YVLGF--DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQER-------REALQRLAEYSWDEIDVASAEREIAE 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1768 TNNELltERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRgkhrmsvaALEAKIETMEEQ 1847
Cdd:COG4913 673 LEAEL--ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD--------ELQDRLEAAEDL 742
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2414917124 1848 LEQERQERAIAnklmrktekklkevMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEE 1906
Cdd:COG4913 743 ARLELRALLEE--------------RFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1464-1950 |
2.38e-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: 53.13 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1464 LEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERAN-KQLRLEMEQLVNQQDDVG 1542
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHqRTVREKERELVDCQRELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1543 KNVHEL-ERTRRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFERE----------ISTNEEKGEEKRRA 1611
Cdd:TIGR00606 330 KLNKERrLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpfserqiknfHTLVIERQEDEAKT 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1612 LSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLrELDEAKVTRDDVIS 1691
Cdd:TIGR00606 410 AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIL-ELDQELRKAERELS 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1692 QSkDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADE------MVSSSSGKNVLSEEKRRLDARVNQLEEDLEE 1765
Cdd:TIGR00606 489 KA-EKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHtttrtqMEMLTKDKMDKDEQIRKIKSRHSDELTSLLG 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1766 EQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAV------------------- 1826
Cdd:TIGR00606 568 YFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsqdeesdlerlkee 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1827 ---RGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKsmvRLKQLKRQ 1903
Cdd:TIGR00606 648 iekSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTES---ELKKKEKR 724
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2414917124 1904 LEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLSFPE 1950
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE 771
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1487-1946 |
2.71e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1487 EERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLvNQQDDVGKNVHELERTRRTLETEAQNLRiQT 1566
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLE-EL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1567 QELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQE 1646
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1647 AEAQVETANrgKEEAMKQLRRLQGQMKEVLreldeAKVTRDDVISQSKDSEKKIQTLEAEVLHLteELAVSERQKRQAQQ 1726
Cdd:COG4717 232 LENELEAAA--LEERLKEARLLLLIAAALL-----ALLGLGGSLLSLILTIAGVLFLVLGLLAL--LFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1727 ERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEDLEEEQTNNELLTERLRKTALQVETLTVQ--------------LQ 1792
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEeleqeiaallaeagVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1793 GERTLAQKAEAARE--QLEKQNKELKARLGEMEGAVRGKHRM-SVAALEAKIETmeeqleQERQERAIANKL--MRKTEK 1867
Cdd:COG4717 383 DEEELRAALEQAEEyqELKEELEELEEQLEELLGELEELLEAlDEEELEEELEE------LEEELEELEEELeeLREELA 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1868 KLKEVMMQAEDERRHADQYREQldksmvrlKQLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQ-TMNREISSLRNQL 1946
Cdd:COG4717 457 ELEAELEQLEEDGELAELLQEL--------EELKAELRELAEEWAALKLALELLEEAREEYREERLpPVLERASEYFSRL 528
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1137-1943 |
4.70e-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: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1137 QVSELKEEVENERGMRERAEKQRRDLSE---ELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLS 1213
Cdd:TIGR00606 225 QITSKEAQLESSREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLN 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1214 ELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLA----QA 1289
Cdd:TIGR00606 305 DLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfER 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1290 DREREDREERMHKLQCEIESlsgnlsssdSKSLRLAKEISSLESQLHDARELLqDESRQKMALASRVRALEEEKnglMER 1369
Cdd:TIGR00606 385 GPFSERQIKNFHTLVIERQE---------DEAKTAAQLCADLQSKERLKQEQA-DEIRDEKKGLGRTIELKKEI---LEK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1370 LEEEEERGKELSRQIQTHSQQL----TELRKQSEEV-----NSAVEAGDEIRRKLQRE---LDSAIQRERQKEEEKERVE 1437
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRIleldQELRKAERELskaekNSLTETLKKEVKSLQNEkadLDRKLRKLDQEMEQLNHHT 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1438 RQRERLREEIEDMTIALQRERQNctalEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQK 1517
Cdd:TIGR00606 532 TTRTQMEMLTKDKMDKDEQIRKI----KSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNK 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1518 EELeraNKQLRLEMEQLVNQQDDV----GKNVHE--LERTRRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALK 1591
Cdd:TIGR00606 608 NHI---NNELESKEEQLSSYEDKLfdvcGSQDEEsdLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQ 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1592 AQFEREISTNEEKGE---------EKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAM 1662
Cdd:TIGR00606 685 RVFQTEAELQEFISDlqsklrlapDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1663 KQLRRLQGQMKEVLRELDEAKVTRDDVI------SQSKDSEKKIQTLEAEVlhLTEELAVSERQKRQAQQERDEIADEMV 1736
Cdd:TIGR00606 765 NDIEEQETLLGTIMPEEESAKVCLTDVTimerfqMELKDVERKIAQQAAKL--QGSDLDRTVQQVNQEKQEKQHELDTVV 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1737 SSSSGKNVLSEEKRR----LDARVNQLEEDLEEEQTN---NELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLE 1809
Cdd:TIGR00606 843 SKIELNRKLIQDQQEqiqhLKSKTNELKSEKLQIGTNlqrRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1810 KQNKELKARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERaiaNKLMRKTEKKLKEVMMQAEDERRHADQYREQ 1889
Cdd:TIGR00606 923 QEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK---DDYLKQKETELNTVNAQLEECEKHQEKINED 999
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 1890 LdksmvRLKQLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLR 1943
Cdd:TIGR00606 1000 M-----RLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
868-1091 |
6.11e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 868 QDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGELET 947
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 948 RLEEEEErgvQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLN 1027
Cdd:COG4942 98 ELEAQKE---ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 1028 EVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSD 1091
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
851-1366 |
6.79e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 851 QWWRLFTKVKPLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEEKAVL-----ADQLQAEAELFAEAE 925
Cdd:TIGR00618 383 TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELcaaaiTCTAQCEKLEKIHLQ 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 926 EMRARLASRKQeleevlgeletrleeeeergvQLANEKKKMQQNIQ-DLEEQLEEEESARQRLLLEKVTLETKVKSLETD 1004
Cdd:TIGR00618 463 ESAQSLKEREQ---------------------QLQTKEQIHLQETRkKAVVLARLLELQEEPCPLCGSCIHPNPARQDID 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1005 LATAVEQR-ERLGKEKKQLEERLNEVTDQLTEEeekTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAM 1083
Cdd:TIGR00618 522 NPGPLTRRmQRGEQTYAQLETSEEDVYHQLTSE---RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1084 EAQEQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENE----RGMRERAEKQR 1159
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHalsiRVLPKELLASR 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1160 RDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQS 1239
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKA 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1240 LEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERmhkLQCEIESLSGNLSSSDS 1319
Cdd:TIGR00618 759 RTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLS 835
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2414917124 1320 KSLRLAKEISSLESQLHDARELLQdESRQKMALASRVRALEEEKNGL 1366
Cdd:TIGR00618 836 RLEEKSATLGEITHQLLKYEECSK-QLAQLTQEQAKIIQLSDKLNGI 881
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
971-1285 |
7.23e-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: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 971 QDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQ--------------LTEE 1036
Cdd:pfam07888 55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEkdallaqraahearIREL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1037 EEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSDLRGSLAQKEKEITSLQGR 1116
Cdd:pfam07888 135 EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1117 LEEEGARRTEAQRslrealsQVSELKEEVENERGMRERAEKQRRdlseELEALRTELEdtldSTAAQqelRSRREAELse 1196
Cdd:pfam07888 215 ITTLTQKLTTAHR-------KEAENEALLEELRSLQERLNASER----KVEGLGEELS----SMAAQ---RDRTQAEL-- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1197 lqrcveeetRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSEL----KSLQASRSESER-- 1270
Cdd:pfam07888 275 ---------HQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELqrleERLQEERMEREKle 345
|
330
....*....|....*...
gi 2414917124 1271 ---GRKRADNQLQELSAR 1285
Cdd:pfam07888 346 velGREKDCNRVQLSESR 363
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1588-1819 |
7.47e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1588 QALKAQFEREISTNEEKGEEKRRALS---KQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQ 1664
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAalkKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1665 LRRLQGQMKEVLRELDEA-KVTRDDVISQSKD---SEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSS 1740
Cdd:COG4942 99 LEAQKEELAELLRALYRLgRQPPLALLLSPEDfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2414917124 1741 GKNVLSEEKRRLDARVNQLEEDLEEEQTNNELLTERLRKTALQVETLTVQLqgERTLAQKAEAAREQLEKQNKELKARL 1819
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI--ARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1675-1947 |
8.27e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1675 VLRELDEAKVTRDDVISQ-----SKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEiADEMVSSSSGKNvlsEEK 1749
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQieekeEKDLHERLNGLESELAELDEEIERYEEQREQARETRDE-ADEVLEEHEERR---EEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1750 RRLDARVNQLEEDLEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRgK 1829
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLE-E 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1830 HRMSVAALEAKIETMEEQLeqerqeraianklmRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEE 1909
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDA--------------DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270
....*....|....*....|....*....|....*...
gi 2414917124 1910 ENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLS 1947
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1646-1960 |
9.17e-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: 51.22 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1646 EAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDEAKVTRDDVISQSKDSEKKIqtlEAEVLHLTEELAVSERQKRQAQ 1725
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKR---EYEGYELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1726 QERDEIADEMvssssgknvlseekrrldarvnqleedleeeqtnnELLTERLRKTALQVETLtvqlqgERTLAQKAEAAR 1805
Cdd:TIGR02169 244 RQLASLEEEL-----------------------------------EKLTEEISELEKRLEEI------EQLLEELNKKIK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1806 EQLEKQNKELKARLGEMEGavrgkhrmSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQ 1885
Cdd:TIGR02169 283 DLGEEEQLRVKEKIGELEA--------EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2414917124 1886 YREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQL-SFPEWRPDIRAALP 1960
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELqRLSEELADLNAAIA 430
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1033-1281 |
9.29e-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: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1033 LTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSDlRGSLAQKEKEITS 1112
Cdd:pfam17380 265 MTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD-RQAAIYAEQERMA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1113 LQGRLEEEGARRTEAQRSLREALSQ--VSELKEEVENERGMRERAEKQRRdLSEELEALRTE--LEDTLDSTAAQQ---- 1184
Cdd:pfam17380 344 MERERELERIRQEERKRELERIRQEeiAMEISRMRELERLQMERQQKNER-VRQELEAARKVkiLEEERQRKIQQQkvem 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1185 -ELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKA---KATLEEERQN-LTSELK 1259
Cdd:pfam17380 423 eQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEkrdRKRAEEQRRKiLEKELE 502
|
250 260
....*....|....*....|..
gi 2414917124 1260 SLQASRSESERGRKRADNQLQE 1281
Cdd:pfam17380 503 ERKQAMIEEERKRKLLEKEMEE 524
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1476-1946 |
9.30e-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: 50.88 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1476 AEEKAVSARLAEERDRAEADSR-------EKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHEL 1548
Cdd:pfam05483 99 AELKQKENKLQENRKIIEAQRKaiqelqfENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYER 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1549 ERTRRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTL-------QALKAQFEREISTNEekgeekrralsKQVRELEI 1621
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLkedhekiQHLEEEYKKEINDKE-----------KQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1622 QLEEERSQRSQSVSskkqLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKevlRELDEAKVTRDDVISQSKDSEKKIQ 1701
Cdd:pfam05483 248 QITEKENKMKDLTF----LLEESRDKANQLEEKTKLQDENLKELIEKKDHLT---KELEDIKMSLQRSMSTQKALEEDLQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1702 TLEAEVLHLTEELAVSERQKRQAQQERDEIADEM-VSSSSGKNVLSEEKRRLDarvnqleedleeeqtNNELlterlrkt 1780
Cdd:pfam05483 321 IATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFeATTCSLEELLRTEQQRLE---------------KNED-------- 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1781 alQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAK---------IETMEEQLEQE 1851
Cdd:pfam05483 378 --QLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKgkeqeliflLQAREKEIHDL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1852 RQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKR-------QLEEVEEENSRSSAQKRKLQRE 1924
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQeasdmtlELKKHQEDIINCKKQEERMLKQ 535
|
490 500
....*....|....*....|..
gi 2414917124 1925 LEELTDSSQTMNREISSLRNQL 1946
Cdd:pfam05483 536 IENLEEKEMNLRDELESVREEF 557
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
828-1340 |
1.01e-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: 50.89 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 828 QQQLSALRVMQRNcaaylklRNWQWWRLFTKVKPLLQVTRQD--EEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLE 905
Cdd:pfam15921 298 QSQLEIIQEQARN-------QNSMYMRQLSDLESTVSQLRSElrEAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQ 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 906 EKAVLADQLQ-------AEAELFAEAEEMRARLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLE 978
Cdd:pfam15921 371 ESGNLDDQLQklladlhKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQM 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 979 EEESARQRLLLEKVTLETKVKSLETDLATAVEQrerLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLE 1058
Cdd:pfam15921 451 AAIQGKNESLEKVSSLTAQLESTKEMLRKVVEE---LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVD 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1059 ERLKREEQGRLEQEKFKR-RMESEAMEAQ------------EQLSDL-------GMLSSDLRGSLAQKEKEITSLQGRLE 1118
Cdd:pfam15921 528 LKLQELQHLKNEGDHLRNvQTECEALKLQmaekdkvieilrQQIENMtqlvgqhGRTAGAMQVEKAQLEKEINDRRLELQ 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1119 EEGARRTEAQRSLREALSQVSELkeEVENERGMRERAEKQR--RDLSEELEALRTELEDTldstaaQQELRSRREaELSE 1196
Cdd:pfam15921 608 EFKILKDKKDAKIRELEARVSDL--ELEKVKLVNAGSERLRavKDIKQERDQLLNEVKTS------RNELNSLSE-DYEV 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1197 LQRCVEEETRRHETQLSELRVKhsaaLDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKslqasrseSERGrkrad 1276
Cdd:pfam15921 679 LKRNFRNKSEEMETTTNKLKMQ----LKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQIT--------AKRG----- 741
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 1277 nQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARE 1340
Cdd:pfam15921 742 -QIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
864-1066 |
1.02e-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: 50.15 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 864 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEaelfaeaeemRARLASRKQELEEVLG 943
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ----------KEELAELLRALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 944 ELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLE 1023
Cdd:COG4942 119 QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2414917124 1024 ERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQ 1066
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
880-1541 |
1.42e-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: 50.50 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 880 QKAKEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEAELFAEaeeMRARLASRKQELEEVLGEletrleeeeergvql 959
Cdd:pfam15921 285 EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQ---LRSELREAKRMYEDKIEE--------------- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 960 anekkkmqqniqdleeqleeeesarqrlllekvtLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLtEEEEK 1039
Cdd:pfam15921 347 ----------------------------------LEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADL-HKREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1040 TKSLNKLKNKQeaviadleeRLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSDLRGslaQKEKEITSLQGRLE- 1118
Cdd:pfam15921 392 ELSLEKEQNKR---------LWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQG---QMERQMAAIQGKNEs 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1119 -EEGARRTEAQRSLREALSQVSelkEEVENERGMRERAEKQRRDLSEELEalrtELEDTLDSTAAQ-QELRSRREAELSE 1196
Cdd:pfam15921 460 lEKVSSLTAQLESTKEMLRKVV---EELTAKKMTLESSERTVSDLTASLQ----EKERAIEATNAEiTKLRSRVDLKLQE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1197 LQRCVEEET--RRHETQLSELRVKHSA---ALDSLQEQLDNSK-------RARQSLEKAKATLEEERQNLTSELKSLQAS 1264
Cdd:pfam15921 533 LQHLKNEGDhlRNVQTECEALKLQMAEkdkVIEILRQQIENMTqlvgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1265 RSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQD 1344
Cdd:pfam15921 613 KDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMET 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1345 ESRQ-KMALASRVRALEEEKNGLMERLEE---EEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGD-------EIRR 1413
Cdd:pfam15921 693 TTNKlKMQLKSAQSELEQTRNTLKSMEGSdghAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANkekhflkEEKN 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1414 KLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIAL--------------QRERQNCTALeKRQKKFD------Q 1473
Cdd:pfam15921 773 KLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALdkaslqfaecqdiiQRQEQESVRL-KLQHTLDvkelqgP 851
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1474 CLAEEKAVSARLAEERDRAEADSREKETRCLA--LSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDV 1541
Cdd:pfam15921 852 GYTSNSSMKPRLLQPASFTRTHSNVPSSQSTAsfLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTV 921
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1654-1871 |
1.46e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1654 ANRGKEEAMKQLRRLQGQMKEVLRELDEAKVTRDDVISQSKDSEKKI-------QTLEAEVLHLTEELAVSERQKRQAQQ 1726
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIaalarriRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1727 ERDEIADEMvssssgknvlseeKRRLDARVNQLEEDLEEEQTNNELLTERLRKTAL----------QVETLTVQLQGERT 1796
Cdd:COG4942 98 ELEAQKEEL-------------AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYlkylaparreQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2414917124 1797 LAQKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMsVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKE 1871
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKL-LARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1127-1346 |
1.85e-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: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1127 AQRSLREALSQVSELKEE---VENERGMRERAEKQRRDLSEE----LEAL---RTELEDTlDSTAAQQELRSRREAeLSE 1196
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQddaAQNALADKERAEADRQRLEQEkqqqLAAIsgsQSQLEST-DQNALETNGQAQRDA-ILE 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1197 LQRCVEEETRRHETQLSELRVKHSAA---------------LDSLQEQLDNSKR-ARQSLEKAKATLEEERQNLTSELKS 1260
Cdd:NF012221 1614 ESRAVTKELTTLAQGLDALDSQATYAgesgdqwrnpfagglLDRVQEQLDDAKKiSGKQLADAKQRHVDNQQKVKDAVAK 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1261 LQASRSESERGRKRADNQLQElsarlAQADREREDREERMHKLQCEIESLSGNLSSSDSKSlRLAKEISSLESQLH---- 1336
Cdd:NF012221 1694 SEAGVAQGEQNQANAEQDIDD-----AKADAEKRKDDALAKQNEAQQAESDANAAANDAQS-RGEQDASAAENKANqaqa 1767
|
250
....*....|
gi 2414917124 1337 DARELLQDES 1346
Cdd:NF012221 1768 DAKGAKQDES 1777
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
993-1176 |
2.14e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 993 TLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKS-LNKLKNKQEAVIADLEERLKREEQGRLEQ 1071
Cdd:PHA02562 185 TLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAeIEELTDELLNLVMDIEDPSAALNKLNTAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1072 EKFKRRMESEAMEAQ------------EQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARR---TEAQRSLREALS 1136
Cdd:PHA02562 265 AKIKSKIEQFQKVIKmyekggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMdefNEQSKKLLELKN 344
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2414917124 1137 QVSELKEEVENERGMR-------ERAEKQRRDLSEELEALRTELEDT 1176
Cdd:PHA02562 345 KISTNKQSLITLVDKAkkvkaaiEELQAEFVDNAEELAKLQDELDKI 391
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1228-1946 |
2.16e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.97 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1228 EQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASrsesergrkradnqLQELSARLAQADREREDREERMHKLQCEI 1307
Cdd:TIGR00618 184 MEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHER--------------KQVLEKELKHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1308 ESLSGNLSSSD--SKSLRLAKEISSLESQLHDARELLqDESRQKMALASRVRALEE---EKNGLMERLEEEEERGKELSR 1382
Cdd:TIGR00618 250 EAQEEQLKKQQllKQLRARIEELRAQEAVLEETQERI-NRARKAAPLAAHIKAVTQieqQAQRIHTELQSKMRSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1383 QIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELdsaiqrerQKEEEKERVERQRERLREEIEDMTIALQRERQNCT 1462
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT--------SIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1463 ALEK---RQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQd 1539
Cdd:TIGR00618 401 ELDIlqrEQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE- 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1540 dvgkNVHELERTRRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRR------ALS 1613
Cdd:TIGR00618 480 ----QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDvyhqltSER 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1614 KQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDEaKVTRDDVISQS 1693
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP-EQDLQDVRLHL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1694 KDSEKKIQTLEAEVLHLTEELAvserQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEDLEEEQTNNELL 1773
Cdd:TIGR00618 635 QQCSQELALKLTALHALQLTLT----QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1774 TERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIEtmeeqLEQERQ 1853
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE-----LSHLAA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1854 ERAIANKLMRKTEKKLKEVMMQAEDERRHADQYRE-QLDKSMVRLKQLKRQLEEveeeNSRSSAQKRKLQRELEELTDSS 1932
Cdd:TIGR00618 786 EIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLEE----KSATLGEITHQLLKYEECSKQL 861
|
730
....*....|....
gi 2414917124 1933 QTMNREISSLRNQL 1946
Cdd:TIGR00618 862 AQLTQEQAKIIQLS 875
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1323-1724 |
2.33e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1323 RLAKEISSLESQLHDARELLQ--DESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEE 1400
Cdd:COG4717 92 ELQEELEELEEELEELEAELEelREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1401 VNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRER---QNCTALEKRQKKFDQCLAE 1477
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELeqlENELEAAALEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1478 EKAVSARLAEERDRAEADSREKE-------------TRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGkn 1544
Cdd:COG4717 252 LLIAAALLALLGLGGSLLSLILTiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALG-- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1545 vheLERTRRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEE------KGEEKRRALSKQVRE 1618
Cdd:COG4717 330 ---LPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelraalEQAEEYQELKEELEE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1619 LEIQLEEER--SQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVL--RELDEAKVTRDDVISQSK 1694
Cdd:COG4717 407 LEEQLEELLgeLEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELR 486
|
410 420 430
....*....|....*....|....*....|
gi 2414917124 1695 DSEKKIQTLEAEVLHLTEELAVSERQKRQA 1724
Cdd:COG4717 487 ELAEEWAALKLALELLEEAREEYREERLPP 516
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1476-1727 |
2.37e-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: 49.26 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1476 AEEKAVSARLAEERDRAEADSREKETrclaLSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERTRRTL 1555
Cdd:pfam05667 226 WNSQGLASRLTPEEYRKRKRTKLLKR----IAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1556 ETE----AQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFErEISTNEEKGEEKRRALSKQVRELEIQLEEERSQRS 1631
Cdd:pfam05667 302 HTEklqfTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLE-DLESSIQELEKEIKKLESSIKQVEEELEELKEQNE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1632 QSVSS---KKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEV-------LRELDEAKVTRDDVISQSKDsekKIQ 1701
Cdd:pfam05667 381 ELEKQykvKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHrvplieeYRALKEAKSNKEDESQRKLE---EIK 457
|
250 260
....*....|....*....|....*.
gi 2414917124 1702 TLEAEVLHLTEELAVSERQKRQAQQE 1727
Cdd:pfam05667 458 ELREKIKEVAEEAKQKEELYKQLVAE 483
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1714-1947 |
2.61e-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: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1714 LAVSERQKRQAQQERDEiademvssssgknvLSEEKRRLDARVNQLEEDLEEEQTNNELLTERLRKTALQVETLTVQLQG 1793
Cdd:COG4942 15 AAAQADAAAEAEAELEQ--------------LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1794 ERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIaNKLMRKTEKKLKEVM 1873
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2414917124 1874 MQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEEN----SRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLS 1947
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERqkllARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
871-1692 |
2.79e-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: 49.66 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 871 EIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGELETRLE 950
Cdd:TIGR00606 313 TVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 951 EEEERGV--QLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNE 1028
Cdd:TIGR00606 393 KNFHTLVieRQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1029 VtdqLTEEEEKTKSLNKLKNKQEAviADLEERLKREEQGRLEQEKFKRRMESEAmeaqEQLSDLGMLSSDLRGSLAQKEK 1108
Cdd:TIGR00606 473 I---LELDQELRKAERELSKAEKN--SLTETLKKEVKSLQNEKADLDRKLRKLD----QEMEQLNHHTTTRTQMEMLTKD 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1109 EITSLQgRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRS 1188
Cdd:TIGR00606 544 KMDKDE-QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLS 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1189 RREAELSELQRCVEEETRrhetqlselrvkhsaaLDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSES 1268
Cdd:TIGR00606 623 SYEDKLFDVCGSQDEESD----------------LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRV 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1269 ERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLH----DARELLQD 1344
Cdd:TIGR00606 687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQkvnrDIQRLKND 766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1345 ESRQKMALASRVRALEEEKN-----GLMERLEEEEERGKELSRQIQTHSQQlTELRKQSEEVNSAVEAGDEIRRKLQREL 1419
Cdd:TIGR00606 767 IEEQETLLGTIMPEEESAKVcltdvTIMERFQMELKDVERKIAQQAAKLQG-SDLDRTVQQVNQEKQEKQHELDTVVSKI 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1420 DSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREK 1499
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1500 ETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDD---------------VGKNVHELERTRRTLETEAQNLR- 1563
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgkddylkqketelntVNAQLEECEKHQEKINEDMRLMRq 1005
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1564 -IQTQELEEELSEAENSRLRLEVTLQALK---AQFEREIstNEEKGEEKRRALSKQVRELE-IQLEEERSQRSQSVSSKK 1638
Cdd:TIGR00606 1006 dIDTQKIQERWLQDNLTLRKRENELKEVEeelKQHLKEM--GQMQVLQMKQEHQKLEENIDlIKRNHVLALGRQKGYEKE 1083
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 1639 QLEAELQEAEAQVETANRGKEEAMKQLRrlqgQMKEVLRELDEAKVTRDDVISQ 1692
Cdd:TIGR00606 1084 IKHFKKELREPQFRDAEEKYREMMIVMR----TTELVNKDLDIYYKTLDQAIMK 1133
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1102-1334 |
2.94e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1102 SLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVEnergmreRAEKQRRDLSEELEALRTELEdtldstA 1181
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-------ELQAELEALQAEIDKLQAEIA------E 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1182 AQQELRSRREaELSELQRcVEEETRRHETQLSELRVKHSAA-----LDSLQEQLDNSKRARQSLEKAKATLEEERQNLTS 1256
Cdd:COG3883 77 AEAEIEERRE-ELGERAR-ALYRSGGSVSYLDVLLGSESFSdfldrLSALSKIADADADLLEELKADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2414917124 1257 ELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQ 1334
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1007-1362 |
3.16e-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: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1007 TAVEQRER-LGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKfkrRMESeameA 1085
Cdd:pfam10174 334 TAKEQRAAiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQK---KIEN----L 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1086 QEQLSDlgmlssdlrgslaqKEKEITSLQGR---LEEEGARRTEAQRSLREALSQvselKEEV-ENERGMRERAEKQRRd 1161
Cdd:pfam10174 407 QEQLRD--------------KDKQLAGLKERvksLQTDSSNTDTALTTLEEALSE----KERIiERLKEQREREDRERL- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1162 lsEELEALRTELEDTLDSTAAQQELRSRREAELSELQrcveeetrRHETQLSELRVKHSAALDSL----QEQLDNSKRAR 1237
Cdd:pfam10174 468 --EELESLKKENKDLKEKVSALQPELTEKESSLIDLK--------EHASSLASSGLKKDSKLKSLeiavEQKKEECSKLE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1238 QSLEKAKATLEEERQN--LTSELKSLqasrsESERGRKRAD-NQLQELSARLAQADREREDREERMHKLQCEIESLSGNL 1314
Cdd:pfam10174 538 NQLKKAHNAEEAVRTNpeINDRIRLL-----EQEVARYKEEsGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQ 612
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2414917124 1315 SSSDSKSLRLAKEISSLESQlhDARELLQDESRQKMALASRVRALEEE 1362
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKK--KGAQLLEEARRREDNLADNSQQLQLE 658
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
864-1145 |
3.54e-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: 49.30 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 864 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLG 943
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 944 ELETR-----LEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKE 1018
Cdd:TIGR02169 776 KLEEAlndleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1019 ----KKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRM---ESEAMEAQEQLSD 1091
Cdd:TIGR02169 856 ienlNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLselKAKLEALEEELSE 935
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1092 LG-------------MLSSDLRGSLAQKEKEITSL-----------------QGRLEEEGARRTEAQRSLREALSQVSEL 1141
Cdd:TIGR02169 936 IEdpkgedeeipeeeLSLEDVQAELQRVEEEIRALepvnmlaiqeyeevlkrLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
....
gi 2414917124 1142 KEEV 1145
Cdd:TIGR02169 1016 KREV 1019
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1112-1352 |
3.91e-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: 48.48 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1112 SLQGRLEEEGARRTEAQRSLREALSQvseLKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRRE 1191
Cdd:pfam05667 230 GLASRLTPEEYRKRKRTKLLKRIAEQ---LRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1192 AELSELQRCVEEETRRHETQlSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERG 1271
Cdd:pfam05667 307 QFTNEAPAATSSPPTKVETE-EELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1272 RKR----------ADNQLQELSARLAQADREREDREERMHK----LQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHD 1337
Cdd:pfam05667 386 YKVkkktldllpdAEENIAKLQALVDASAQRLVELAGQWEKhrvpLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKE 465
|
250
....*....|....*
gi 2414917124 1338 ArellQDESRQKMAL 1352
Cdd:pfam05667 466 V----AEEAKQKEEL 476
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
820-1288 |
4.04e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.03 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 820 SRKAFLKKQQQLSALRVMQRncAAYLKLrnwQWWRLFTKVKPLLQVTRQDEEIQTReaaLQKAKEQLTRAEQDYTeldKK 899
Cdd:PRK10246 269 ALAAEEKAQPQLAALSLAQP--ARQLRP---HWERIQEQSAALAHTRQQIEEVNTR---LQSTMALRARIRHHAA---KQ 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 900 HAQLLEEKAVLADQLQAEAELFAEAEEM---RARLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQ 976
Cdd:PRK10246 338 SAELQAQQQSLNTWLAEHDRFRQWNNELagwRAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 977 LEEEESARQRLLlekvTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLteeEEKTKSLNKLKN--KQEAVI 1054
Cdd:PRK10246 418 HAEQRPLRQRLV----ALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRY---KEKTQQLADVKTicEQEARI 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1055 ADLEerlkrEEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSDLRgsLAQKEKEITSLQgrleEEGArrteAQRSLREA 1134
Cdd:PRK10246 491 KDLE-----AQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSR--LDALEKEVKKLG----EEGA----ALRGQLDA 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1135 LSQvselkeevenergMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRsrreaelSELQRCVEEETrRHETQLSE 1214
Cdd:PRK10246 556 LTK-------------QLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQ-------DDIQPWLDAQE-EHERQLRL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1215 LRVKH--SAALDSLQEQLdnsKRARQSLEKAKATLEEERQNLT-------SELKSLQASRSESERGRKRaDNQLQELSAR 1285
Cdd:PRK10246 615 LSQRHelQGQIAAHNQQI---IQYQQQIEQRQQQLLTALAGYAltlpqedEEASWLATRQQEAQSWQQR-QNELTALQNR 690
|
...
gi 2414917124 1286 LAQ 1288
Cdd:PRK10246 691 IQQ 693
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1146-1404 |
4.09e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1146 ENERGMRERAEKQRRDLSEELEALRTELEdtldstAAQQELRS-RREAELSELqrcvEEETRRHETQLSELRvkhsAALD 1224
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELE------EAEAALEEfRQKNGLVDL----SEEAKLLLQQLSELE----SQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1225 SLQEQLDNSKRARQSLEKAKATLEEERQNLTselkslqasrsesergrkrADNQLQELSARLAQADReredreermhklq 1304
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPELL-------------------QSPVIQQLRAQLAELEA------------- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1305 cEIESLSGNLSSSDSKSLRLAKEISSLESQLHD-ARELLQDESRQKMALASRVRALEEEKNGL---MERLEEEEERGKEL 1380
Cdd:COG3206 278 -ELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLearLAELPELEAELRRL 356
|
250 260
....*....|....*....|....
gi 2414917124 1381 SRQIQTHSQQLTELRKQSEEVNSA 1404
Cdd:COG3206 357 EREVEVARELYESLLQRLEEARLA 380
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1107-1362 |
4.15e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.99 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1107 EKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEAL---RTELEDTLDSTaaQ 1183
Cdd:pfam00038 53 EKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEAtlaRVDLEAKIESL--K 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1184 QELRSRR---EAELSELQRCVEEETRRHETQLSeLRVKHSAALDSLQEQLDN-SKRARQSLEKA-KATLEEERQNLTSEL 1258
Cdd:pfam00038 131 EELAFLKknhEEEVRELQAQVSDTQVNVEMDAA-RKLDLTSALAEIRAQYEEiAAKNREEAEEWyQSKLEELQQAAARNG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1259 KSLQASRSESERGRKradnQLQELSARLAQADREREDREERMHKLQceiESLSGNLSSSDSKslrlakeISSLESQLHDA 1338
Cdd:pfam00038 210 DALRSAKEEITELRR----TIQSLEIELQSLKKQKASLERQLAETE---ERYELQLADYQEL-------ISELEAELQET 275
|
250 260
....*....|....*....|....
gi 2414917124 1339 RELLQDESRQKMALASRVRALEEE 1362
Cdd:pfam00038 276 RQEMARQLREYQELLNVKLALDIE 299
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1083-1258 |
4.38e-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: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1083 MEAQEQLSDLGMLSSDLRGSLAQKE---KEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQR 1159
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKelpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1160 RDLS--EELEALRTELEdtldstaAQQELRSRREAELSELqrcvEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRAR 1237
Cdd:COG1579 83 GNVRnnKEYEALQKEIE-------SLKRRISDLEDEILEL----MERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|.
gi 2414917124 1238 QSLEKAKATLEEERQNLTSEL 1258
Cdd:COG1579 152 AELEAELEELEAEREELAAKI 172
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1019-1288 |
5.13e-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: 48.42 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1019 KKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQgrleqekfKRRMESEAMEAQEQLSdlgmlSSD 1098
Cdd:COG5185 256 EKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTK--------SIDIKKATESLEEQLA-----AAE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1099 LRGSLAQKEKEITSLQGRLEEEGARRteaQRSLREALSQVSELKEEVENERGMRERAEKQrRDLSEELEALRTEL-EDTL 1177
Cdd:COG5185 323 AEQELEESKRETETGIQNLTAEIEQG---QESLTENLEAIKEEIENIVGEVELSKSSEEL-DSFKDTIESTKESLdEIPQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1178 DSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKhSAALDSLQEQLDnsKRARQSLEKAKATLEEERQNLTSE 1257
Cdd:COG5185 399 NQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEV-SKLLNELISELN--KVMREADEESQSRLEEAYDEINRS 475
|
250 260 270
....*....|....*....|....*....|.
gi 2414917124 1258 LKSlqaSRSESERGRKRADNQLQELSARLAQ 1288
Cdd:COG5185 476 VRS---KKEDLNEELTQIESRVSTLKATLEK 503
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1039-1194 |
6.28e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.27 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1039 KTKSLNKLkNKQeavIADLEERLKREEQGrleqekfkrrmeSEAMEAQeqlsdlgmlSSDLRGSLAQKEKEITSLQGRLE 1118
Cdd:PRK09039 51 KDSALDRL-NSQ---IAELADLLSLERQG------------NQDLQDS---------VANLRASLSAAEAERSRLQALLA 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2414917124 1119 EEGARRTEAQRslrealsQVSELKEEVENERGMRERAEKQRRDLSEELEALRTEL---EDTLDSTAAQQELRSRREAEL 1194
Cdd:PRK09039 106 ELAGAGAAAEG-------RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLaalEAALDASEKRDRESQAKIADL 177
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
985-1218 |
6.50e-05 |
|
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: 47.33 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 985 QRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIAD-------L 1057
Cdd:pfam04849 90 QSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHgcvqldaL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1058 EERLKR--EEQGRLEQEKFKRRMESEAMEAQEQlsdlgMLSSDLRGSLAQKEKEItslqGRLEEEGARRTEAQRSLREA- 1134
Cdd:pfam04849 170 QEKLRGleEENLKLRSEASHLKTETDTYEEKEQ-----QLMSDCVEQLSEANQQM----AELSEELARKMEENLRQQEEi 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1135 ---LSQVSELkeevenergmreraEKQRRDLSEELEALRTELEDTLDstaAQQELRSrreaELSELQ-RCVEEETRRHET 1210
Cdd:pfam04849 241 tslLAQIVDL--------------QHKCKELGIENEELQQHLQASKE---AQRQLTS----ELQELQdRYAECLGMLHEA 299
|
250
....*....|
gi 2414917124 1211 Q--LSELRVK 1218
Cdd:pfam04849 300 QeeLKELRKK 309
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
961-1262 |
6.50e-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: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 961 NEKKKMQQNIQDLEEQLEEEESARQRlllekvtLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKT 1040
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKLNQQ-------KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1041 KSLNKLKNKQEAVIADLEERLKREEQgrlEQEKFKRRMESEameaQEQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEE 1120
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKQ---NLEQKQKELKSK----EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1121 GARRTEAQRSLREALSQVSELKEEVEnergmRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRC 1200
Cdd:TIGR04523 530 ESEKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2414917124 1201 VEEETrrhetqlselrvkhsAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQ 1262
Cdd:TIGR04523 605 IEEKE---------------KKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
996-1335 |
7.08e-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: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 996 TKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREeqgrleqekfk 1075
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN----------- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1076 RRMESEAMEAQEQLSDLgmlssdlrgslaqkEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERA 1155
Cdd:TIGR04523 214 KSLESQISELKKQNNQL--------------KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1156 EKQRRDLSEELEALRTELEDTldSTAAQQELRSRREAELSELQRCVEE---ETRRHETQLSELR---------VKHSAAL 1223
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDL--NNQKEQDWNKELKSELKNQEKKLEEiqnQISQNNKIISQLNeqisqlkkeLTNSESE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1224 DS-LQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHK 1302
Cdd:TIGR04523 358 NSeKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
330 340 350
....*....|....*....|....*....|...
gi 2414917124 1303 LQCEIESLSGNLSSSDSKSLRLAKEISSLESQL 1335
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
958-1145 |
7.10e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 958 QLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQL---- 1033
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaell 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1034 ---------------------TEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDL 1092
Cdd:COG4942 111 ralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2414917124 1093 GMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEV 1145
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1539-1734 |
8.72e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1539 DDVGKNVHELERTRRTLETEAQNLRIQTQELEEELSEAENsRLRLEVtLQALKAQFEREistneeKGEEKRRALSKQVRE 1618
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAA-RERLAE-LEYLRAALRLW------FAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1619 LEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMK-QLRRLQGQMKEVLRELD-----------EAKVTR 1686
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLErEIERLERELEERERRRArleallaalglPLPASA 379
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2414917124 1687 DDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADE 1734
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| 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 2414917124 675 YKESLTKLMATLRNTNPNFLRCIIP 699
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
994-1264 |
9.00e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 994 LETKVKSLETDLATA---VEQRERLGKEKKQLEERLNEVTDQLTEeeeKTKSLNKLKNKQEAVIAdleERLKREEQGRLE 1070
Cdd:PRK11281 54 LEAEDKLVQQDLEQTlalLDKIDRQKEETEQLKQQLAQAPAKLRQ---AQAELEALKDDNDEETR---ETLSTLSLRQLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1071 QEKFKRRmeSEAMEAQEQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEE----------EGARRTEAQRSLREA----LS 1136
Cdd:PRK11281 128 SRLAQTL--DQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQirnllkggkvGGKALRPSQRVLLQAeqalLN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1137 QVSEL-KEEVENERGMRERAEKQRRDLSEELEALRTELEDTldstaaqQELRSRREAELSELQrcVEEETRRHET----- 1210
Cdd:PRK11281 206 AQNDLqRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLL-------QEAINSKRLTLSEKT--VQEAQSQDEAariqa 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2414917124 1211 ------------QLSELRVKHSAALDSLQEQldnSKRARQSLEKAKATleeeRQNLTSELKSLQAS 1264
Cdd:PRK11281 277 nplvaqeleinlQLSQRLLKATEKLNTLTQQ---NLRVKNWLDRLTQS----ERNIKEQISVLKGS 335
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1505-1928 |
9.33e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1505 ALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGknvhELERTRRTLETEAQNlriqtqeleeelseaenSRLRLE 1584
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQA-----------------ASDHLN 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1585 VTLQALKAQfereistneEKGEEKRRALSkqvrELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRG---KEEA 1661
Cdd:PRK04863 339 LVQTALRQQ---------EKIERYQADLE----ELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladYQQA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1662 MKQLRRLQGQMKEVLRELDEAK-------VTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSE---RQKRQAQQERDEI 1731
Cdd:PRK04863 406 LDVQQTRAIQYQQAVQALERAKqlcglpdLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQaahSQFEQAYQLVRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1732 ADEMVSS---SSGKNVL--SEEKRRLDARVNQLEEDLE--EEQTNNELLTERLRKTALQVetLTVQLQGERTLAQKAEAA 1804
Cdd:PRK04863 486 AGEVSRSeawDVARELLrrLREQRHLAEQLQQLRMRLSelEQRLRQQQRAERLLAEFCKR--LGKNLDDEDELEQLQEEL 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1805 REQLEKQNKELkarlgEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEvmmqaederrhad 1884
Cdd:PRK04863 564 EARLESLSESV-----SEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFED------------- 625
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2414917124 1885 qyREQLDKSMvrlKQLKRQLEEVEEENSRSSAQKRKLQRELEEL 1928
Cdd:PRK04863 626 --SQDVTEYM---QQLLERERELTVERDELAARKQALDEEIERL 664
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
995-1245 |
9.41e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 995 ETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREeqgrleQEKF 1074
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER------REEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1075 KRRMESeameAQEQLSDLGMLSSdLRGSlaqkeKEITSLQGRLEeegaRRTEAQRSLREALSQVSELKEEVENERgmrER 1154
Cdd:COG3883 89 GERARA----LYRSGGSVSYLDV-LLGS-----ESFSDFLDRLS----ALSKIADADADLLEELKADKAELEAKK---AE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1155 AEKQRrdlsEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSK 1234
Cdd:COG3883 152 LEAKL----AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250
....*....|.
gi 2414917124 1235 RARQSLEKAKA 1245
Cdd:COG3883 228 AAAAAAAAAAA 238
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
983-1146 |
1.04e-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: 46.07 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 983 ARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKtksLNKLKNKQEAVIADLEERLK 1062
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNVRNNKEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1063 REEQGRLEQEkfkrrmESEAMEAQEQlsdlgmlssdLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELK 1142
Cdd:COG1579 102 KRRISDLEDE------ILELMERIEE----------LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....
gi 2414917124 1143 EEVE 1146
Cdd:COG1579 166 EELA 169
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
995-1269 |
1.19e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 47.06 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 995 ETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEK--TKSLNKLKNKQEAVIADLEERLK-------REE 1065
Cdd:pfam09731 160 KAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQseEEAAPPLLDAAPETPPKLPEHLDnveekveKAQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1066 QGRLEQEKFKRRMESEAMEAQEQLS------------DLGMLSSDLRGSLAQKEKEITSLQGRLEEEGAR---------- 1123
Cdd:pfam09731 240 SLAKLVDQYKELVASERIVFQQELVsifpdiipvlkeDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKReekhierale 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1124 -RTEAQRSLREALSQ-------VSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAeLS 1195
Cdd:pfam09731 320 kQKEELDKLAEELSArleevraADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREF-LQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1196 ELQRCVEEETRRHETQLSEL--RVKH-SAALDSLQEQLDNSKRARQ---SLEKAKATLE-----EERQNLTSELKSLQAS 1264
Cdd:pfam09731 399 DIKEKVEEERAGRLLKLNELlaNLKGlEKATSSHSEVEDENRKAQQlwlAVEALRSTLEdgsadSRPRPLVRELKALKEL 478
|
....*
gi 2414917124 1265 RSESE 1269
Cdd:pfam09731 479 ASDDE 483
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1072-1539 |
1.20e-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: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1072 EKFKRRMESEAMEAQEQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGM 1151
Cdd:pfam05557 12 SQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1152 RERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHeTQLSELRVKHSAALDSLQEQLD 1231
Cdd:pfam05557 92 LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKA-SEAEQLRQNLEKQQSSLAEAEQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1232 NSKRARQSLEkakatLEEERQNLTSELKSLQASRSESERGRKRadnqLQELSARLAQADREREDREERMHKLQCEIESLS 1311
Cdd:pfam05557 171 RIKELEFEIQ-----SQEQDSEIVKNSKSELARIPELEKELER----LREHNKHLNENIENKLLLKEEVEDLKRKLEREE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1312 GnlssSDSKSLRLAKEISSLESQLHDARELLQD---ESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHS 1388
Cdd:pfam05557 242 K----YREEAATLELEKEKLEQELQSWVKLAQDtglNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1389 QQLTELRKQSEEVNSAVEAGDEIRRKLQRELD---------SAIQRERQKEEEKERVERQRERLREEIEDMTIALQR--- 1456
Cdd:pfam05557 318 QELAQYLKKIEDLNKKLKRHKALVRRLQRRVLlltkerdgyRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAhne 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1457 --ERQNCTALEKRQKKFDQCLAEEKAVSARLAEErdrAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQL 1534
Cdd:pfam05557 398 emEAQLSVAEEELGGYKQQAQTLERELQALRQQE---SLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERR 474
|
....*
gi 2414917124 1535 VNQQD 1539
Cdd:pfam05557 475 CLQGD 479
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1153-1947 |
1.22e-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: 47.35 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1153 ERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQrCVEEETRRHETQLSEL--RVKHSAALDSLQEQL 1230
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLE-SSREIVKSYENELDPLknRLKEIEHNLSKIMKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1231 DNSKRARQSLEKakatleeERQNLTSELKSLQasrsesERGRKRADNQLQELSARLAQADREREDREERMHKlqcEIESL 1310
Cdd:TIGR00606 268 DNEIKALKSRKK-------QMEKDNSELELKM------EKVFQGTDEQLNDLYHNHQRTVREKERELVDCQR---ELEKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1311 SGNLSSSDSKSLRLAKEIS--SLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHS 1388
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGrlQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1389 QQLTELrkqSEEVNSAVEAGDEIRRKlQRELDSAIQRERQKEEEKERVERQRerlreeiedmtialQRERQNCTALEKRQ 1468
Cdd:TIGR00606 412 QLCADL---QSKERLKQEQADEIRDE-KKGLGRTIELKKEILEKKQEELKFV--------------IKELQQLEGSSDRI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1469 KKFDQCLAEEKAvsaRLAEERDRAEADSREKETRCLalsralqeaQDQKEELERANKQLRLEMEQLvNQQDDVGKNVHEL 1548
Cdd:TIGR00606 474 LELDQELRKAER---ELSKAEKNSLTETLKKEVKSL---------QNEKADLDRKLRKLDQEMEQL-NHHTTTRTQMEML 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1549 ERTRRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALkaqfereiSTNEEKGEEKRRALSKQVRELE-----IQL 1623
Cdd:TIGR00606 541 TKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSK--------SKEINQTRDRLAKLNKELASLEqnknhINN 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1624 EEERSQRSQSVSSKKQLEA-ELQEAEAQVETANRGKEEAMKQLRRLQGQ-------MKEVLRELDEAKVTRDDVISQSKD 1695
Cdd:TIGR00606 613 ELESKEEQLSSYEDKLFDVcGSQDEESDLERLKEEIEKSSKQRAMLAGAtavysqfITQLTDENQSCCPVCQRVFQTEAE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1696 SEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARvNQLEEDLEEEQTNNELLTE 1775
Cdd:TIGR00606 693 LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNK-LQKVNRDIQRLKNDIEEQE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1776 RLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGavrgkhRMSVAALEAKIEtmeeqleqerqer 1855
Cdd:TIGR00606 772 TLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDL------DRTVQQVNQEKQ------------- 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1856 aianklmrKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEensrSSAQKRKLQRELEELTDSSQTM 1935
Cdd:TIGR00606 833 --------EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGT----NLQRRQQFEEQLVELSTEVQSL 900
|
810
....*....|..
gi 2414917124 1936 NREISSLRNQLS 1947
Cdd:TIGR00606 901 IREIKDAKEQDS 912
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1457-1754 |
1.39e-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: 47.04 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1457 ERQNCTALEKRQKKFDQC----LAEEKAVSARLAEERDRAEA--DSREKETRCLALSRALQE--AQDQKEELERANKQLR 1528
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMeqerLRQEKEEKAREVERRRKLEEaeKARQAEMDRQAAIYAEQErmAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1529 -LEMEQLVNQQDDVG-KNVHELERTRrtLETEAQNLRIqtqeleeelseaensRLRLEVTLQALKAQFEREISTNEEKGE 1606
Cdd:pfam17380 359 kRELERIRQEEIAMEiSRMRELERLQ--MERQQKNERV---------------RQELEAARKVKILEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1607 -EKRRALSKQVRELEIQ-LEEERSQRSQSVSSK-----------KQLEAELQEAEAQVETANRGKEEAMKQLRR-LQGQM 1672
Cdd:pfam17380 422 mEQIRAEQEEARQREVRrLEEERAREMERVRLEeqerqqqverlRQQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKEL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1673 KEVLRELDEAKVTRDDVISQSKDSEKKIqtLEAEVLHLTEElavsERQKRQAQQERDEIADEMvssssgkNVLSEEKRRL 1752
Cdd:pfam17380 502 EERKQAMIEEERKRKLLEKEMEERQKAI--YEEERRREAEE----ERRKQQEMEERRRIQEQM-------RKATEERSRL 568
|
..
gi 2414917124 1753 DA 1754
Cdd:pfam17380 569 EA 570
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1034-1289 |
1.52e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1034 TEEEEKTKSLNKLKNKQEAVIADLEErlkreeqgrleqekfkrrMESEAMEAQEQLSDLGMLSSDLRGSLAQKEKEITSL 1113
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDA------------------LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1114 QGRLEEEGARRTEAQRSLREALSQVSELK--------EEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQE 1185
Cdd:COG3883 78 EAEIEERREELGERARALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1186 LRSRREAELSELQRCVEEETRRHETQLSELrvkhSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASR 1265
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQL----SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
250 260
....*....|....*....|....
gi 2414917124 1266 SESERGRKRADNQLQELSARLAQA 1289
Cdd:COG3883 234 AAAAAAAAAAASAAGAGAAGAAGA 257
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1606-1946 |
1.93e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.43 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1606 EEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDEAKVT 1685
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1686 RDDVISQSKDSEKKIQTLEAEVLHLTEELA--------VSERQKRQAQQERDEIADEMvSSSSGKNVLSEEKRRLDARVN 1757
Cdd:pfam07888 117 KDALLAQRAAHEARIRELEEDIKTLTQRVLeretelerMKERAKKAGAQRKEEEAERK-QLQAKLQQTEEELRSLSKEFQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1758 QLEEDLEEEQTNnellterlrktALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEgavrgkhrMSVAAL 1837
Cdd:pfam07888 196 ELRNSLAQRDTQ-----------VLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE--------RKVEGL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1838 EAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSM----VRLKQLKRQLEEVEEENSR 1913
Cdd:pfam07888 257 GEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAeadkDRIEKLSAELQRLEERLQE 336
|
330 340 350
....*....|....*....|....*....|....*..
gi 2414917124 1914 SSAQKRKLQRELEELTDSSQTM----NREISSLRNQL 1946
Cdd:pfam07888 337 ERMEREKLEVELGREKDCNRVQlsesRRELQELKASL 373
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1008-1325 |
1.96e-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: 46.87 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1008 AVEQRERLGKEKKQL---EERLNEVTDQLTEEEEKTKSL-----------NKLKN---KQEAV------IADLEERLkrE 1064
Cdd:COG3096 287 ALELRRELFGARRQLaeeQYRLVEMARELEELSARESDLeqdyqaasdhlNLVQTalrQQEKIeryqedLEELTERL--E 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1065 EQG---------RLEQEKFKRRMESEAMEAQEQLSD----LGMLSS-------------DLRGSLAQKEKEITSLQGRLE 1118
Cdd:COG3096 365 EQEevveeaaeqLAEAEARLEAAEEEVDSLKSQLADyqqaLDVQQTraiqyqqavqaleKARALCGLPDLTPENAEDYLA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1119 EEGARRTEAQRSLREALSQVSELKEEV-ENERGM-----------RERAEKQRRDL----------SEELEALRTELEDt 1176
Cdd:COG3096 445 AFRAKEQQATEEVLELEQKLSVADAARrQFEKAYelvckiageveRSQAWQTARELlrryrsqqalAQRLQQLRAQLAE- 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1177 ldstaAQQELRSRREAE--LSELQRCVEEEtRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNL 1254
Cdd:COG3096 524 -----LEQRLRQQQNAErlLEEFCQRIGQQ-LDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKEL 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1255 TSE----------LKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRL 1324
Cdd:COG3096 598 AARapawlaaqdaLERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRLLAL 677
|
.
gi 2414917124 1325 A 1325
Cdd:COG3096 678 A 678
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
864-1049 |
2.33e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 864 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKK----HAQLLEEKAVLADQLQAEAELFAEAEEMR-------ARLA 932
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEiaelRAELEAQKEELAELLRALYRLGRQPPLALllspedfLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 933 SRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQR 1012
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
170 180 190
....*....|....*....|....*....|....*..
gi 2414917124 1013 ERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNK 1049
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
994-1198 |
2.35e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 994 LETKVKSLETDLATAVEQRER---------LGKEKKQLEERLNEVTDQLTEEEEKTKSLnklknkqEAVIADLEERLKRE 1064
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEA-------EARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1065 EQ--GRLEQEKFKRRMESEAMEAQEQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGAR-RTEAQRSLREALSQVSEL 1141
Cdd:COG3206 253 PDalPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRiLASLEAELEALQAREASL 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1142 KEEVENERGMRER---AEKQRRDLSEELEALRTELEDTLdstAAQQELRSRREAELSELQ 1198
Cdd:COG3206 333 QAQLAQLEARLAElpeLEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVGNVR 389
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1488-1687 |
2.52e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1488 ERDRAEADSREK--ETRCLALSRALQEAQDQKEELERANK--QLRLEMEQLVNQQDDVGKNVHELERTRRTLETEAQNLR 1563
Cdd:COG3206 167 ELRREEARKALEflEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1564 IQTQELEEELSEAENSRL--RLEVTLQALKAQfEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQsvsskkQLE 1641
Cdd:COG3206 247 AQLGSGPDALPELLQSPViqQLRAQLAELEAE-LAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA------SLE 319
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2414917124 1642 AELQEAEAQVETANRGKEEAMKQLRRLQGQMKEvLRELD-EAKVTRD 1687
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLErEVEVARE 365
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1598-1928 |
2.66e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1598 ISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLR 1677
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1678 ELDEAKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVN 1757
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1758 QLEEDLEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAAL 1837
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1838 EAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQ 1917
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
330
....*....|.
gi 2414917124 1918 KRKLQRELEEL 1928
Cdd:COG4372 349 GLLDNDVLELL 359
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
864-1669 |
2.88e-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: 46.19 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 864 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLleeKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLG 943
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEI---KALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 944 ELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLE 1023
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1024 ERL--NEVTDQLTEEEEKTKSLNKLKNKQEAviadlEERLKREEQGRLEQEK--FKRRMESEAMEAQEQLSDLGMLSSDL 1099
Cdd:TIGR00606 389 ERQikNFHTLVIERQEDEAKTAAQLCADLQS-----KERLKQEQADEIRDEKkgLGRTIELKKEILEKKQEELKFVIKEL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1100 RgSLAQKEKEITSLqgrleEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEdtlds 1179
Cdd:TIGR00606 464 Q-QLEGSSDRILEL-----DQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTT----- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1180 TAAQQELRSRREAELSElqrcveeetrrhetQLSELRVKHSAALDSLQEQLDNSKRARQ---SLEKAKATLEEERQNLTS 1256
Cdd:TIGR00606 533 TRTQMEMLTKDKMDKDE--------------QIRKIKSRHSDELTSLLGYFPNKKQLEDwlhSKSKEINQTRDRLAKLNK 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1257 ELKSLQASRSESERGRKRADNQLQELSARLAQAdREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLH 1336
Cdd:TIGR00606 599 ELASLEQNKNHINNELESKEEQLSSYEDKLFDV-CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQ 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1337 DARELLQDESRQKMALASRVRALEeekNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQ 1416
Cdd:TIGR00606 678 SCCPVCQRVFQTEAELQEFISDLQ---SKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1417 ---RELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQnctaLEKRQKKFDQCLAEEKAVSARLAEERDRAE 1493
Cdd:TIGR00606 755 kvnRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQME----LKDVERKIAQQAAKLQGSDLDRTVQQVNQE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1494 ADSREKETRclALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHElertRRTLETEAQNLRIQTQELEEEL 1573
Cdd:TIGR00606 831 KQEKQHELD--TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR----RQQFEEQLVELSTEVQSLIREI 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1574 SEAENSRLRLEVTLQALKAQFEREISTNEE---KGEEKRRALSKQVRELEIQLEE-ERSQRSQSVSSKKQLEAELQEAEA 1649
Cdd:TIGR00606 905 KDAKEQDSPLETFLEKDQQEKEELISSKETsnkKAQDKVNDIKEKVKNIHGYMKDiENKIQDGKDDYLKQKETELNTVNA 984
|
810 820
....*....|....*....|
gi 2414917124 1650 QVETANRGKEEAMKQLRRLQ 1669
Cdd:TIGR00606 985 QLEECEKHQEKINEDMRLMR 1004
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1606-1734 |
2.93e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1606 EEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQG--QMKEVLRELDEAK 1683
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLK 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2414917124 1684 VTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADE 1734
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
883-1548 |
2.98e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.98 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 883 KEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEAELFAEAEemrARLASRKQELEEVLGELETRLEEEEERGVQLANE 962
Cdd:pfam12128 215 KSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAE---LRLSHLHFGYKSDETLIASRQEERQETSAELNQL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 963 KKKMQQNIQDLeeqleeeesaRQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEK----KQLEERLNEVTDQLTEEEE 1038
Cdd:pfam12128 292 LRTLDDQWKEK----------RDELNGELSAADAAVAKDRSELEALEDQHGAFLDADietaAADQEQLPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1039 KTKSL----NKLKNKQEAVIADLEERLKREEQGrLEQEKFKRRmESEAMEAQEQLSDLGMLSSDLRGSLAQKEKEITSLQ 1114
Cdd:pfam12128 362 RLKALtgkhQDVTAKYNRRRSKIKEQNNRDIAG-IKDKLAKIR-EARDRQLAVAEDDLQALESELREQLEAGKLEFNEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1115 GRLEeegarrtEAQRSLREALSQVSELKEEVENERGMRERAEKQRrdlsEELEALRTELEDTLDSTAAqqeLRSRREAEL 1194
Cdd:pfam12128 440 YRLK-------SRLGELKLRLNQATATPELLLQLENFDERIERAR----EEQEAANAEVERLQSELRQ---ARKRRDQAS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1195 SELQRCvEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRA-RQSLEKAKATLEEERQNLTSELKSLQASRSESERGRK 1273
Cdd:pfam12128 506 EALRQA-SRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDwEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1274 RADNQL---------QELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDskslrlaKEISSLESQLHDARELLQD 1344
Cdd:pfam12128 585 LDLKRIdvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS-------REETFARTALKNARLDLRR 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1345 ESRQKMALASRV-RALEEEKNGLMERLEEEEERGKELSRQIQTHSQ----QLTELRKQSEEVNSAVE-AGDEIRRKLQRE 1418
Cdd:pfam12128 658 LFDEKQSEKDKKnKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeqkeQKREARTEKQAYWQVVEgALDAQLALLKAA 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1419 LDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAE-EKAVSARLAEERDRAEADSR 1497
Cdd:pfam12128 738 IAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRyFDWYQETWLQRRPRLATQLS 817
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2414917124 1498 EKETrclALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHEL 1548
Cdd:pfam12128 818 NIER---AISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGL 865
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
959-1720 |
3.40e-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: 45.88 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 959 LANEKKKMQQNIQDLeeqleeeesarqrllleKVTLETKVKSLETdlataveqrerlgkeKKQLEErlnevtDQLTEEEE 1038
Cdd:pfam15921 129 MADIRRRESQSQEDL-----------------RNQLQNTVHELEA---------------AKCLKE------DMLEDSNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1039 KTKSLNKLKNKQEAVIADLEERLKreeqgRLEQEKFKRRMESEAMEAQEQLSdlgmLSSDLRGSLAQKEKEITSLQGRL- 1117
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSILV-----DFEEASGKKIYEHDSMSTMHFRS----LGSAISKILRELDTEISYLKGRIf 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1118 ---EEEGARRTEAQRSLREALSQVSELKEEVENER-----GMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSR 1189
Cdd:pfam15921 242 pveDQLEALKSESQNKIELLLQQHQDRIEQLISEHeveitGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1190 REAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEqldnSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESE 1269
Cdd:pfam15921 322 LESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTE----ARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1270 RGRKR-----------ADNQLQELSARLAQADREREDREERMHKLQCEIESlsgNLSSSDSKSLRLAKeISSLESQLHDA 1338
Cdd:pfam15921 398 EQNKRlwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMER---QMAAIQGKNESLEK-VSSLTAQLEST 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1339 RELL----QDESRQKMALASRVRALEEEKNGLmerleeeeergKELSRQIQTHSQQLTELRKQS----EEVNSAVEAGDE 1410
Cdd:pfam15921 474 KEMLrkvvEELTAKKMTLESSERTVSDLTASL-----------QEKERAIEATNAEITKLRSRVdlklQELQHLKNEGDH 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1411 IrRKLQRELDSaiqrerqKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERD 1490
Cdd:pfam15921 543 L-RNVQTECEA-------LKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKD 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1491 RAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQ----QDDVGKNVHELERTRRTLETEAQNLRIQT 1566
Cdd:pfam15921 615 KKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEvktsRNELNSLSEDYEVLKRNFRNKSEEMETTT 694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1567 QELEEELSEAENSRLRLEVTLQALKAQ--FEREISTNEEKGEEKRRAlskQVRELEIQLEEERSQRSQSVSSKKQLEAEL 1644
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTLKSMEGSdgHAMKVAMGMQKQITAKRG---QIDALQSKIQFLEEAMTNANKEKHFLKEEK 771
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2414917124 1645 QEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDEAKVTRDDVISQSKDSEKKIQTLEAEV--LHLTEELAVSERQ 1720
Cdd:pfam15921 772 NKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESvrLKLQHTLDVKELQ 849
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1221-1366 |
3.49e-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: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1221 AALDSLQE---QLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLA--QADRERED 1295
Cdd:COG1579 7 RALLDLQEldsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyEEQLGNVR 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2414917124 1296 REERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQ----KMALASRVRALEEEKNGL 1366
Cdd:COG1579 87 NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekKAELDEELAELEAELEEL 161
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1008-1281 |
4.14e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1008 AVEQRERLgkekKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRleQEKFKRRMEsEAMEAQE 1087
Cdd:pfam02029 15 AREERRRQ----KEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKR--EERRQKRLQ-EALERQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1088 QLSDLGMLSSD-----------LRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAE 1156
Cdd:pfam02029 88 EFDPTIADEKEsvaerkenneeEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1157 KQRRDLSEE----LEALRTELEDTLDSTAAQQELRSRRE-----AELSELQRCVEEETRRHETQLSELRVKHSAALDSLQ 1227
Cdd:pfam02029 168 EVPTENFAKeevkDEKIKKEKKVKYESKVFLDQKRGHPEvksqnGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAE 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 1228 EQLDNSKRARQSLEKAKAT-LEEERQNLTSELKSLQASR-------SESERGRK--RADNQLQE 1281
Cdd:pfam02029 248 QKLEELRRRRQEKESEEFEkLRQKQQEAELELEELKKKReerrkllEEEEQRRKqeEAERKLRE 311
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
982-1283 |
4.21e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 45.70 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 982 SARQRLLLEKVTLETKvKSLETDLATAVEQRERlGKEKKQLEERLnevtdQLTEEEEKTKSL-NKLKNKQEAVIAdLEER 1060
Cdd:PLN03188 1012 SARKRNSLLKLTYSCE-PSQAPPLNTIPESTDE-SPEKKLEQERL-----RWTEAESKWISLaEELRTELDASRA-LAEK 1083
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1061 LKREeqgrLEQEKFKRRMESEAMEAQ--------EQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAqRSLR 1132
Cdd:PLN03188 1084 QKHE----LDTEKRCAEELKEAMQMAmegharmlEQYADLEEKHIQLLARHRRIQEGIDDVKKAAARAGVRGAES-KFIN 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1133 EALSQVSELKEEvenergmrerAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSR-REAE--LSELQRC---VEEETR 1206
Cdd:PLN03188 1159 ALAAEISALKVE----------REKERRYLRDENKSLQAQLRDTAEAVQAAGELLVRlKEAEeaLTVAQKRamdAEQEAA 1228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2414917124 1207 RHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSEL-KSLQASRSESERGRKRADNQLQELS 1283
Cdd:PLN03188 1229 EAYKQIDKLKRKHENEISTLNQLVAESRLPKEAIRPACNDDCMAKYDAGEPLsEGDQQWREEFEPFYKKEDGELSKLA 1306
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1154-1534 |
4.39e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1154 RAEKQRRDLSEELEALRTELEDTLDSTAAQQELrsrreaeLSELQRCVEEETRRhetqLSELRVKHSAALDSL------- 1226
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYR-------LVEMARELAELNEA----ESDLEQDYQAASDHLnlvqtal 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1227 --QEQLdnsKRARQSLEKAKATLEEerQNLTSELKSLQasRSESERGRKRADNQLQELSARLA----------------- 1287
Cdd:PRK04863 345 rqQEKI---ERYQADLEELEERLEE--QNEVVEEADEQ--QEENEARAEAAEEEVDELKSQLAdyqqaldvqqtraiqyq 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1288 QADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLqDESRQKMALA-------SRVRALE 1360
Cdd:PRK04863 418 QAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAH-SQFEQAYQLVrkiagevSRSEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1361 EEKNGLmerleEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQR 1440
Cdd:PRK04863 497 VARELL-----RRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1441 ERLREEIEDMTiALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEEL 1520
Cdd:PRK04863 572 ESVSEARERRM-ALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDEL 650
|
410
....*....|....
gi 2414917124 1521 ERANKQLRLEMEQL 1534
Cdd:PRK04863 651 AARKQALDEEIERL 664
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
867-1124 |
4.81e-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: 45.11 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 867 RQDEEIQTREAALQKAK-EQLTRAEQDYTELDKKHAQLLEekAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGEL 945
Cdd:pfam17380 360 RELERIRQEEIAMEISRmRELERLQMERQQKNERVRQELE--AARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 946 ETRLEEEEERGVQLANEKKKMQQNIQdlEEQLEEEESARQRLLLEKVtletkvkslETDLATAVEQRerlgkeKKQLEER 1025
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVE--RLRQQEEERKRKKLELEKE---------KRDRKRAEEQR------RKILEKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1026 LNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRmeseamEAQEQLsdlgMLSSDLRGSLAQ 1105
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR------RIQEQM----RKATEERSRLEA 570
|
250
....*....|....*....
gi 2414917124 1106 KEKEITSLQGRLEEEGARR 1124
Cdd:pfam17380 571 MEREREMMRQIVESEKARA 589
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1464-1946 |
5.29e-04 |
|
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: 45.10 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1464 LEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGK 1543
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1544 N-------VHELERTRRTLE----TEAQNLR----------IQTQELEEELSEAENSRLRLEVTLQALKA---------- 1592
Cdd:pfam05483 343 AkaahsfvVTEFEATTCSLEellrTEQQRLEknedqlkiitMELQKKSSELEEMTKFKNNKEVELEELKKilaedeklld 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1593 ---QFER---EISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLR 1666
Cdd:pfam05483 423 ekkQFEKiaeELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENK 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1667 RLQGQMKEVLRELdeaKVTRDDVISQSKDSE---KKIQTLEAEVLHLTEELavsERQKRQAQQERDEIademvssssgkn 1743
Cdd:pfam05483 503 ELTQEASDMTLEL---KKHQEDIINCKKQEErmlKQIENLEEKEMNLRDEL---ESVREEFIQKGDEV------------ 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1744 vlseeKRRLDarvnqleedleEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARlGEME 1823
Cdd:pfam05483 565 -----KCKLD-----------KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK-GSAE 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1824 GAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDK-------SMVR 1896
Cdd:pfam05483 628 NKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKrcqhkiaEMVA 707
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2414917124 1897 L-KQLKRQLEE-VEEENSRSSAQKRKLQreleELTDSSQTMNREISSLRNQL 1946
Cdd:pfam05483 708 LmEKHKHQYDKiIEERDSELGLYKNKEQ----EQSSAKAALEIELSNIKAEL 755
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1179-1408 |
5.31e-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: 44.75 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1179 STAAQQELRSRREAELSELQrcveEETRRHETQLSELRVKHSAA---LDSLQEQLDNSKRARQSLEKAKATLEEERQNLT 1255
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQ----QEIAELEKELAALKKEEKALlkqLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1256 SELKSLQASRSESERGRKRADNQLQELSAR-----------LAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRL 1324
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1325 AKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSA 1404
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
....
gi 2414917124 1405 VEAG 1408
Cdd:COG4942 250 ALKG 253
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
826-1197 |
5.71e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 826 KKQQQLSALRVMQRNCAAYLKLRNWQWWRLFTKVkpLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKHAQLLE 905
Cdd:COG4717 164 ELEELEAELAELQEELEELLEQLSLATEEELQDL--AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 906 EKAVlaDQLQAEAELFAEAEEMRARLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQ 985
Cdd:COG4717 242 EERL--KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 986 RL--LLEKVTLETKV-KSLETDLATAVEQRERLGKEKKQLEERLnevtDQLTEEEEKTKSLNKLKNKQEAVIADLEERLK 1062
Cdd:COG4717 320 ELeeLLAALGLPPDLsPEELLELLDRIEELQELLREAEELEEEL----QLEELEQEIAALLAEAGVEDEEELRAALEQAE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1063 REEQGRLEQEKFKRRMESEAMEAQEQLSDLgmlssdlrgSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELK 1142
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEAL---------DEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2414917124 1143 E--EVENERGMRERAEKQRRDLSEELEALRTeLEDTLDstAAQQELRSRREAELSEL 1197
Cdd:COG4717 467 EdgELAELLQELEELKAELRELAEEWAALKL-ALELLE--EAREEYREERLPPVLER 520
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
879-1257 |
6.81e-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: 44.73 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 879 LQKAKEQLTRAEQDYTElDKKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLasRKQELEEVLGELETRLEEEEERGVQ 958
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE-KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEM--DRQAAIYAEQERMAMERERELERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 959 LANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKsletdlatavEQRERLGKEKKQLEERLNEVTDQLTEEEE 1038
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVR----------QELEAARKVKILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1039 KTKSLNKLKNKQEAVIAdlEERLKREEQGRLEQekfkrrmeseaMEAQEQLSDLgmlssdlrgslaqkekeitslqgRLE 1118
Cdd:pfam17380 425 IRAEQEEARQREVRRLE--EERAREMERVRLEE-----------QERQQQVERL-----------------------RQQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1119 EEGARRTeaqrslrealsqvselKEEVENERGMRERAEKQRRD-LSEELEALRTE-LEDTLDSTAAQQELRSRREAELSE 1196
Cdd:pfam17380 469 EEERKRK----------------KLELEKEKRDRKRAEEQRRKiLEKELEERKQAmIEEERKRKLLEKEMEERQKAIYEE 532
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2414917124 1197 LQRCVEEETRRHETQLSELRvkhsaaldSLQEQLDNSKRARQSLEKAKATLEEERQNLTSE 1257
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERR--------RIQEQMRKATEERSRLEAMEREREMMRQIVESE 585
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1077-1230 |
6.94e-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: 43.37 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1077 RMESEAMEAQEQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRE--- 1153
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyea 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1154 ------RAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQ 1227
Cdd:COG1579 94 lqkeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
...
gi 2414917124 1228 EQL 1230
Cdd:COG1579 174 PEL 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1382-1946 |
7.03e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1382 RQIQTHSQQLTELRKQSEEVNSAV-EAGDEIRRKLqRELDSAIQRERQKEEEKERVERQRERLREEIEDMT---IALQRE 1457
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIkEKEKELEEVL-REINEISSELPELREELEKLEKEVKELEELKEEIEeleKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1458 RQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEaDSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQ 1537
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1538 QDDVGKNVHELERTRRTLETEAQNLriqtqELEEELSEAENSRLRLEVTLQALKAQFEREistNEEKGEEKRRALSKQVR 1617
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRL-----EELEERHELYEEAKAKKEELERLKKRLTGL---TPEKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1618 ELEIQLEEERSQRSQSVSSKKQLEA---ELQEAEAQVETANRGKEEAMKQ--LRRLQGQMKEVLRELDEAkvtrddvisq 1692
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKaieELKKAKGKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEI---------- 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1693 skdsEKKIQTLEAEVLHLTEELAVSERQKRQaqqerDEIADEMVSSSSGKNVLSEEKRRLDARvnqleedleeeqtNNEL 1772
Cdd:PRK03918 472 ----EEKERKLRKELRELEKVLKKESELIKL-----KELAEQLKELEEKLKKYNLEELEKKAE-------------EYEK 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1773 LTERLRKTALQVETLTVQLQGERTLAQKaeaaREQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQER 1852
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYL 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1853 QeraianklMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEV-----EEENSRSSAQKRKLQRE--- 1924
Cdd:PRK03918 606 E--------LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkysEEEYEELREEYLELSRElag 677
|
570 580
....*....|....*....|....*.
gi 2414917124 1925 ----LEELTDSSQTMNREISSLRNQL 1946
Cdd:PRK03918 678 lraeLEELEKRREEIKKTLEKLKEEL 703
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1465-1685 |
8.56e-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: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1465 EKRQKKFDQCLAEEKAVSARlaeerdraEADSREKETRCLALSRALQEAQDQKEELERANkqlrlEMEQLVNQQDDVGKN 1544
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAE--------QEEARQREVRRLEEERAREMERVRLEEQERQQ-----QVERLRQQEEERKRK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1545 VHELERTRRTlETEAQNLRiqtqeleeelseaensRLRLEVTLQALKAQFEREistneekgEEKRRALSKQVRELEIQLE 1624
Cdd:pfam17380 476 KLELEKEKRD-RKRAEEQR----------------RKILEKELEERKQAMIEE--------ERKRKLLEKEMEERQKAIY 530
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 1625 EERSQRSQSVSSKKQLEAELQ---EAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDEAKVT 1685
Cdd:pfam17380 531 EEERRREAEEERRKQQEMEERrriQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1483-1684 |
9.71e-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: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1483 ARLAEERDRAEADSrEKETRcLALSRALQEAQDQKEELERAnkqlrLEMEQLVNQQDDVGKNVHELERTRRTLETEA-QN 1561
Cdd:COG2268 195 AEIIRDARIAEAEA-ERETE-IAIAQANREAEEAELEQERE-----IETARIAEAEAELAKKKAEERREAETARAEAeAA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1562 LRIQTQeleeelseaensRLRLEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRE------LEIQLEEERSQRSQSVS 1635
Cdd:COG2268 268 YEIAEA------------NAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKpaeaekQAAEAEAEAEAEAIRAK 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1636 SKKQLEAELQEAEAQVETANRGKEEAM-KQLRRLQGQMKEVLRELDEAKV 1684
Cdd:COG2268 336 GLAEAEGKRALAEAWNKLGDAAILLMLiEKLPEIAEAAAKPLEKIDKITI 385
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1610-1735 |
1.10e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.50 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1610 RALSKQVRELEIQLEEERSQRSQSVSSKKQlEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVL---RELDEAKVTR 1686
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAvsqQELDEARAAL 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2414917124 1687 DDVISQSKDSEKKIQTLEAEVLhLTEELAVSERQKRQAQQERDEIADEM 1735
Cdd:COG1566 158 DAAQAQLEAAQAQLAQAQAGLR-EEEELAAAQAQVAQAEAALAQAELNL 205
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1461-1682 |
1.18e-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: 43.60 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1461 CTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDD 1540
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1541 VGKNVHELERTRRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKaQFEREISTNEEKGEEKRRALSKQVRELE 1620
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2414917124 1621 IQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDEA 1682
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
997-1250 |
1.21e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.71 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 997 KVKSLETDLATAVEQ--------RERLGKEKkqLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEE---RLK--- 1062
Cdd:COG2268 98 KVNSDPEDIANAAERflgrdpeeIEELAEEK--LEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKnglELEsva 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1063 ----REEQGRLEQEKFKRRMESEAMEAQEQlsdlgmlssdlrgSLAQKEKEITSLQGRLEEEGARrTEAQRslrealsqv 1138
Cdd:COG2268 176 itdlEDENNYLDALGRRKIAEIIRDARIAE-------------AEAERETEIAIAQANREAEEAE-LEQER--------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1139 selkeEVENERGMRERAEKQRRDLSEELEALRTELEdtldstaAQQELRSRREAELSELQRCVEEETRRHETQLSELRVK 1218
Cdd:COG2268 233 -----EIETARIAEAEAELAKKKAEERREAETARAE-------AEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAE 300
|
250 260 270
....*....|....*....|....*....|..
gi 2414917124 1219 HSaaldslQEQLDNSKRARQSLEKAKATLEEE 1250
Cdd:COG2268 301 RE------EAELEADVRKPAEAEKQAAEAEAE 326
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1034-1361 |
1.48e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1034 TEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLgmlssdlRGSLAQKEKEITSL 1113
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQL-------EEELEQARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1114 QGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAE 1193
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1194 LSELQrcvEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRK 1273
Cdd:COG4372 159 LESLQ---EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1274 RADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALA 1353
Cdd:COG4372 236 SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
....*...
gi 2414917124 1354 SRVRALEE 1361
Cdd:COG4372 316 ALLAALLE 323
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1058-1289 |
1.53e-03 |
|
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: 42.82 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1058 EERLKREEQGRLEQEKFKRRMESEAMEAQEQLSdlgmlssdlrgsLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQ 1137
Cdd:pfam09787 55 ERDLLREEIQKLRGQIQQLRTELQELEAQQQEE------------AESSREQLQELEEQLATERSARREAEAELERLQEE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1138 VSELKEEVENERGMREraeKQRRDLSEELEALRTELEDTLDSTAAQQELRSRreaeLSELQRCVEEEtrrhETQLSELrv 1217
Cdd:pfam09787 123 LRYLEEELRRSKATLQ---SRIKDREAEIEKLRNQLTSKSQSSSSQSELENR----LHQLTETLIQK----QTMLEAL-- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1218 khSAALDSLQEQLDNSKRARQSLEKAKA-----------TLEEERQNLTSELKSLQASRSESERGR-KRADNQLQELSAR 1285
Cdd:pfam09787 190 --STEKNSLVLQLERMEQQIKELQGEGSngtsinmegisDGEGTRLRNVPGLFSESDSDRAGMYGKvRKAASVIDKFSIR 267
|
....
gi 2414917124 1286 LAQA 1289
Cdd:pfam09787 268 LGIF 271
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1596-1946 |
1.58e-03 |
|
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: 43.47 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1596 REISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEV 1675
Cdd:TIGR04523 57 KNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKEN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1676 LRELDEAKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVL---SEEKRRL 1752
Cdd:TIGR04523 137 KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLkkkIQKNKSL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1753 DARVNQLEEDLEEEQTNNELLTERLRKTALQVETLTVQLQgerTLAQKAEAAREQLEKQNKEL---KARLGEMEGAVRgk 1829
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN---QLKDEQNKIKKQLSEKQKELeqnNKKIKELEKQLN-- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1830 hrmsvaALEAKIETMEEQleqerqeraianklmrKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEE 1909
Cdd:TIGR04523 292 ------QLKSEISDLNNQ----------------KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK 349
|
330 340 350
....*....|....*....|....*....|....*..
gi 2414917124 1910 ENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQL 1946
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1102-1270 |
1.63e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1102 SLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRRD------LSEELEALRTELED 1175
Cdd:PRK12705 23 VLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREeerlvqKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1176 TLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLT 1255
Cdd:PRK12705 103 LENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNIL 182
|
170
....*....|....*
gi 2414917124 1256 SELKSLQASRSESER 1270
Cdd:PRK12705 183 AQAMQRIASETASDL 197
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1639-1946 |
1.77e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1639 QLEAELQEAEAQVETANRGKEEAMKQlRRLQGQMKEVLRE------LDEAKVTRDDVISQSKDSEKKIQTLEAEVLHLTE 1712
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQ-ERLRQEKEEKAREverrrkLEEAEKARQAEMDRQAAIYAEQERMAMERERELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1713 ELAVSERQKRQAQQERDEIADEMvSSSSGKNVLSEEKRRLDARVNQLEEDLEEEQTNNElltERLRKTALQVETLTvQLQ 1792
Cdd:pfam17380 352 RIRQEERKRELERIRQEEIAMEI-SRMRELERLQMERQQKNERVRQELEAARKVKILEE---ERQRKIQQQKVEME-QIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1793 GERTLAQKAEAAREQLEKQNKELKARLGEMEgavRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKT-EKKLKE 1871
Cdd:pfam17380 427 AEQEEARQREVRRLEEERAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEE 503
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2414917124 1872 VMMQAEDERRHadqyREQLDKSMVrlkqlKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMnREISSLRNQL 1946
Cdd:pfam17380 504 RKQAMIEEERK----RKLLEKEME-----ERQKAIYEEERRREAEEERRKQQEMEERRRIQEQM-RKATEERSRL 568
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
963-1242 |
2.80e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 963 KKKMQQNIQDLEEQLEEEESARqRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEeeeKTKS 1042
Cdd:pfam15905 62 KKKSQKNLKESKDQKELEKEIR-ALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLE---LTRV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1043 LNKLKNKQEAviadlEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGA 1122
Cdd:pfam15905 138 NELLKAKFSE-----DGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1123 RRTEAQrslrealSQVSELKEEVENERGMRERAEKQRRD---LSEELEALRTELEDTLDSTAAQQELRSRREAELSELQR 1199
Cdd:pfam15905 213 EKIEEK-------SETEKLLEYITELSCVSEQVEKYKLDiaqLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCK 285
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2414917124 1200 CVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEK 1242
Cdd:pfam15905 286 LLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1007-1231 |
2.89e-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: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1007 TAVEQRERLGKEKKQlEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQ 1086
Cdd:pfam06008 24 LTKQLQEYLSPENAH-KIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEIN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1087 EQLSDLGMLSSDLRGS-LAQKEKEITSLQGRLEEE--GARRTEAQRSLREA---LSQVSELKEEVENE-RGMRERAEKQR 1159
Cdd:pfam06008 103 EKVATLGENDFALPSSdLSRMLAEAQRMLGEIRSRdfGTQLQNAEAELKAAqdlLSRIQTWFQSPQEEnKALANALRDSL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2414917124 1160 RDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVeEETRRHETQLSELRVKHSAALDSLQEQLD 1231
Cdd:pfam06008 183 AEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKK-EEVSEQKNQLEETLKTARDSLDAANLLLQ 253
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1654-1732 |
2.89e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 42.36 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1654 ANRGKEEAMKQLRRLQGQMKEVLRELDEAKVTRDDV---ISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDE 1730
Cdd:PRK05431 19 AKRGFPLDVDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKEEIKALEAELDELEAELEE 98
|
..
gi 2414917124 1731 IA 1732
Cdd:PRK05431 99 LL 100
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
1013-1143 |
2.93e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 41.61 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1013 ERLGKEKKQLEERLNEVTDQLTEE-EEKTKSLNKLKNKQEAVIAdleerLKREEQGRLEQEKFKRRMESEAMEAQEQLSD 1091
Cdd:pfam15294 136 ERLKEENEKLKERLKTLESQATQAlDEKSKLEKALKDLQKEQGA-----KKDVKSNLKEISDLEEKMAALKSDLEKTLNA 210
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2414917124 1092 LGMLSSDLRGSLAQKEKEITSLQGRLE------EEGARRTEAQRSLREALSQVSE-LKE 1143
Cdd:pfam15294 211 STALQKSLEEDLASTKHELLKVQEQLEmaekelEKKFQQTAAYRNMKEMLTKKNEqIKE 269
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1664-1947 |
3.07e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1664 QLRRLQGQMKEVLRELDEAKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELavserqkRQAQQERDEIADEMVSSSSGKN 1743
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEA-------QELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1744 VLSEEKRRLDARVNQLEEDLEEEQTNNEL---LTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKArlg 1820
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSidkLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEK--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1821 emegavrgkhrmsvaaleakietmeeqleqerqeraiaNKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQL 1900
Cdd:COG1340 159 --------------------------------------NEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIEL 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2414917124 1901 KRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLS 1947
Cdd:COG1340 201 YKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1130-1289 |
3.34e-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: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1130 SLREALSQVSELKEEVENERGMRERAEKQRrdLSEELEALRTELEDtlDSTAAQQELRSRREAELSELQRCVEEETRRHE 1209
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDR--LEKETEALRERLQK--DLEEVRAKLEPYLEELQAKLGQNVEELRQRLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1210 TQLSELRVKHSAALDSLQEQLDNS-----KRARQSLEKAKATL----EEERQNLTSELKSLQAS-RSESERGRKRADNQL 1279
Cdd:pfam01442 77 PYTEELRKRLNADAEELQEKLAPYgeelrERLEQNVDALRARLapyaEELRQKLAERLEELKESlAPYAEEVQAQLSQRL 156
|
170
....*....|
gi 2414917124 1280 QELSARLAQA 1289
Cdd:pfam01442 157 QELREKLEPQ 166
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
821-1275 |
3.37e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 821 RKAFLKKQQQLSALRVMQRNCAAYLKLRNwQWWRLFTKVKPLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDKKH 900
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 901 AQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQEleevlgeletrleeeeergvQLANEKKKMQQNIQDLEEQLEEE 980
Cdd:COG4717 173 AELQEELEELLEQLSLATEEELQDLAEELEELQQRLA--------------------ELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 981 ESARQRLLLEKVTLETKVKSLETDLATAVeqrerLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEER 1060
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAAALLAL-----LGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1061 LKREEQGRLEQEkfkrrmeseamEAQEQLSDLGMLSSDLRGSLAQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSE 1140
Cdd:COG4717 308 QALPALEELEEE-----------ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1141 LKEEVENERGMRERAE--KQRRDLSEELEALRTELEDTLDSTAAQQELRSRR--EAELSELQRCVEEETRRHETQLSELr 1216
Cdd:COG4717 377 AEAGVEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREEL- 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2414917124 1217 vkhsAALDSLQEQLDNSKRARQsLEKAKATLEEERQNLTSELKSLQASRSESERGRKRA 1275
Cdd:COG4717 456 ----AELEAELEQLEEDGELAE-LLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1641-1840 |
3.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1641 EAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDEAKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAvseRQ 1720
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG---ER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1721 KRQAQQERDEI-----------ADEMVSSSSGKNVLSEEKRRLDARVNQLEEDLEEEQTNNELLTERLRKTALQVETLTV 1789
Cdd:COG3883 92 ARALYRSGGSVsyldvllgsesFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2414917124 1790 QLQGERTlaqKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAK 1840
Cdd:COG3883 172 ELEAQQA---EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1006-1260 |
3.61e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.58 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1006 ATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEaVIADLEERLKREEQGRLEQEKFKRRMESEAMEA 1085
Cdd:PLN02939 152 LQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVE-ILEEQLEKLRNELLIRGATEGLCVHSLSKELDV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1086 --QEQLS---DLGMLSSDL------RGSLAQKEKEITSLQGRLEEEGARRTEAQrslrEALSQVSELK-----EEVENER 1149
Cdd:PLN02939 231 lkEENMLlkdDIQFLKAELievaetEERVFKLEKERSLLDASLRELESKFIVAQ----EDVSKLSPLQydcwwEKVENLQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1150 GMRERAEK----------QRRDLSEELEALRTELEDTLDSTAA-------QQELRSRREaelsELQRCveeetrrHETQL 1212
Cdd:PLN02939 307 DLLDRATNqvekaalvldQNQDLRDKVDKLEASLKEANVSKFSsykvellQQKLKLLEE----RLQAS-------DHEIH 375
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2414917124 1213 SELRVKHsaalDSLQEQLDNSKRARQslEKAKATLEEERQNLTSELKS 1260
Cdd:PLN02939 376 SYIQLYQ----ESIKEFQDTLSKLKE--ESKKRSLEHPADDMPSEFWS 417
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1002-1289 |
3.64e-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: 42.63 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1002 ETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLkNKQEAVIAD--LEERLK--REEQGRLEQ-EKFKR 1076
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL-LPQANLLADetLADRLEelREELDAAQEaQAFIQ 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1077 RMESEAMEAQEQLSdlgMLSSD------LRGSLAQKEKEITSLQGR---LEEEGARRTEAqrSLREALSQVSELKEEVEN 1147
Cdd:COG3096 914 QHGKALAQLEPLVA---VLQSDpeqfeqLQADYLQAKEQQRRLKQQifaLSEVVQRRPHF--SYEDAVGLLGENSDLNEK 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1148 ERGMRERAEKQRRDLSEELEALRTELEDtldSTAAQQELRSRREAELSELQRCVEEetrrhetqLSELRVKHSAAldslq 1227
Cdd:COG3096 989 LRARLEQAEEARREAREQLRQAQAQYSQ---YNQVLASLKSSRDAKQQTLQELEQE--------LEELGVQADAE----- 1052
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2414917124 1228 eqldnskrarqslekAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQA 1289
Cdd:COG3096 1053 ---------------AEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKA 1099
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
927-1362 |
4.31e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 927 MRARLASRKQELEEVLGELETRLeeeeergvqlanekkKMQQNIQDLEEQLEEEESARQRLllekVTLETKVKSLETDLa 1006
Cdd:pfam10174 142 MELRIETQKQTLGARDESIKKLL---------------EMLQSKGLPKKSGEEDWERTRRI----AEAEMQLGHLEVLL- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1007 tavEQRErlgKEKKQLEERLNEvTDQLTEEEEKTKSLNKLKNKQEAVIADLeERLKREEQGRLEQEK-------FKRRME 1079
Cdd:pfam10174 202 ---DQKE---KENIHLREELHR-RNQLQPDPAKTKALQTVIEMKDTKISSL-ERNIRDLEDEVQMLKtngllhtEDREEE 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1080 SEAMEAQEQLSDLGMLSSD-LRGSLAQKEKEITSLQGRLEEEGARRTEAQRS---LREAL-----------SQVSELKEE 1144
Cdd:pfam10174 274 IKQMEVYKSHSKFMKNKIDqLKQELSKKESELLALQTKLETLTNQNSDCKQHievLKESLtakeqraailqTEVDALRLR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1145 VENERGMRERAEKQRRDLSEELEALRTELEDTLDSTaaqqELRSRREAELSELQRCVEEETRRHETQLSELRvkhsAALD 1224
Cdd:pfam10174 354 LEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDML----DVKERKINVLQKKIENLQEQLRDKDKQLAGLK----ERVK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1225 SLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSL-QASRSESERGRKradnQLQELSARLAQADREREDREERMHKL 1303
Cdd:pfam10174 426 SLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREdRERLEELESLKK----ENKDLKEKVSALQPELTEKESSLIDL 501
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2414917124 1304 QCEIESL--SGNLSSSDSKSLRLA-----KEISSLESQLHDARElLQDESRQKMALASRVRALEEE 1362
Cdd:pfam10174 502 KEHASSLasSGLKKDSKLKSLEIAveqkkEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQE 566
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1085-1231 |
4.59e-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: 39.94 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1085 AQEQLSDLGMLSSDLRGSLAQKEKEIT-SLQGRLEEEGARRTEAQRSLREALSQ-VSELKEEVENE-RGMRERAEKQRRD 1161
Cdd:pfam01442 13 AEELQEQLGPVAQELVDRLEKETEALReRLQKDLEEVRAKLEPYLEELQAKLGQnVEELRQRLEPYtEELRKRLNADAEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1162 LSEELEA----LRTELEDTLDSTAAQ-----QELRSRREAELSELQRCVEEETRRHETQLS----ELRVKHSAALDSLQE 1228
Cdd:pfam01442 93 LQEKLAPygeeLRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAEEVQAQLSqrlqELREKLEPQAEDLRE 172
|
...
gi 2414917124 1229 QLD 1231
Cdd:pfam01442 173 KLD 175
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1124-1284 |
4.66e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1124 RTEAQRSLREALSQVSELKEEVENErgmreraekqrrdLSEELEALRTELEdtldstaaqQELRSRREaelsELQRcVEE 1203
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALLE-------------AKEEIHKLRNEFE---------KELRERRN----ELQK-LEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1204 ETRRHEtqlselrvkhsaaldslqEQLDNSKrarQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELS 1283
Cdd:PRK12704 90 RLLQKE------------------ENLDRKL---ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIS 148
|
.
gi 2414917124 1284 A 1284
Cdd:PRK12704 149 G 149
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1045-1178 |
5.30e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1045 KLKNKQEAVIADLEERLKREEQGRLEQEKFKRrmeSEAMEAQEQLSDLgmlssdlRGSLAQKEKEITSLQGRLEEEgarr 1124
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKK---EQDEASFERLAEL-------RDELAELEEELEALKARWEAE---- 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 1125 teaqrslREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLD 1178
Cdd:COG0542 467 -------KELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1579-1709 |
5.52e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1579 SRLRLEVT-----LQALKAQF-----EREISTNEEKGEEKRRAlsKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAE 1648
Cdd:COG0542 400 ARVRMEIDskpeeLDELERRLeqleiEKEALKKEQDEASFERL--AELRDELAELEEELEALKARWEAEKELIEEIQELK 477
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2414917124 1649 AQVETANRGKEEAMKQLRRLQGQMKEVLRELDEaKVTRDD---VISQ------SK--DSEK-KIQTLEaEVLH 1709
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLRE-EVTEEDiaeVVSRwtgipvGKllEGEReKLLNLE-EELH 548
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1104-1267 |
6.25e-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: 41.55 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1104 AQKEKEITSLQGRLEEEGARRTEAQRSLREALSQVSELKEEVENERGMRERAEKQRR------DLSEELEALRTELEDTL 1177
Cdd:pfam05667 331 QQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKvkkktlDLLPDAEENIAKLQALV 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1178 DSTAAQ-QELRSRREA----------ELSELQRCVEEETRRhetQLSELRvkhsaaldSLQEQLdnskraRQSLEKAKAT 1246
Cdd:pfam05667 411 DASAQRlVELAGQWEKhrvplieeyrALKEAKSNKEDESQR---KLEEIK--------ELREKI------KEVAEEAKQK 473
|
170 180
....*....|....*....|...
gi 2414917124 1247 lEEERQNLTSELKSL--QASRSE 1267
Cdd:pfam05667 474 -EELYKQLVAEYERLpkDVSRSA 495
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1029-1249 |
7.07e-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: 41.09 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1029 VTDQLTEEEEKTKSLNK---LKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSDLRGSLAQ 1105
Cdd:pfam15709 305 VTGNMESEEERSEEDPSkalLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1106 KEKEITSLQGRLEEEGARRTEAQRSLRealsqvseLKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQE 1185
Cdd:pfam15709 385 RFEEIRLRKQRLEEERQRQEEEERKQR--------LQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKE 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 1186 LRSRREAELSELQRCVEEEtrrhetQLSELRVKHSAALDSLQEQldnSKRARQSLEKAKATLEE 1249
Cdd:pfam15709 457 LEMQLAEEQKRLMEMAEEE------RLEYQRQKQEAEEKARLEA---EERRQKEEEAARLALEE 511
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1028-1196 |
7.57e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 41.54 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1028 EVTDQLTEE----------EEKTKSlnklknkQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMeaqeqlsdlgmlss 1097
Cdd:PTZ00491 639 EPVDERTRDslqksvqlaiEITTKS-------QEAAARHQAELLEQEARGRLERQKMHDKAKAEEQ-------------- 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1098 dlRGSLAQKEKEITSlqgrLEEEGARRTEAqrslrEALSQVSELKEEVENERGmRERAEKQRRDLSEELEALRTELEDTL 1177
Cdd:PTZ00491 698 --RTKLLELQAESAA----VESSGQSRAEA-----LAEAEARLIEAEAEVEQA-ELRAKALRIEAEAELEKLRKRQELEL 765
|
170
....*....|....*....
gi 2414917124 1178 DSTAAQQELRSRREAELSE 1196
Cdd:PTZ00491 766 EYEQAQNELEIAKAKELAD 784
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1012-1343 |
7.69e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1012 RERLGKEKKQLEERLNEVTDQ-LTEEEEKTKSLN----------KLKNK-QEAV---IADLEERLKREEQgrlEQEKFK- 1075
Cdd:PRK04778 24 RKRNYKRIDELEERKQELENLpVNDELEKVKKLNltgqseekfeEWRQKwDEIVtnsLPDIEEQLFEAEE---LNDKFRf 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1076 RRMESEAMEAQEQLSDL-----GMLS--SDLRGSLAQKEKEITSLQGRLEEegARRT---------EAQRSLREALSQVS 1139
Cdd:PRK04778 101 RKAKHEINEIESLLDLIeedieQILEelQELLESEEKNREEVEQLKDLYRE--LRKSllanrfsfgPALDELEKQLENLE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1140 ELKEEVE--NERGMRERAEKQRRDLSEELEALRTELED------TLDSTAAQQ--ELRS-RREAE-----------LSEL 1197
Cdd:PRK04778 179 EEFSQFVelTESGDYVEAREILDQLEEELAALEQIMEEipellkELQTELPDQlqELKAgYRELVeegyhldhldiEKEI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1198 QRcVEEETRRHETQLSELRVKH--------SAALDSLQEQLDNSKRARQSLEKAKATL-------EEERQNLTSELKSLQ 1262
Cdd:PRK04778 259 QD-LKEQIDENLALLEELDLDEaeekneeiQERIDQLYDILEREVKARKYVEKNSDTLpdflehaKEQNKELKEEIDRVK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1263 ASR--SESERGRKRA-DNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDAR 1339
Cdd:PRK04778 338 QSYtlNESELESVRQlEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAR 417
|
....
gi 2414917124 1340 ELLQ 1343
Cdd:PRK04778 418 EKLE 421
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1187-1947 |
7.79e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1187 RSRREAELSELQRCVEEETRRHETQLSELRVKhsaALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQAS-R 1265
Cdd:pfam12128 220 RQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFN---TLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTlD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1266 SESERGRKRADNQLQELSARLAQADREREDREERMHK-LQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQD 1344
Cdd:pfam12128 297 DQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAfLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1345 ESRQKMALASR-VRALEEEKNGLMERLEEEEERGKELSRQIQ--------THSQQLTELRKQSEEVNSAVEagdeirrKL 1415
Cdd:pfam12128 377 YNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVAEDDLQaleselreQLEAGKLEFNEEEYRLKSRLG-------EL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1416 QRELDSAIQRERQkeeekerverqrerlreeiedmtiaLQRERQNCTALEKRQKKFDQCLAEekavsaRLAEERDRAEAD 1495
Cdd:pfam12128 450 KLRLNQATATPEL-------------------------LLQLENFDERIERAREEQEAANAE------VERLQSELRQAR 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1496 SREKETrclalSRALQEAqdqkeelERANKQLRLEMEQLVNQQDDVGKNVHELertrrtLETEAQNLRiqtqeleeelse 1575
Cdd:pfam12128 499 KRRDQA-----SEALRQA-------SRRLEERQSALDELELQLFPQAGTLLHF------LRKEAPDWE------------ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1576 aeNSRLRLEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQleeersqrsQSVSSKKQLEAELQEAEAQVETAN 1655
Cdd:pfam12128 549 --QSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVP---------EWAASEEELRERLDKAEEALQSAR 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1656 RGKEEAMKQLRRLQGQMKEVLRELDEAKVTRddvisqsKDSEKKIQTL----EAEVLHLTEELavsERQKRQAQQERDEI 1731
Cdd:pfam12128 618 EKQAAAEEQLVQANGELEKASREETFARTAL-------KNARLDLRRLfdekQSEKDKKNKAL---AERKDSANERLNSL 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1732 ADEMVSSSSGKNVLSEEKRRldarvnqleedleeeqTNNELLTERLRKTALQVETLTVQLQgerTLAQKAEAAREQLEKQ 1811
Cdd:pfam12128 688 EAQLKQLDKKHQAWLEEQKE----------------QKREARTEKQAYWQVVEGALDAQLA---LLKAAIAARRSGAKAE 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1812 NKELKARLgEMEGAVRGKHRMSVAALEAKIETMEEQleqerqeraIANKLMRKTEKKLKEVMMQaEDERRHADQYREQLD 1891
Cdd:pfam12128 749 LKALETWY-KRDLASLGVDPDVIAKLKREIRTLERK---------IERIAVRRQEVLRYFDWYQ-ETWLQRRPRLATQLS 817
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 2414917124 1892 KSMVRLKQLKRQLEEVEEENSRssaQKRKLQRELEELTDSSQTMNREISSLRNQLS 1947
Cdd:pfam12128 818 NIERAISELQQQLARLIADTKL---RRAKLEMERKASEKQQVRLSENLRGLRCEMS 870
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
876-1284 |
8.11e-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: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 876 EAALQKAKEQLTRAEQDYTELDKKHAQLLEEKAVLADQLQAEaelfaeaeemRARLAsrkqeleevlgeletrleeeeer 955
Cdd:COG3096 291 RRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAA----------SDHLN----------------------- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 956 GVQLAnekKKMQQNIQdleeqleeeesaRQRLLLEKvtLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTE 1035
Cdd:COG3096 338 LVQTA---LRQQEKIE------------RYQEDLEE--LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1036 -----EEEKTKSLnklkNKQEAVIAdLEERLKREEQGRLEQEKFKRRMesEAMEAQEQLSDLGMLSSDLRGSLAQKEKE- 1109
Cdd:COG3096 401 yqqalDVQQTRAI----QYQQAVQA-LEKARALCGLPDLTPENAEDYL--AAFRAKEQQATEEVLELEQKLSVADAARRq 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1110 -------ITSLQGRLEeegarRTEAQRSLREALSQVSELKEEVENERGMR------ERAEKQRRDLSEELEAL----RTE 1172
Cdd:COG3096 474 fekayelVCKIAGEVE-----RSQAWQTARELLRRYRSQQALAQRLQQLRaqlaelEQRLRQQQNAERLLEEFcqriGQQ 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1173 LEDTLDSTAAQQELRSRREAELSELQRCVEE--ETRRHETQL----SELRVKH------SAALDSLQEQLDnskrarQSL 1240
Cdd:COG3096 549 LDAAEELEELLAELEAQLEELEEQAAEAVEQrsELRQQLEQLrariKELAARApawlaaQDALERLREQSG------EAL 622
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2414917124 1241 EKAKAtLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSA 1284
Cdd:COG3096 623 ADSQE-VTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1021-1154 |
8.29e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.83 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1021 QLEERLNEVTDQLTEEEEKtkslnklKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSDLR 1100
Cdd:PRK11637 174 ELKQTREELAAQKAELEEK-------QSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLR 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2414917124 1101 GSLAQKEKEItslQGRLEEEgARRTEAQRSLREALSQVSELKEEVENERGMRER 1154
Cdd:PRK11637 247 DSIARAEREA---KARAERE-AREAARVRDKQKQAKRKGSTYKPTESERSLMSR 296
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1309-1703 |
9.41e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1309 SLSGNLSSSDSKSLR---------LAKEISSLESQLHDARELLQD---------------ESRQKMALASRVRAlEEEKN 1364
Cdd:PRK04863 204 SLYGGISSAITRSLRdyllpensgVRKAFQDMEAALRENRMTLEAirvtqsdrdlfkhliTESTNYVAADYMRH-ANERR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1365 GLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAveagdeiRRKLQRELDSAiqrerqkeeekerverqrerlr 1444
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEA-------ESDLEQDYQAA---------------------- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1445 eeiedmtialqRERQNC--TALeKRQKKFDQC----------LAEEKAVSARLAEERDRAEADSREKETRCLAL------ 1506
Cdd:PRK04863 334 -----------SDHLNLvqTAL-RQQEKIERYqadleeleerLEEQNEVVEEADEQQEENEARAEAAEEEVDELksqlad 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1507 ---------SRALQeAQDQKEELERANKQLRLE----------MEQLVNQQDDVGKNVHELE------------------ 1549
Cdd:PRK04863 402 yqqaldvqqTRAIQ-YQQAVQALERAKQLCGLPdltadnaedwLEEFQAKEQEATEELLSLEqklsvaqaahsqfeqayq 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1550 ---------------RTRRTLETEAQNLRIQTQELEEELSEAEN--SRLRLEVTLQALKAQFEREIS---TNEEKGEEKR 1609
Cdd:PRK04863 481 lvrkiagevsrseawDVARELLRRLREQRHLAEQLQQLRMRLSEleQRLRQQQRAERLLAEFCKRLGknlDDEDELEQLQ 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1610 RALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQvETANRGKEEAMKQLR-----------RLQGQMKEVLRE 1678
Cdd:PRK04863 561 EELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAAR-APAWLAAQDALARLReqsgeefedsqDVTEYMQQLLER 639
|
490 500
....*....|....*....|....*
gi 2414917124 1679 LDEAKVTRDDVISQSKDSEKKIQTL 1703
Cdd:PRK04863 640 ERELTVERDELAARKQALDEEIERL 664
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1102-1287 |
9.53e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 41.01 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1102 SLAQKEKEITSLQGRLEEEGAR-RTEAQRslrEALSQVSELKEEVENE-RGMRERAEKQRRDLSEELEALRTELEDTLDS 1179
Cdd:PRK00106 36 TLLNAEQEAVNLRGKAERDAEHiKKTAKR---ESKALKKELLLEAKEEaRKYREEIEQEFKSERQELKQIESRLTERATS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1180 TAAQQELRSRREAELSELQRCVEEETR---RHETQLSELRVKHSAALDSLqeqldnskrARQSLEKAKAT-LEEERQNLT 1255
Cdd:PRK00106 113 LDRKDENLSSKEKTLESKEQSLTDKSKhidEREEQVEKLEEQKKAELERV---------AALSQAEAREIiLAETENKLT 183
|
170 180 190
....*....|....*....|....*....|....
gi 2414917124 1256 SELKSL--QASRSESERGRKRADNQLQELSARLA 1287
Cdd:PRK00106 184 HEIATRirEAEREVKDRSDKMAKDLLAQAMQRLA 217
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1773-1931 |
9.76e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1773 LTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAV-RGKHRMSVA-------ALEAKIETm 1844
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIkKYEEQLGNVrnnkeyeALQKEIES- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414917124 1845 eeqleqerqeraiANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEEnsrSSAQKRKLQRE 1924
Cdd:COG1579 101 -------------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELEELEAE 164
|
....*..
gi 2414917124 1925 LEELTDS 1931
Cdd:COG1579 165 REELAAK 171
|
|
| |
