|
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 ... |
109-793 |
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: 1449.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGRKkeavqsmqYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNI--------PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTM 348
Cdd:cd14920 153 DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 349 DSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQK 428
Cdd:cd14920 233 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 429 AQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 508
Cdd:cd14920 313 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 509 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPR 588
Cdd:cd14920 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 589 GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSSGessaPVTFGAAGLKTK 668
Cdd:cd14920 473 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGM----TETAFGSAYKTK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 669 KGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 748
Cdd:cd14920 549 KGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1988774933 749 RYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14920 629 RYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
109-793 |
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: 1301.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEavqsmqyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKK-------GTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLL-GTADQYRFLSGGSIPVPGQSDSENFTQT 347
Cdd:cd01377 154 GSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLtGDPSYYFFLSQGELTIDGVDDAEEFKLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQ 427
Cdd:cd01377 234 DEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 428 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRrQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 507
Cdd:cd01377 314 KGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDT-KSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 508 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFF-KSKQ 586
Cdd:cd01377 393 HMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFkKPKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 587 PRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGldqvssgessapvtfGAAGLK 666
Cdd:cd01377 471 KKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGG---------------GGGKKK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 667 TKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEF 746
Cdd:cd01377 536 KKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEF 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1988774933 747 RQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd01377 616 KQRYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
109-793 |
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: 1168.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVASSHKGgtlgRKKEAVQSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKT----KKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTM 348
Cdd:cd14932 157 DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 349 DSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQK 428
Cdd:cd14932 237 EAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 429 AQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 508
Cdd:cd14932 317 AQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 509 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPR 588
Cdd:cd14932 397 MFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 589 GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSSGESSAPVTFgaaglKTK 668
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHGAF-----KTR 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 669 KGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 748
Cdd:cd14932 552 KGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1988774933 749 RYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14932 632 RYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
109-793 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 1157.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVASSH-KGGTLGRKKEAVQSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 267
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKpKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 268 FDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQT 347
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQ 427
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 428 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 507
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 508 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQp 587
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDF- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 588 RGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDrIVGLDQVSSGESsapvTFGAaglKT 667
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQALTDT----QFGA---RT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 668 KKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 747
Cdd:cd14911 549 RKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1988774933 748 QRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14911 629 QRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
109-793 |
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: 1118.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVASSHKGgtlgrKKEavqSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKG-----KKD---TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTM 348
Cdd:cd14921 153 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 349 DSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQK 428
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 429 AQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 508
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 509 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPR 588
Cdd:cd14921 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 589 GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSS-GESSAPvtfgaAGLKT 667
Cdd:cd14921 473 DKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKmTESSLP-----SASKT 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 668 KKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 747
Cdd:cd14921 548 KKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1988774933 748 QRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14921 628 QRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
109-793 |
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: 1118.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVASSHKGgtlgrKKEAvqsmqyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKS-----KKDQ------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTM 348
Cdd:cd14919 150 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 349 DSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQK 428
Cdd:cd14919 230 EAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 429 AQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 508
Cdd:cd14919 310 AQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 509 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPR 588
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 589 GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSS-GESSAPVTFgaaglKT 667
Cdd:cd14919 470 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGmSETALPGAF-----KT 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 668 KKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 747
Cdd:cd14919 545 RKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFR 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1988774933 748 QRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14919 625 QRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
109-793 |
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: 1113.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVASSHKGgtlgRKKEAVQSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKT----KKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTM 348
Cdd:cd15896 157 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 349 DSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQK 428
Cdd:cd15896 237 EAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 429 AQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 508
Cdd:cd15896 317 AQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 509 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPR 588
Cdd:cd15896 397 MFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 589 GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVsSGESSAPVTFgaaglKTK 668
Cdd:cd15896 477 DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKV-SGMSEMPGAF-----KTR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 669 KGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 748
Cdd:cd15896 551 KGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1988774933 749 RYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd15896 631 RYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
870-1950 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1107.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 870 TRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGEL 949
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 950 ETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEER 1029
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1030 LNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQ 1109
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1110 KEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQE 1189
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1190 LRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASR 1269
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1270 SESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDE 1349
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1350 SRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQR 1429
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1430 ERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLA 1509
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1510 LSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEV 1589
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1590 TLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQL 1669
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1670 RRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVL 1749
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1750 SEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGA 1829
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1830 VRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLE 1909
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1988774933 1910 EVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQL 1950
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
97-793 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1100.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 97 VEDMADLTCLNEASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSML 176
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 177 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGtlgrkkeavqsmQYGELERQLLQANPILEAFGNAKTVKNDN 256
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAG------------NVGRLEEQILQSNPILEAFGNAKTVRNNN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 257 SSRFGKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPV 335
Cdd:pfam00063 149 SSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSqSGCYTI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 336 PGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAIL 415
Cdd:pfam00063 229 DGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALC 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 416 TPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCIN 495
Cdd:pfam00063 309 KRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCIN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 496 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPRATDRSFVEKLSGEQ 575
Cdd:pfam00063 389 YVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTF 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 576 GSHPKFFKSKqPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSSGESS 655
Cdd:pfam00063 466 SKHPHFQKPR-LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKST 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 656 APvtfgaaglKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQ 735
Cdd:pfam00063 545 PK--------RTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRA 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774933 736 GFPNRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:pfam00063 617 GFPNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
109-793 |
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: 1095.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVASSHKGgtlgRKKEAVQsmqyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKG----RKEPGVP----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQsDSENFTQTM 348
Cdd:cd14930 153 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ-ERELFQETL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 349 DSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQK 428
Cdd:cd14930 232 ESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 429 AQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 508
Cdd:cd14930 312 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 509 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPR 588
Cdd:cd14930 392 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 589 GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSSGESSAPvtfgaaGLKTK 668
Cdd:cd14930 472 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPP------GGRPR 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 669 KGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 748
Cdd:cd14930 546 RGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1988774933 749 RYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14930 626 RYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
90-805 |
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: 1013.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 90 NPPRFSKVEDMADLTCLNEASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISE 169
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 170 AAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGtlgrkkeavqsmqyGELERQLLQANPILEAFGNA 249
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV--------------GSVEDQILESNPILEAFGNA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 250 KTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS 329
Cdd:smart00242 147 KTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 330 -GGSIPVPGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNT-AAQKLCHLLGVNV 407
Cdd:smart00242 227 qGGCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 408 LEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQgASFIGILDIAGFEIFQLN 487
Cdd:smart00242 307 EELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 488 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATDRSF 567
Cdd:smart00242 386 SFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 568 VEKLSGEQGSHPKFFKSKQpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdrivgld 647
Cdd:smart00242 463 LEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 648 qvssgessapvtfgaAGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVL 727
Cdd:smart00242 535 ---------------VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVL 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774933 728 EGIRICRQGFPNRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFRAGVLAHLEEERD 805
Cdd:smart00242 600 ENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
46-1265 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 897.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 46 VWVPSEKQGFESASIREERGDEVEVELTDSQRRVTLSREEVQ-----RMNPPRFSKVEDMADLTCLNEASVLHNLRERYY 120
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEGKKEDGESVSVKKKvlgndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 121 SGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGESGAGKTENTKK 200
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 201 VIQYLAHVASSHkggtlgrkkeavqSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANIE 280
Cdd:COG5022 172 IMQYLASVTSSS-------------TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 281 TYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTMDSMAIMGFTPE 359
Cdd:COG5022 239 TYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSqGGCDKIDGIDDAKEFKITLDALKTIGIDEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 360 ELMSMLKVISAVLQFGNISFMKEKNhDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKEQADFAV 439
Cdd:COG5022 319 EQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 440 EALAKATYERLFRWLVHRINRALDRRQRQGaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 519
Cdd:COG5022 398 DSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 520 EGIEWNFIDFgLDLQPCIDLIERpANPPGVLALLDEECWFPRATDRSFVEKLSG--EQGSHPKFFKSKQprGEADFSIIH 597
Cdd:COG5022 477 EGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRF--RDNKFVVKH 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 598 YAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVgldqvssgessapvtfgaaglktKKGMFRTVGQ 677
Cdd:COG5022 553 YAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-----------------------SKGRFPTLGS 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 678 LYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPNA 757
Cdd:COG5022 610 RFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSK 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 758 IPRT----FMDGKQASELMISALELDKNLFRVGQSKVFFRAGVLAHLEEERDLKITDTIIRFQSAARGFLSRKAFLKKQQ 833
Cdd:COG5022 690 SWTGeytwKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALK 769
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 834 QLSALRVMQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQDEEIQTREAALQKAKEQLTR---AEQDYTELDRKHAQLLEE 910
Cdd:COG5022 770 RIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKRekkLRETEEVEFSLKAEVLIQ 849
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 911 KAVLADQLQAEAELFAEAEEMRarlasrkqeleevlgeletrleeeeergVQLANEKKKMQQNIQDLEEQLEEEESARQR 990
Cdd:COG5022 850 KFGRSLKAKKRFSLLKKETIYL----------------------------QSAQRVELAERQLQELKIDVKSISSLKLVN 901
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 991 LLLEKVTLEtKVKSLETDLATAVE-QRERLGKEKKQLEERlnEVTDQLTEEEEKTKSLNKL---KNKQEAVIADLEERLK 1066
Cdd:COG5022 902 LELESEIIE-LKKSLSSDLIENLEfKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLhevESKLKETSEEYEDLLK 978
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1067 REEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRgSLAQKEKEITSLQgrleeegarraEAQRSLREALSQVSELK 1146
Cdd:COG5022 979 KSTILVREGNKANSELKNFKKELAELSKQYGALQESTK-QLKELPVEVAELQ-----------SASKIISSESTELSILK 1046
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1147 EEVENERGMreraEKQRRDLSEELEALRTELEDTLDSTaAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAA 1226
Cdd:COG5022 1047 PLQKLKGLL----LLENNQLQARYKALKLRRENSLLDD-KQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQ 1121
|
1210 1220 1230
....*....|....*....|....*....|....*....
gi 1988774933 1227 ldslQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSL 1265
Cdd:COG5022 1122 ----MIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLEL 1156
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
109-793 |
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: 868.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRH-EMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 188 GESGAGKTENTKKVIQYLAHVASSHKGgtlgrkkeaVQSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 267
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSS---------KSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 268 FDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFL-----SGGSIPVPGQSDSE 342
Cdd:cd00124 152 FDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 343 NFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKN--HDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIK 420
Cdd:cd00124 232 EFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEdeDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 421 VGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALD-RRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNE 499
Cdd:cd00124 312 VGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSpTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 500 KLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHP 579
Cdd:cd00124 392 KLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 580 KFFKSKQPRGEAdFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDhfvselwkevdrivgldqvssgessapvt 659
Cdd:cd00124 469 RFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ----------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 660 fgaaglktkkgmfrtvgqlYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPN 739
Cdd:cd00124 519 -------------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPV 579
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1988774933 740 RIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd00124 580 RLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
109-793 |
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: 795.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVASshKGGTLGRKKEAVQSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAA--LGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRaDLLLGTAD--QYRFLSGGSIPVPGQSDSENFTQ 346
Cdd:cd14927 159 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEELMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 347 TMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 426
Cdd:cd14927 238 TDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 427 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRR-QRQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 505
Cdd:cd14927 318 TKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKlPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 506 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFK- 583
Cdd:cd14927 396 NHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKp 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 584 --SKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivglDQVSSGESSAPVTFG 661
Cdd:cd14927 473 rpDKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---------ENYVGSDSTEDPKSG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 662 AAGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRI 741
Cdd:cd14927 544 VKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRI 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1988774933 742 PFQEFRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14927 624 LYADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
110-793 |
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: 769.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 190 SGAGKTENTKKVIQYLAHVASShkgGTLGRKKEAvqSMQyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 269
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAAT---GDLAKKKDS--KMK-GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 270 VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETrADLLLGTADQYR--FLSGGSIPVPGQSDSENFTQT 347
Cdd:cd14913 156 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEILVASIDDAEELLAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 426
Cdd:cd14913 235 DSAIDILGFTPEEKSGLYKLTGAVMHYGNMKF-KQKQREEQAEPDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 427 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRR-QRQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 505
Cdd:cd14913 314 TKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKlPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 506 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKS 584
Cdd:cd14913 392 NHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 585 KQPRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivgldqVSSGESSAPVTFGa 662
Cdd:cd14913 469 KVVKGraEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY-----------ATFATADADSGKK- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 663 AGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIP 742
Cdd:cd14913 537 KVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRIL 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 743 FQEFRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14913 617 YGDFKQRYRVLNASAIPEgQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
109-793 |
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: 754.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKeavqsmqyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSK--------GSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGT-ADQYRFLSGGSIPVPGQSDSENFTQT 347
Cdd:cd14909 153 GPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDnIYDYYIVSQGKVTVPNVDDGEEFSLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQ 427
Cdd:cd14909 233 DQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 428 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 507
Cdd:cd14909 313 QGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKR-QHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 508 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKSKQ 586
Cdd:cd14909 392 HMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 587 PRG---EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEvdrivgldqvSSGESSAPVtfGAA 663
Cdd:cd14909 469 PKPgqqAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD----------HAGQSGGGE--QAK 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 664 GLKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIP 742
Cdd:cd14909 537 GGRGKKGGgFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMM 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1988774933 743 FQEFRQRYEILTPNAIpRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14909 617 YPDFKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
109-793 |
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: 744.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLGRkkeavqsmqyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGK----------GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLL-GTADQYRFLSGGSIPVPGQSDSENFTQT 347
Cdd:cd14934 151 GTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQGVTVVDNMDDGEELQIT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQ 427
Cdd:cd14934 231 DVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 428 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRR-QRQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 506
Cdd:cd14934 311 KGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKmQRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 507 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKSK 585
Cdd:cd14934 389 HHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 586 QPRG---EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSdHFVSELWKEvdrivgldqvssgESSAPvtfgA 662
Cdd:cd14934 466 GGKGkgpEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS-LGLLALLFK-------------EEEAP----A 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 663 AGLKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRI 741
Cdd:cd14934 528 GSKKQKRGSsFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRL 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 742 PFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14934 608 QYPEFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
110-793 |
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: 723.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSG-LIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVASSHKGGTlgrkkeavqsmqygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET--------------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQT 347
Cdd:cd01380 148 DKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNqGGSPVIDGVDDAAEFEET 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQ 427
Cdd:cd01380 228 RKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 428 KAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 506
Cdd:cd01380 308 KPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 507 HTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPRATDRSFVEKLSGE-QGSHPKFFKSk 585
Cdd:cd01380 388 QHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQhLKKPNKHFKK- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 586 qPR-GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHfvselwkevdrivgldqvssgessapvtfgaag 664
Cdd:cd01380 463 -PRfSNTAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR--------------------------------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 665 lktKKgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 744
Cdd:cd01380 509 ---KK----TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYE 581
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1988774933 745 EFRQRYEILTPNAiPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd01380 582 EFFSRYRVLLPSK-EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
109-793 |
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: 709.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVAsshkggTLGRKKEavqsmQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIA------AMIESKK-----KLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEetRADLLLGTAD--QYRFLSGGSIPVPGQSDSENFTQ 346
Cdd:cd14929 150 GARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEELLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 347 TMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 426
Cdd:cd14929 228 TEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 427 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRR-QRQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 505
Cdd:cd14929 308 TRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKlSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 506 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKS 584
Cdd:cd14929 386 NQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 585 KQPRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKevdrivglDQVSSGESSapvTFGA 662
Cdd:cd14929 463 KPDKKkfEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFE--------NYISTDSAI---QFGE 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 663 AglKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRI 741
Cdd:cd14929 532 K--KRKKGAsFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRL 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1988774933 742 PFQEFRQRYEILTPNAIPRT-FMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14929 610 LYADFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
110-793 |
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: 705.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 190 SGAGKTENTKKVIQYLAHVASshkggtLGRKKEAVQSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 269
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAA------IGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 270 VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETrADLLLGTAD--QYRFLSGGSIPVPGQSDSENFTQT 347
Cdd:cd14917 156 ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEELMAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASmPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 426
Cdd:cd14917 235 DNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 427 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 505
Cdd:cd14917 314 TKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQpRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 506 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKL-SGEQGSHPKFFKS 584
Cdd:cd14917 392 NHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLfDNHLGKSNNFQKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 585 KQPRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivgldqVSSGESSAPVTFGA 662
Cdd:cd14917 469 RNIKGkpEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLF-----------ANYAGADAPIEKGK 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 663 AglKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRI 741
Cdd:cd14917 538 G--KAKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRI 615
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1988774933 742 PFQEFRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14917 616 LYGDFRQRYRILNPAAIPEgQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
111-793 |
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: 694.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 111 VLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGES 190
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 191 GAGKTENTKKVIQYLAHVASShkggtlGRKKEAVQSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 270
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVT------GEKKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 271 AGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTAD-QYRFLSGGSIPVPGQSDSENFTQTMD 349
Cdd:cd14918 157 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMATDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 350 SMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQK 428
Cdd:cd14918 237 AIDILGFTPEEKVSIYKLTGAVMHYGNMKF-KQKQREEQAEPDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 429 AQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 507
Cdd:cd14918 316 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 508 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKSKQ 586
Cdd:cd14918 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 587 PRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKevdrivgldQVSSGESSAPVTFGAag 664
Cdd:cd14918 471 VKGkaEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFS---------TYASAEADSGAKKGA-- 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 665 lKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 744
Cdd:cd14918 540 -KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYG 618
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1988774933 745 EFRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14918 619 DFKQRYKVLNASAIPEgQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
110-793 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 691.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 190 SGAGKTENTKKVIQYLAHVASSHKggtlgRKKEAVQSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 269
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGD-----KKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 270 VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETrADLLLGTADQYR--FLSGGSIPVPGQSDSENFTQT 347
Cdd:cd14923 157 ATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELLAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 426
Cdd:cd14923 236 DNAIDILGFSSEEKVGIYKLTGAVMHYGNMKF-KQKQREEQAEPDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 427 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 505
Cdd:cd14923 315 TKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 506 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSK 585
Cdd:cd14923 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 586 QP---RGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdriVGLDQVSSGESSapvtfga 662
Cdd:cd14923 470 KPakgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSK------- 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 663 AGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIP 742
Cdd:cd14923 540 KGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRIL 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 743 FQEFRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14923 620 YADFKQRYRILNASAIPEgQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
110-793 |
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: 688.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 190 SGAGKTENTKKVIQYLAHVASshkggTLGRKKEAVQSMQY-GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAV-----TGEKKKEEATSGKMqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTAD-QYRFLSGGSIPVPGQSDSENFTQT 347
Cdd:cd14910 157 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 426
Cdd:cd14910 237 DSAIEILGFTSDERVSIYKLTGAVMHYGNMKF-KQKQREEQAEPDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 427 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 505
Cdd:cd14910 316 TKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 506 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKS 584
Cdd:cd14910 394 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 585 KQPRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivgldqvsSGESSAPVTFGA 662
Cdd:cd14910 471 KPAKGkvEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF-------------SGAAAAEAEEGG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 663 A--GLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNR 740
Cdd:cd14910 538 GkkGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1988774933 741 IPFQEFRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14910 618 ILYADFKQRYKVLNASAIPEgQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
110-793 |
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: 686.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 190 SGAGKTENTKKVIQYLAHVAS-SHKGgtlgrKKEAVQSMQyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRS-----KKENPNANK-GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETrADLLLGTAD--QYRFLSGGSIPVPGQSDSENFTQ 346
Cdd:cd14916 156 GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPEL-LDMLLVTNNpyDYAFVSQGEVSVASIDDSEELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 347 TMDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNTA-AQKLCHLLGVNVLEFTRAILTPRIKVGREY 425
Cdd:cd14916 235 TDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKF-KQKQREEQAEPDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 426 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 504
Cdd:cd14916 314 VTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQpRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 505 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKL-SGEQGSHPKFFK 583
Cdd:cd14916 392 FNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLyDNHLGKSNNFQK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 584 SKQPRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdriVGLDQVSSGESSapvtfg 661
Cdd:cd14916 469 PRNVKGkqEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY---ASADTGDSGKGK------ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 662 aaGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRI 741
Cdd:cd14916 540 --GGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRI 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1988774933 742 PFQEFRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14916 618 LYGDFRQRYRILNPAAIPEgQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
110-793 |
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: 683.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 190 SGAGKTENTKKVIQYLAHVASSHKggtlgRKKEAVQSMQY-GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGE-----KKKEEITSGKMqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTAD-QYRFLSGGSIPVPGQSDSENFTQT 347
Cdd:cd14912 157 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPyDYPFVSQGEISVASIDDQEELMAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 426
Cdd:cd14912 237 DSAIDILGFTNEEKVSIYKLTGAVMHYGNLKF-KQKQREEQAEPDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 427 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 505
Cdd:cd14912 316 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 506 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKS 584
Cdd:cd14912 394 NHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 585 KQPRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdrivgldQVSSGESSApvtfGA 662
Cdd:cd14912 471 KVVKGkaEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGA-------QTAEGASAG----GG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 663 A--GLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNR 740
Cdd:cd14912 540 AkkGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSR 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1988774933 741 IPFQEFRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14912 620 ILYADFKQRYKVLNASAIPEgQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
110-793 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 679.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 190 SGAGKTENTKKVIQYLAHVASSHKggtlGRKKEAVQSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 269
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGE----KKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 270 VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETrADLLLGTADQYRF--LSGGSIPVPGQSDSENFTQT 347
Cdd:cd14915 158 ATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNT-AAQKLCHLLGVNVLEFTRAILTPRIKVGREYV 426
Cdd:cd14915 237 DSAVDILGFSADEKVAIYKLTGAVMHYGNMKF-KQKQREEQAEPDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 427 QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-RQgaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 505
Cdd:cd14915 316 TKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 506 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQ-GSHPKFFKS 584
Cdd:cd14915 394 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 585 KQPRG--EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSdhfvselWKEVDRIVGLDQVSSGESSApvtfGA 662
Cdd:cd14915 471 KPAKGkaEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSG-------MKTLAFLFSGGQTAEAEGGG----GK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 663 AGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIP 742
Cdd:cd14915 540 KGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 743 FQEFRQRYEILTPNAIPR-TFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14915 620 YADFKQRYKVLNASAIPEgQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
110-793 |
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: 670.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 190 SGAGKTENTKKVIQYLAHVASSHKggtlgrkkeavqsmqygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 269
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-----------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 270 VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGA--SEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQ 346
Cdd:cd14883 145 ASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAkhSKELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 347 TMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMK-EKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREY 425
Cdd:cd14883 225 LRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 426 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 505
Cdd:cd14883 305 TEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 506 NHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSK 585
Cdd:cd14883 384 NHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 586 QPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVD--RIVGLDQVSSGESSApvtfgaa 663
Cdd:cd14883 461 RRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDllALTGLSISLGGDTTS------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 664 gLKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPF 743
Cdd:cd14883 534 -RGTSKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTF 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1988774933 744 QEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14883 612 KEFVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
110-793 |
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: 660.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 190 SGAGKTENTKKVIQYLAHVASSHKGGTlgrkkEAVQSMqygelerqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 269
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEV-----ERVKDM--------LLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 270 VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQTM 348
Cdd:cd01378 149 FKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSkSGCFDVDGIDDAADFKEVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 349 DSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREY--- 425
Cdd:cd01378 229 NAMKVIGFTEEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsv 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 426 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 505
Cdd:cd01378 308 YEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 506 nhTMFIL--EQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-RATDRSFVEKLSGEQGSHPKFF 582
Cdd:cd01378 388 --IELTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 583 KSKQPR--GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDrivgldqvssgessapvtf 660
Cdd:cd01378 463 CPSGHFelRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGV------------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 661 gaagLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNR 740
Cdd:cd01378 524 ----DLDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYR 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1988774933 741 IPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd01378 600 QTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
110-793 |
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: 641.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRgkKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 190 SGAGKTENTKKVIQYLAHVAsshkGGTLGrkkeavqsmqygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 269
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALG----GGSSG-------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 270 VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSG-GSIPVPGQSDSENFTQTM 348
Cdd:cd01383 143 AAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQsNCLTIDGVDDAKKFHELK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 349 DSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQK 428
Cdd:cd01383 223 EALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 429 AQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 508
Cdd:cd01383 303 KLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRH 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 509 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPR 588
Cdd:cd01383 383 LFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGERGGA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 589 geadFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLhQSSDHFVSELWKEVDRIVGLDQVSSgessapvtfgaAGLKTK 668
Cdd:cd01383 460 ----FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQLFASKMLDASRKALPL-----------TKASGS 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 669 KGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 748
Cdd:cd01383 524 DSQKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFAR 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1988774933 749 RYEILTPNAiprtfMDGKQaSELMISALELDKN-----LFRVGQSKVFFR 793
Cdd:cd01383 604 RYGFLLPED-----VSASQ-DPLSTSVAILQQFnilpeMYQVGYTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
109-793 |
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: 626.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 188 GESGAGKTENTKKVIQYLAHVASshKGGTLGRKkeavqsmqygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 267
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGG--RAVTEGRS-----------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 268 FDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQ 346
Cdd:cd01384 148 FDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNqSKCFELDGVDDAEEYRA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 347 TMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKL---CHLLGVNVLEFTRAILTPRIKVGR 423
Cdd:cd01384 228 TRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDALCKRVIVTPD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 424 EYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 503
Cdd:cd01384 308 GIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 504 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFK 583
Cdd:cd01384 387 HFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 584 SKQPRgeADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRivgldqvsSGESSApvtfgaa 663
Cdd:cd01384 464 PKLSR--TDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR--------EGTSSS------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 664 glkTKkgmFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPF 743
Cdd:cd01384 527 ---SK---FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPF 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1988774933 744 QEFRQRYEILTPNAIPRTFmDGKQASELMISALELDKnlFRVGQSKVFFR 793
Cdd:cd01384 601 EEFLDRFGLLAPEVLKGSD-DEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
109-793 |
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: 625.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVasshkggtlgrkkeavqSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAI-----------------SGQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQT 347
Cdd:cd01381 144 NKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTqGNCLTCEGRDDAAEFADI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFMK--EKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREY 425
Cdd:cd01381 224 RSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGET 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 426 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAS--FIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 503
Cdd:cd01381 304 VVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 504 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFF 582
Cdd:cd01381 384 FFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 583 KSKQpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFvselwkeVDRIVGLDQVSSGESSApvtfga 662
Cdd:cd01381 460 KPKS-DLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKF-------LKQLFNEDISMGSETRK------ 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 663 aglKTKkgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIP 742
Cdd:cd01381 526 ---KSP-----TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHT 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1988774933 743 FQEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd01381 598 FEEFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
109-793 |
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: 576.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVASSHKGgtlgrkkeavqsmqygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-----------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLllGTADQYRFLS-GGSIPVPGQSDSENFTQT 347
Cdd:cd14872 144 DNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGW--GSSAAYGYLSlSGCIEVEGVDDVADFEEV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISF---MKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKV-GR 423
Cdd:cd14872 222 VLAMEQLGFDDADINNVMSLIAAILKLGNIEFasgGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 424 EYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 503
Cdd:cd14872 302 DPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 504 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFK 583
Cdd:cd14872 382 HFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVY 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 584 SKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivgldqvssgessaPVTFGAA 663
Cdd:cd14872 459 AEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF-------------------PPSEGDQ 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 664 glKTKKGmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPF 743
Cdd:cd14872 520 --KTSKV---TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSH 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1988774933 744 QEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14872 595 ERFLKRYRFLVKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
109-793 |
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: 569.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 188 GESGAGKTENTKKVIQYLAHVasshkGGTLGrkkeavqsmqyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 267
Cdd:cd01382 81 GESGAGKTESTKYILRYLTES-----WGSGA-----------GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 268 FDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGtadqyrflsggsipvPGQSDSENFTQT 347
Cdd:cd01382 145 FNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKD---------------PLLDDVGDFIRM 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFmkEKNHDQA---SMPDNTAAQKL---CHLLGVNVLEF-----TRAILT 416
Cdd:cd01382 210 DKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEF--EENGSDSgggCNVKPKSEQSLeyaAELLGLDQDELrvsltTRVMQT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 417 PRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRrqRQGASFIGILDIAGFEIFQLNSFEQLCINY 496
Cdd:cd01382 288 TRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPF--ETSSYFIGVLDIAGFEYFEVNSFEQFCINY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 497 TNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPRATDRSFVEKLSGEQG 576
Cdd:cd01382 366 CNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHK 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 577 SH-----PKFFKSKQPRGEAD---FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKevdrivglDQ 648
Cdd:cd01382 443 NHfrlsiPRKSKLKIHRNLRDdegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFE--------SS 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 649 VSSGESSAPvtfgaaglKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLE 728
Cdd:cd01382 515 TNNNKDSKQ--------KAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVS 586
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774933 729 GIRICRQGFPNRIPFQEFRQRYEILTPNAI----PRTFmdgkqaSELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd01382 587 VLDLMQGGFPSRTSFHDLYNMYKKYLPPKLarldPRLF------CKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
109-793 |
2.13e-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: 562.09 E-value: 2.13e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQ----DREDQS 183
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 184 ILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQSMQ--YGELERQLLQANPILEAFGNAKTVKNDNSSRFG 261
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEAIEqtLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 262 KFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDS 341
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 342 ENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFmkEKNHDQASMPDNTAAQKLCH---LLGVNVLEFTRAILTPR 418
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDF--ESENDTTVLEDATTLQSLKLaaeLLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 419 IKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQgASFIGILDIAGFEIFQLNSFEQLCINYTN 498
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 499 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPRAT--DRSFVEKL---- 571
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLhasf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 572 ---------SGEQGSHPKFFkskQPRGEAD--FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDhfvselwkev 640
Cdd:cd14890 476 grksgsggtRRGSSQHPHFV---HPKFDADkqFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRR---------- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 641 drivGLDQVSsgessapvtfgaaglktkkgmfrtVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQ 720
Cdd:cd14890 543 ----SIREVS------------------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQ 594
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774933 721 LRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPNAiprtfMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14890 595 LKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
109-793 |
1.03e-175 |
|
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: 549.36 E-value: 1.03e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVASShkGGTLgrkkeavqsmqygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQR--RNNL--------------VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DvAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQT 347
Cdd:cd01387 145 E-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNqGGNCEIAGKSDADDFRRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFMK---EKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGRE 424
Cdd:cd01387 224 LAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKrqlRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 425 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINrALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 504
Cdd:cd01387 304 RIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 505 FNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKs 584
Cdd:cd01387 383 FNKHVFKLEQEEYIREQIDWTEIAFA-DNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSK- 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 585 kqPR-GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKevdrivgldQVSSGESSAPVTFGAA 663
Cdd:cd01387 459 --PRmPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFS---------SHRAQTDKAPPRLGKG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 664 GLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPF 743
Cdd:cd01387 528 RFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPF 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1988774933 744 QEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd01387 608 QVFIDRYRCLVALKLPRPAPGDMCVSLLSRLCTVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
109-793 |
2.80e-174 |
|
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: 546.59 E-value: 2.80e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLahVASSHKGGTLGrkkeavqsmqygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKGYGSG-------------VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQT 347
Cdd:cd01385 146 RENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFERL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEK-NHDQASMPDNTAAQKL-CHLLGVNVLEFTRAILTPRIKVGREY 425
Cdd:cd01385 226 KQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVGET 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 426 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL----DRRQRQGASfIGILDIAGFEIFQLNSFEQLCINYTNEKL 501
Cdd:cd01385 306 LILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 502 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPkf 581
Cdd:cd01385 385 QYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNK-- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 582 FKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELwkevdriVGLDQV------------ 649
Cdd:cd01385 460 YYEKPQVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVavfrwavlraff 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 650 -------------------SSGESSAPVTFGAAGL-KTKKGMfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRA 709
Cdd:cd01385 533 ramaafreagrrraqrtagHSLTLHDRTTKSLLHLhKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKP 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 710 GKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMisalELDKNLFRVGQSK 789
Cdd:cd01385 611 LRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKL----NLDRDNYQIGKTK 686
|
....
gi 1988774933 790 VFFR 793
Cdd:cd01385 687 VFLK 690
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
109-793 |
3.99e-172 |
|
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: 539.73 E-value: 3.99e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEM---PPHIYAISEAAYRSMLQDR----ED 181
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 182 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQSmqygELERQLLQANPILEAFGNAKTVKNDNSSRFG 261
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHE----SIEECVLLSNLILEAFGNAKTIRNDNSSRFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 262 KFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGS-IPVPGQSD 340
Cdd:cd14892 157 KYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 341 SENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFmkEKNHDQ----ASMPDNTAAQKLCHLLGVNVLEFTRAILT 416
Cdd:cd14892 237 ATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 417 PRIKVGR-EYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQ---------GASFIGILDIAGFEIFQL 486
Cdd:cd14892 315 QTTSTARgSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 487 NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPR-ATDR 565
Cdd:cd14892 395 NSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKRkTTDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 566 SFVEKLSGEQGSHPKFFksKQPRGEAD-FSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDhfvselwkevdriv 644
Cdd:cd14892 472 QLLTIYHQTHLDKHPHY--AKPRFECDeFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK-------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 645 gldqvssgessapvtfgaaglktkkgmFRTvgqlykeSLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCN 724
Cdd:cd14892 536 ---------------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYS 581
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774933 725 GVLEGIRICRQGFPNRIPFQEFRQRYEILTPN-AIPRTFMDGKQASELM-----ISALELDKNLFRVGQSKVFFR 793
Cdd:cd14892 582 GVLEVVRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
109-791 |
4.89e-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: 539.38 E-value: 4.89e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMY------RGKKRHEMPPHIYAISEAAYRSMLQDRE-- 180
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 181 --DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQSmqygelerQLLQANPILEAFGNAKTVKNDNSS 258
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRD--------RVLESNPILEAFGNARTNRNNNSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 259 RFGKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFL--SGGSIPVP 336
Cdd:cd14901 153 RFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 337 GQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFM-KEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAIL 415
Cdd:cd14901 233 GVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVkKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 416 TPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAS-FIGILDIAGFEIFQLNSFEQLCI 494
Cdd:cd14901 313 TREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 495 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATDRSFVEKLSGE 574
Cdd:cd14901 393 NFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 575 QGSHPKFFKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSElwkevdrivgldqvssges 654
Cdd:cd14901 470 LAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 655 sapvtfgaaglktkkgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICR 734
Cdd:cd14901 531 -------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISR 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 735 QGFPNRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNL-----FRVGQSKVF 791
Cdd:cd14901 592 SGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIehlppFQVGKTKVF 653
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
109-793 |
4.28e-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: 534.36 E-value: 4.28e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 188 GESGAGKTENTKKVIQYLAHVASSHKGGTLgrkkeavqsmqygeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 267
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLNDSTI----------------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 268 FDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRadLLLGTADQYRFL-SGGSIPVPGQSDSENFTQ 346
Cdd:cd14903 145 FDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEER--LFLDSANECAYTgANKTIKIEGMSDRKHFAR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 347 TMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASM--PDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGRE 424
Cdd:cd14903 223 TKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 425 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 504
Cdd:cd14903 303 VYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 505 FNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPRATDRSFVEKLSG---EQGSHPKF 581
Cdd:cd14903 382 FTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLSSihkDEQDVIEF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 582 fkskqPR-GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVSSGESSAPVTF 660
Cdd:cd14903 458 -----PRtSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRG 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 661 GAAGLKtkkgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNR 740
Cdd:cd14903 533 GALTTT-------TVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNR 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1988774933 741 IPFQEFRQRYEILTPNAiPRTFMDGKQASELMISALELDK-NLFRVGQSKVFFR 793
Cdd:cd14903 606 LLHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
110-793 |
3.60e-169 |
|
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: 530.70 E-value: 3.60e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 190 SGAGKTENTKKVIQYLAHvasshkggtLGRKKeavqsmqYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 269
Cdd:cd01379 82 SGAGKTESANLLVQQLTV---------LGKAN-------NRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 270 VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETR-ADLLLGTADQYRFLSGGSIPVPG----QSDSENF 344
Cdd:cd01379 146 STGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDivnnSGNREKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 345 TQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISF----MKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAiLTPRIK 420
Cdd:cd01379 226 EEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFteveSNHQTDKSSRISNPEALNNVAKLLGIEADELQEA-LTSHSV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 421 VGR-EYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL--DRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYT 497
Cdd:cd01379 305 VTRgETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 498 NEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPRATDRSFVEKLsgEQG 576
Cdd:cd01379 385 NEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKF--HNN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 577 SHPKFFkSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSElwkevdrivgldqvssgessa 656
Cdd:cd01379 459 IKSKYY-WRPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ--------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 657 pvtfgaaglktkkgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQG 736
Cdd:cd01379 517 -----------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQG 579
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774933 737 FPNRIPFQEFRQRYEILTPNAIPRTFMDgKQASELMISALELDKnlFRVGQSKVFFR 793
Cdd:cd01379 580 FSHRILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
109-793 |
1.00e-168 |
|
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: 529.65 E-value: 1.00e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKK-RHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 188 GESGAGKTENTKKVIQYLAHVASShkggtlgrkkeavqsmQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 267
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS----------------DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 268 FDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSEN---- 343
Cdd:cd14897 145 FTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDSEEleyy 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 344 ---FTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIK 420
Cdd:cd14897 225 rqmFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 421 VGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL----DRRQRQGASFIGILDIAGFEIFQLNSFEQLCINY 496
Cdd:cd14897 305 IRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 497 TNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQG 576
Cdd:cd14897 385 SNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 577 SHPKFfkSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKevdrivgldqvssgessa 656
Cdd:cd14897 462 ESPRY--VASPGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT------------------ 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 657 pvtfgaaglktkkgmfrtvgQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQG 736
Cdd:cd14897 522 --------------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDG 581
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774933 737 FPNRIPFQEFRQRYEILTPNaiPRTFMDGKQASELMISALELDKNlFRVGQSKVFFR 793
Cdd:cd14897 582 YPIRIKYEDFVKRYKEICDF--SNKVRSDDLGKCQKILKTAGIKG-YQFGKTKVFLK 635
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
109-793 |
4.15e-166 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 523.20 E-value: 4.15e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 188 GESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVqsmqygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 267
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCV--------EQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 268 FDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQ 346
Cdd:cd14873 153 ICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 347 TMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMkekNHDQASMPDNTAAQKLCHLLGVNVLEFTRAiLTPRIKVGR-EY 425
Cdd:cd14873 233 VITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQRSMFLRgEE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 426 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALdrRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 505
Cdd:cd14873 309 ILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 506 NHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKsk 585
Cdd:cd14873 387 NKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVK-- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 586 qPR-GEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDrivgldqvSSGESSAPVTfgaaG 664
Cdd:cd14873 461 -PRvAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVS--------SRNNQDTLKC----G 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 665 LKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 744
Cdd:cd14873 528 SKHRR---PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQ 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1988774933 745 EFRQRYEILTPNAIPRTFMDGKQASelMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14873 605 DFYKRYKVLMRNLALPEDVRGKCTS--LLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
109-755 |
1.14e-162 |
|
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: 514.24 E-value: 1.14e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRgKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 188 GESGAGKTENTKKVIQYLAHVASSHKggtlgRKKEAVqsmqygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 267
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDI-----KKRSLV--------EAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 268 FD---------VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLlCGASEETR-ADLLLGTADQYRFLSGGSIPV-- 335
Cdd:cd14888 147 FSklkskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQL-CAAAREAKnTGLSYEENDEKLAKGADAKPIsi 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 336 ----------------------PGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDN 393
Cdd:cd14888 226 dmssfephlkfryltksschelPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 394 TAAQKL---CHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGA 470
Cdd:cd14888 306 SCTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 471 SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVL 550
Cdd:cd14888 386 LFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 551 ALLDEECWFPRATDRSFVEKLSGEQGSHPKF--FKSKQprgeADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQS 628
Cdd:cd14888 463 CMLDEECFVPGGKDQGLCNKLCQKHKGHKRFdvVKTDP----NSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNS 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 629 SDHFVSELWKE-VDRIVgldqvssgessapvtfgaaGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEK 707
Cdd:cd14888 539 KNPFISNLFSAyLRRGT-------------------DGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQN 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1988774933 708 RAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTP 755
Cdd:cd14888 600 VPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
109-793 |
8.56e-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: 470.67 E-value: 8.56e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRH--------EMPPHIYAISEAAYRSMLQDR 179
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 180 EDQSILCTGESGAGKTENTKKVIQYL----AHVASSHKGGTLGRKKEAVQSMQYGeLERQLLQANPILEAFGNAKTVKND 255
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLtqlsQQEQNSEEVLTLTSSIRATSKSTKS-IEQKILSCNPILEAFGNAKTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 256 NSSRFGKFIRINFD-VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLL---GTADQYRFLS-G 330
Cdd:cd14907 160 NSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLknqLSGDRYDYLKkS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 331 GSIPVPGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEK-NHDQASMPDNTAA-QKLCHLLGVNVL 408
Cdd:cd14907 240 NCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTlDDNSPCCVKNKETlQIIAKLLGIDEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 409 EFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL------DRRQRQGASF-IGILDIAGF 481
Cdd:cd14907 320 ELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYLsIGLLDIFGF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 482 EIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWF 559
Cdd:cd14907 400 EVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 560 PRATDRSFVEKLSGEQGSHPKFFKSKQPRGEAdFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWke 639
Cdd:cd14907 477 ATGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF-- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 640 vdriVGLDQVSSGESSAPVtfgaaglKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLD 719
Cdd:cd14907 554 ----SGEDGSQQQNQSKQK-------KSQKKD-KFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLN 621
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774933 720 QLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEiltpnaiprtfmdgkqaselmisalELDKNLFrVGQSKVFFR 793
Cdd:cd14907 622 QIRYLGVLESIRVRKQGYPYRKSYEDFYKQYS-------------------------LLKKNVL-FGKTKIFMK 669
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
110-760 |
2.16e-146 |
|
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: 468.25 E-value: 2.16e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMY-----------RGKKRHEMPPHIYAISEAAYRSM-- 175
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 176 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVasshkgGTLGRKKEAVQSMQYGELERQLLQANPILEAFGNAKTVK 253
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQA------GDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 254 NDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRAdlllgtadqyrflsggsi 333
Cdd:cd14900 156 NDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------------------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 334 pvpgqsdSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISF-MKEKNHDQASMPDNTAAQKL------CHLLGVN 406
Cdd:cd14900 218 -------RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFeHDENSDRLGQLKSDLAPSSIwsrdaaATLLSVD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 407 VLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL---DRRQRQGAS-FIGILDIAGFE 482
Cdd:cd14900 291 ATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 483 IFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRA 562
Cdd:cd14900 371 VFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 563 TDRSFVEKLSGEQGSHPKFFKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDplndnvasLLHQSSdhfvselwkeVDr 642
Cdd:cd14900 448 SDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------VD- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 643 ivgldqvssgessapvtfgaaglktkkgMFRTVGQlYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLR 722
Cdd:cd14900 509 ----------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLR 559
|
650 660 670
....*....|....*....|....*....|....*...
gi 1988774933 723 CNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPNAIPR 760
Cdd:cd14900 560 CNGVMEAVRVARAGFPIRLLHDEFVARYFSLARAKNRL 597
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
111-793 |
3.50e-144 |
|
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: 463.22 E-value: 3.50e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 111 VLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSML----QDREDQSILC 186
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 187 TGESGAGKTENTKKVIQYLAHVAsshKGGTlgrkkeavqsmqygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 266
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---RGNS--------------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 267 NFDvAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSipvpGQSDS----- 341
Cdd:cd14889 146 RFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGA----GCKREvqywk 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 342 ENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISF-MKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAiLTPRIK 420
Cdd:cd14889 221 KKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFeMDDDEALKVENDSNGWLKAAAGQFGVSEEDLLKT-LTCTVT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 421 VGR-EYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQG--ASFIGILDIAGFEIFQLNSFEQLCINYT 497
Cdd:cd14889 300 FTRgEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 498 NEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIerPANPPGVLALLDEECWFPRATDRSFVEKLSGEQGS 577
Cdd:cd14889 380 NEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKG 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 578 HPKFFKSKqpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEvdRIVGLDQVSSGESSAP 657
Cdd:cd14889 457 NSYYGKSR--SKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTA--TRSRTGTLMPRAKLPQ 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 658 VTFGAAGLKTKKgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGF 737
Cdd:cd14889 533 AGSDNFNSTRKQ----SVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGF 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774933 738 PNRIPFQEFRQRYEIL--TPNaIPRTfmdgKQASELMISALELDKnlFRVGQSKVFFR 793
Cdd:cd14889 609 SWRPSFAEFAERYKILlcEPA-LPGT----KQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
109-793 |
1.74e-137 |
|
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: 445.51 E-value: 1.74e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYR--GKKRHE-------MPPHIYAISEAAYRSMLQD- 178
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 179 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTlgrkkEAVQSMQYGELERQLLQANPILEAFGNAKTVKNDNSS 258
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAP-----NEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 259 RFGKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRA-----DLLLGT---ADQYRFLSG 330
Cdd:cd14908 156 RFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyefhDGITGGlqlPNEFHYTGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 331 GSIPVPGQ-SDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNTAAQK----LCHLLGV 405
Cdd:cd14908 236 GGAPDLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEF-ESKEEDGAAEIAEEGNEKclarVAKLLGV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 406 NVLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL--DRRQRQGASfIGILDIAGFEI 483
Cdd:cd14908 315 DVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFEC 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 484 FQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP-RA 562
Cdd:cd14908 394 FAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 563 TDRSFVEKL--------SGEQGSHPKFFKSKQPRGEADFSIIHYAGKVDYKA-NDWLVKNMDPLNdnvasllhqssdhfv 633
Cdd:cd14908 471 SDANYASRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIP--------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 634 selwkevdrivgldqvssgessapvtfgaaglKTKKGMFRTvGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLS 713
Cdd:cd14908 536 --------------------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVT 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 714 PHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPnAIPRT----FMDGKQASEL-----------------M 772
Cdd:cd14908 583 RKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVvlswSMERLDPQKLcvkkmckdlvkgvlspaM 661
|
730 740
....*....|....*....|.
gi 1988774933 773 ISALELDKNLFRVGQSKVFFR 793
Cdd:cd14908 662 VSMKNIPEDTMQLGKSKVFMR 682
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
109-793 |
8.78e-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: 442.46 E-value: 8.78e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 188 GESGAGKTENTKKVIQYLAHVASSHKGGTLGRkkeavqsmqygelerqLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 267
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTIAK----------------VIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 268 FDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGG--SIPVPGQSDSENFT 345
Cdd:cd14904 145 FDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSlaQMQIPGLDDAKLFA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 346 QTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMpDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREY 425
Cdd:cd14904 225 STQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRIS-NGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNES 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 426 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 505
Cdd:cd14904 304 VTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 506 NHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPRATDRSFVEKL---SGEQGSHP--K 580
Cdd:cd14904 384 TTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNEsiD 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 581 FFKSKQPRgeadFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWkevdrivgldqvSSGESSAPVTF 660
Cdd:cd14904 460 FPKVKRTQ----FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF------------GSSEAPSETKE 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 661 GAAGLKTKKGmfRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNR 740
Cdd:cd14904 524 GKSGKGTKAP--KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSR 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1988774933 741 IPFQEFRQRYEILTPNAIPRTfmDGKQASELMISALELDKNL-FRVGQSKVFFR 793
Cdd:cd14904 602 LTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIGRKSPLeYQIGKSLIYFK 653
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
109-793 |
1.15e-136 |
|
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: 441.79 E-value: 1.15e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERyySGLI----YTYSGLFCVVVNPYKNLPiytESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDRE---D 181
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 182 QSILCTGESGAGKTENTKKVIQYLAH--VASSHKGGTLGRKKEAVQSMQYGELERQLLQANPILEAFGNAKTVKNDNSSR 259
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTraVGGKKASGQDIEQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 260 FGKFIRINFDVAGY-IVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPG 337
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 338 QSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEK----NHDQASMPDNTAAQKLCHLLGVNVLEFTRA 413
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDtsegEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 414 ILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrRQRQGASFIGILDIAGFEIFQL-NSFEQL 492
Cdd:cd14891 316 ITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLG-HDPDPLPYIGVLDIFGFESFETkNDFEQL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 493 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATDRSFVEKLS 572
Cdd:cd14891 395 LINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNETLH 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 573 GEQGSHPKFFKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSsdhfvselwkevdrivgldqvssg 652
Cdd:cd14891 472 KTHKRHPCFPRPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS------------------------ 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 653 essapvtfgaaglktkkgmfrtvgQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRI 732
Cdd:cd14891 528 ------------------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEV 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 733 CRQGFPNRIPFQEFRQRYEILTPNAIPRTFMDGKQA-SELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14891 584 LKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
109-793 |
7.05e-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: 431.13 E-value: 7.05e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAhvasshkggtlgrkkeAVQSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLS----------------SLYQDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DvAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQT 347
Cdd:cd14896 145 Q-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNqGGACRLQGKEDAQDFEGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQ--ASMPDNTAAQKLCHLLGVNVlEFTRAILTPRIKV---G 422
Cdd:cd14896 224 LKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPP-ERLEGAVTHRVTEtpyG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 423 ReyVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALD-RRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKL 501
Cdd:cd14896 303 R--VSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLApPGEAESDATIGVVDAYGFEALRVNGLEQLCINLASERL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 502 QQLFNHTMFILEQEEYQREGIEWNFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKF 581
Cdd:cd14896 381 QLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSY 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 582 FKSKQPRgeADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQvssgessapvtfG 661
Cdd:cd14896 458 AKPQLPL--PVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQ------------G 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 662 AAGLKTKkgmfrtvgqlYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRI 741
Cdd:cd14896 524 KPTLASR----------FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRV 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 742 PFQEFRQRYEILTPNAIPrTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14896 594 PFQAFLARFGALGSERQE-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
110-793 |
9.59e-132 |
|
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: 430.14 E-value: 9.59e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPiytesivEMYRGKKRHE-------MPPHIYAISEAAYRSMLQ----- 177
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 178 --DREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAVQSmqygeleRQLLQANPILEAFGNAKTVKND 255
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISG-------SELLSANPILESFGNARTLRND 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 256 NSSRFGKFIRINF-----DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEE--TRADLLLGTADQYRFL 328
Cdd:cd14895 148 NSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmkLELQLELLSAQEFQYI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 329 SGGSIPV--PGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHD---------------QASMP 391
Cdd:cd14895 228 SGGQCYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 392 DNTAAQKL---CHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQ-- 466
Cdd:cd14895 308 SLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfa 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 467 --------RQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCID 538
Cdd:cd14895 388 lnpnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 539 LIErpANPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLN 618
Cdd:cd14895 467 MLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPN 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 619 DNVASLLHQSSDHFVSELWKEVDRIVgldqvssgesSAPVTFGAAGLKTKKGMFRTV--GQLYKESLTKLMATLRNTNPN 696
Cdd:cd14895 545 AELFSVLGKTSDAHLRELFEFFKASE----------SAELSLGQPKLRRRSSVLSSVgiGSQFKQQLASLLDVVQQTQTH 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 697 FLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISAL 776
Cdd:cd14895 615 YIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHA 694
|
730
....*....|....*..
gi 1988774933 777 ELdknlfrvGQSKVFFR 793
Cdd:cd14895 695 EL-------GKTRVFLR 704
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
99-804 |
2.65e-128 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 424.44 E-value: 2.65e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 99 DMADLTCLNEASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHE-MPPHIYAISEAAYRSMLQ 177
Cdd:PTZ00014 100 DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 178 DREDQSILCTGESGAGKTENTKKVIQYLAhvasSHKGGTLGRKkeavqsmqygeLERQLLQANPILEAFGNAKTVKNDNS 257
Cdd:PTZ00014 180 VKKSQTIIVSGESGAGKTEATKQIMRYFA----SSKSGNMDLK-----------IQNAIMAANPVLEAFGNAKTIRNNNS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 258 SRFGKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPG 337
Cdd:PTZ00014 245 SRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 338 QSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFM-KEKN-HDQASM--PDNTAA-QKLCHLLGVNVLEFTR 412
Cdd:PTZ00014 325 IDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEgKEEGgLTDAAAisDESLEVfNEACELLFLDYESLKK 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 413 AILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAsFIGILDIAGFEIFQLNSFEQL 492
Cdd:PTZ00014 405 ELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQL 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 493 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPRATDRSFVEKLS 572
Cdd:PTZ00014 484 FINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCN 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 573 GEQGSHPKFFKSKQpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdrivgldQVSSG 652
Cdd:PTZ00014 561 TNLKNNPKYKPAKV-DSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGV-------EVEKG 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 653 essapvtfgaaglKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRI 732
Cdd:PTZ00014 633 -------------KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQL 697
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774933 733 CRQGFPNRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR---AGVLAHLEEER 804
Cdd:PTZ00014 698 RQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREK 772
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
109-755 |
1.45e-126 |
|
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: 415.83 E-value: 1.45e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYR--------GKKRHEMPPHIYAISEAAYRSMLQ-D 178
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 179 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTlgrkKEAVQSMqygELERQLLQANPILEAFGNAKTVKNDNSS 258
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTE----QEGSDAV---EIGKRILQTNPILESFGNAQTIRNDNSS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 259 RFGKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFL-----SGGSI 333
Cdd:cd14902 154 RFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLnsygpSFARK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 334 PVPGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDqasmpDNTAAQKLC--------HLLGV 405
Cdd:cd14902 234 RAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQE-----DATAVTAASrfhlakcaELMGV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 406 NVLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALD--------RRQRQGASFIGILD 477
Cdd:cd14902 309 DVDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 478 IAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEEC 557
Cdd:cd14902 389 IFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQEC 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 558 WFPRATDRSFVEklsgeqgshpKFFKSKQPRGEadFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELw 637
Cdd:cd14902 466 LMPKGSNQALST----------KFYRYHGGLGQ--FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAI- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 638 kevdrivGLDqvssGESSAPVTFGAAGLKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPH 715
Cdd:cd14902 533 -------GAD----ENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRE 601
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1988774933 716 LVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTP 755
Cdd:cd14902 602 RMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
109-793 |
3.46e-125 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 410.93 E-value: 3.46e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVASSHKGGTlgrKKEAVQSmqygelerqllqANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVL---SVEKLNA------------ALTVLEAFGNVRTALNGNATRFSQLFSLDF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLG--TADQYRFLSGGSIPVPGQSDSENFTQ 346
Cdd:cd01386 146 DQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNqlAESNSFGIVPLQKPEDKQKAAAAFSK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 347 TMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAI------------ 414
Cdd:cd01386 226 LQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqs 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 415 LTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASfIGILDIAGfeiFQLN------- 487
Cdd:cd01386 306 TTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPG---FQNPahsgsqr 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 488 --SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERP---ANPP---------GVLALL 553
Cdd:cd01386 382 gaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 554 DEECWFPRATDRSFVEKLS---GEQGS---HPKFFKSKQPRgeaDFSIIHYAGK--VDYKANDWLVK-NMDPLNDNVASL 624
Cdd:cd01386 462 DEEALYPGSSDDTFLERLFshyGDKEGgkgHSLLRRSEGPL---QFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQL 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 625 LHQSSDHFvselwkevdrivgldqvssgessapvtfgaAGLKtKKGMFRTVgqlyKESLTKLMATLRNTNPNFLRCIIPN 704
Cdd:cd01386 539 LQESQKET------------------------------AAVK-RKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQ 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 705 HE------KRAGKLSPHLVLD------QLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTP-----NAIPRTFMDGKQ 767
Cdd:cd01386 584 HNagkderSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkkLGLNSEVADERK 663
|
730 740
....*....|....*....|....*.
gi 1988774933 768 ASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd01386 664 AVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
109-791 |
2.10e-123 |
|
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: 404.37 E-value: 2.10e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRH-EMPPHIYAISEAAYRSMLQDREDQSILCT 187
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 188 GESGAGKTENTKKVIQYLAhvaSSHKGGTLGRKKEAVqsmqygelerqlLQANPILEAFGNAKTVKNDNSSRFGKFIRIn 267
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRIQTAI------------MAANPVLEAFGNAKTIRNNNSSRFGRFMQL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 268 fDVA--GYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFT 345
Cdd:cd14876 145 -DVAseGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 346 QTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKnhdQASMPDntAA----------QKLCHLLGVNVLEFTRAIL 415
Cdd:cd14876 224 EVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKT---EQGVDD--AAaisneslevfKEACSLLFLDPEALKRELT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 416 TPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAsFIGILDIAGFEIFQLNSFEQLCIN 495
Cdd:cd14876 299 VKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFIN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 496 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPRATDRSFVEKLSGEQ 575
Cdd:cd14876 378 ITNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 576 GSHPKFFKSKQpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdrivgldqvssgess 655
Cdd:cd14876 455 KSNGKFKPAKV-DSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGV--------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 656 aPVTFGaaglKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQ 735
Cdd:cd14876 519 -VVEKG----KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQL 591
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774933 736 GFPNRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVF 791
Cdd:cd14876 592 GYSYRRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
109-791 |
7.11e-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: 402.44 E-value: 7.11e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKR-HEMPPHIYAISEAAYRSMLQDREDQSILC 186
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 187 TGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEAvqsmqyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 266
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNN------NSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 267 NFDVAGYIV-GANIETYLLEKSRAT-RQAKDERTFHIFYQLLCGASEETRADLLLGT-ADQYRFL--------------S 329
Cdd:cd14906 155 EFRSSDGKIdGASIETYLLEKSRIShRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqsS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 330 GGSIPVPGQSDS-ENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQAS--MPDNTAA-QKLCHLLGV 405
Cdd:cd14906 235 NKNSNHNNKTESiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 406 NVLEFTRAILTPRIKVGREYVQKAQTKE--QADFAVEALAKATYERLFRWLVHRINRALDR----RQRQGAS------FI 473
Cdd:cd14906 315 IESVFKQALLNRNLKAGGRGSVYCRPMEvaQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsNDLAGGSnkknnlFI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 474 GILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALL 553
Cdd:cd14906 395 GVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 554 DEECWFPRATDRSFVEKLSGEQGSHPKFFKSKQPRGEadFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFV 633
Cdd:cd14906 472 DDECIMPKGSEQSLLEKYNKQYHNTNQYYQRTLAKGT--LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 634 SELWkevdrivgldqvSSGESSAPVTfgaaglKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLS 713
Cdd:cd14906 550 KSLF------------QQQITSTTNT------TKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFN 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 714 PHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISALEL--------------- 778
Cdd:cd14906 612 NVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSklktmgisnnkkknn 691
|
730 740
....*....|....*....|..
gi 1988774933 779 ---------DKNLFRVGQSKVF 791
Cdd:cd14906 692 snsnsnttnDKPLFQIGKTKIF 713
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
109-755 |
1.44e-120 |
|
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: 396.91 E-value: 1.44e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKR-HEMPPHIYAISEAAYRSMLQDRE--DQSI 184
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 185 LCTGESGAGKTENTKKVIQYLAHVASSHKGGTLGRKKEavqsmqygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFI 264
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAE--------RIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 265 RINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLsggsiPVPGQS-DSEN 343
Cdd:cd14880 153 QLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL-----PNPERNlEEDC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 344 FTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTA---AQKLCHLLGVNVLEFTRAILTPRIK 420
Cdd:cd14880 228 FEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 421 VGREYV--QKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTN 498
Cdd:cd14880 308 AGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYAN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 499 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATD----RSFVEK-LSG 573
Cdd:cd14880 388 EKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSaaqlQTRIESaLAG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 574 EQG-SHPKFfkSKQPrgeaDFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLDQVsSG 652
Cdd:cd14880 465 NPClGHNKL--SREP----SFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEP-SG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 653 ESSAPVTfgaaglktkkgmfrTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRI 732
Cdd:cd14880 538 QSRAPVL--------------TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHI 603
|
650 660
....*....|....*....|...
gi 1988774933 733 CRQGFPNRIPFQEFRQRYEILTP 755
Cdd:cd14880 604 SAAGFPIRVSHQNFVERYKLLRR 626
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
109-793 |
1.30e-115 |
|
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: 382.62 E-value: 1.30e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYS-GLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRG-KKRHEMPPHIYAISEAAYRSM-LQDREDQSIL 185
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 186 CTGESGAGKTENTKKVIQYLAHVASSHKGGTlgrkkeaVQSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 265
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNT-------SQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 266 INFD-VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADL-LLGTADQYRFLSGGSI----PVPGQ- 338
Cdd:cd14875 154 LYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDGKt 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 339 -SDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFmKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILtp 417
Cdd:cd14875 234 lDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEF-ESDQNDKAQIADETPFLTACRLLQLDPAKLRECFL-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 418 rIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQR-QGASFIGILDIAGFEIFQLNSFEQLCINY 496
Cdd:cd14875 311 -VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDcSGCKYIGLLDIFGFENFTRNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 497 TNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPRATDRSFVEKLSGEQG 576
Cdd:cd14875 390 ANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQWA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 577 SHPKFF---KSKQPRgeaDFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELwkevdrivgldqvssge 653
Cdd:cd14875 467 NKSPYFvlpKSTIPN---QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL----------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 654 ssapvtfgaagLKTKKGMFR---TVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGI 730
Cdd:cd14875 527 -----------LSTEKGLARrkqTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTI 595
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 731 RICRQGFPNRIPFQEFRQRYEILTPNAIPRTFMDGKqASELMISALELDKNLFR-------VGQSKVFFR 793
Cdd:cd14875 596 ALKRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQEK-YSEAAKDFLAYYQRLYGwakpnyaVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
109-793 |
9.27e-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: 374.22 E-value: 9.27e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRH-----EMPPHIYAISEAAYRSMLQDREDQ 182
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 183 SILCTGESGAGKTENTKKVIQYLAHVASShkggtlgrKKEAVQSMqygelerqLLQANPILEAFGNAKTVKNDNSSRFGK 262
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHST--------SSTDVQSL--------ILGSNPLLESFGNAKTLRNNNSSRFGK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 263 FIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSI-PVPGQSDS 341
Cdd:cd14886 145 FIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGIDDQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 342 ENFTQTMDSMAIMgFTPEELMSMLKVISAVLQFGNISFMKEKNH---DQASMPDNTAAQKLCHLLGVNVLEFTRAILTPR 418
Cdd:cd14886 225 KEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMgviNAAKISNDEDFGKMCELLGIESSKAAQAIITKV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 419 IKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALdRRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTN 498
Cdd:cd14886 304 VVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYAN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 499 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPRATDRSFVEKLSgeqgSH 578
Cdd:cd14886 383 ERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSSCK----SK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 579 PK---FFKSKQprGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRIVGLdqvssgess 655
Cdd:cd14886 456 IKnnsFIPGKG--SQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN--------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 656 apvtfgaaglktKKGMFrtVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQ 735
Cdd:cd14886 525 ------------MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHR 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 736 GFPNRIPFQEFRQRYEILT--PNAIPRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14886 591 GFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
109-750 |
4.30e-107 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 360.18 E-value: 4.30e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMY----------RGKKRHEMPPHIYAISEAAYRSMLQ 177
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 178 DREDQSILCTGESGAGKTENTKKVIQYLA-HVASSHKGGTLGRKKEAVQSMQYGELERQLLQANPILEAFGNAKTVKNDN 256
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvHCGTGNNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 257 SSRFGKFIRINF-DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLL-----CGASEETRADLLLGTADQYRFLSG 330
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLsadnnCVSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 331 G--SIPVPGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISF--MKEKNHDQASMPDNTAAQ--------- 397
Cdd:cd14899 241 SlcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqIPHKGDDTVFADEARVMSsttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 398 -KLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRR----------- 465
Cdd:cd14899 321 tKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 466 ---QRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIER 542
Cdd:cd14899 401 vddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 543 paNPPGVLALLDEECWFPRATDRSFVEKLSGE---QGSHPKFFKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLND 619
Cdd:cd14899 480 --RPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 620 NVASLLHQSSDHFVSELWKEvdrivGLDQVSSGESSAPVTFGAAGLKTKKGMFR-TVGQLYKESLTKLMATLRNTNPNFL 698
Cdd:cd14899 558 SAAQLLAGSSNPLIQALAAG-----SNDEDANGDSELDGFGGRTRRRAKSAIAAvSVGTQFKIQLNELLSTVRATTPRYV 632
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 699 RCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 750
Cdd:cd14899 633 RCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
109-793 |
1.17e-97 |
|
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: 332.77 E-value: 1.17e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYS--------GLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDRE 180
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 181 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTlgrkkeavqsmqYGELERQLLQANPILEAFGNAKTVKNDNSSRF 260
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGAD------------SQGLEARLLQSGPVLEAFGNAHTVLNANSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 261 GKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFlsggsipvpgqsD 340
Cdd:cd14887 149 GKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST------------D 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 341 SENFTQTMDSMAIMGFTPEELmsmLKVISAVLQFGNISFMKEKNHDQASMPDNTA--------AQKLCHLL--------- 403
Cdd:cd14887 217 LRRITAAMKTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssgl 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 404 ---------------------GVNVLEFTRAILTprIKVGREyVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRAL 462
Cdd:cd14887 294 kvteasrkhlktvarllglppGVEGEEMLRLALV--SRSVRE-TRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 463 DR-------------RQRQGASFIGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNF 526
Cdd:cd14887 371 QRsakpsesdsdedtPSTTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 527 I--DFGLDLQPCIDLIERPAN---------------------PPGVLALLDE------ECWFPRATDRSFVEKLSGEQGS 577
Cdd:cd14887 451 DcsAFPFSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIIN 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 578 HPKFFKSKQ--PRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLhQSSDHFVSElwkevdriVGLDQVSsgess 655
Cdd:cd14887 531 SAKYKNITPalSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRL--------VGSKKNS----- 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 656 apvtfgaaGLKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQ 735
Cdd:cd14887 597 --------GVRAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMAD 668
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774933 736 GFPNRIPFQEFRQRYEILTPNAIpRTFMDGKQASELMISALELDKNLFRVGQSKVFFR 793
Cdd:cd14887 669 GFPCRLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
110-757 |
8.59e-97 |
|
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: 325.31 E-value: 8.59e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNlpIYTESIVEMYRGKKRHeMPPHIYAISEAAYRSMLQdREDQSILCTGE 189
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 190 SGAGKTENTKKVIQYLAHvasshkgGTLGRKKeavqsmqygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 269
Cdd:cd14898 78 SGSGKTENAKLVIKYLVE-------RTASTTS----------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 270 vaGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLlgtadQYRFLSGGSIPVPgqSDSENFTQTMD 349
Cdd:cd14898 141 --GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI-----DTSSTAGNKESIV--QLSEKYKMTCS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 350 SMAIMGFTpeELMSMLKVISAVLQFGNISFMkekNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKA 429
Cdd:cd14898 212 AMKSLGIA--NFKSIEDCLLGILYLGSIQFV---NDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 430 QTKEQADFAVEALAKATYERLFRWLVHRINRALdrrQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 509
Cdd:cd14898 287 NTLKQARTIRNSMARLLYSNVFNYITASINNCL---EGSGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKM 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 510 FILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPRATDRSFVEKLsgeqgshpKFFKSKQPRG 589
Cdd:cd14898 364 FRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI--------KKYLNGFINT 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 590 EADFSII--HYAGKVDYKANDWLVKNMdplndnvasllhqssdhfvselwkevdrivgldqvssgESSAPVTFGAAGLKT 667
Cdd:cd14898 432 KARDKIKvsHYAGDVEYDLRDFLDKNR--------------------------------------EKGQLLIFKNLLIND 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 668 kKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 747
Cdd:cd14898 474 -EGSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFE 552
|
650
....*....|
gi 1988774933 748 QRYEILTPNA 757
Cdd:cd14898 553 ERYRILGITL 562
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
106-792 |
7.61e-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: 324.89 E-value: 7.61e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 106 LNEASVLHNLRERYYSGLIYTY---SGLfcVVVNPYKNLPIYTESIVEMYR-------GKKRHEMPPHIYAISEAAYRSM 175
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 176 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGGTlgrkkeavqsmqygELERQLLQANPILEAFGNAKTVKND 255
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGT--------------KLSSQISAAEFVLDSFGNAKTLTNP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 256 NSSRFGKFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFL-SGGSIP 334
Cdd:cd14879 145 NASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLaSYGCHP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 335 V---PGQSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFM--KEKNHDQASMpDNTAA-QKLCHLLGV--N 406
Cdd:cd14879 225 LplgPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTydHEGGEESAVV-KNTDVlDIVAAFLGVspE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 407 VLEftrAILTPRIK-VGRE----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINRALDRRQRQGASFIGILDIAGF 481
Cdd:cd14879 304 DLE---TSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 482 EifQL-----NSFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIERPanPPGVLA 551
Cdd:cd14879 377 Q--NRsstggNSLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGK--PGGLLG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 552 LLDEEC-WFPRATDRSFVEKLSGEQGSHPKF---FKSKQPRGEADFSIIHYAGKVDYKANDWLVKNMDPLndnvasllhq 627
Cdd:cd14879 447 ILDDQTrRMPKKTDEQMLEALRKRFGNHSSFiavGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVL---------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 628 SSDhFVSelwkevdrivgldqvssgessapvtfgaaglktkkgMFRTVGQLyKESLTKLMATLRNTNPNFLRCIIPNHEK 707
Cdd:cd14879 517 SPD-FVN------------------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQ 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 708 RAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPnaiprtFMDGKQASELMISALELDKNLFRVGQ 787
Cdd:cd14879 559 LPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGN 632
|
....*
gi 1988774933 788 SKVFF 792
Cdd:cd14879 633 TKVFL 637
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
109-793 |
2.54e-91 |
|
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: 311.56 E-value: 2.54e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLpiytESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHvasshkggtlGRKKEavqsmqyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14937 77 ESGSGKTEASKLVIKYYLS----------GVKED-------NEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQTM 348
Cdd:cd14937 140 DEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 349 DSMAIMGftpeelMSMLK-----VISAVLQFGNISFM---KEKNHDQASMPDNT--AAQKLCHLLGVNVLEFTRAILTPR 418
Cdd:cd14937 220 ISFDKMN------MHDMKddlflTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 419 IKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDrRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTN 498
Cdd:cd14937 294 KTIANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLN-NNKELNNYIGILDIFGFEIFSKNSLEQLLINIAN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 499 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPRATDRSFVEKLSGEQGSH 578
Cdd:cd14937 373 EEIHSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKH 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 579 PKFFKSKQPRGEaDFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVdrivgldQVSSgessapv 658
Cdd:cd14937 449 EKYASTKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDV-------EVSE------- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 659 TFGAAGLKTKKgmfrtvgqlYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRIcRQGFP 738
Cdd:cd14937 514 SLGRKNLITFK---------YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQ 583
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774933 739 NRIPFQEFRQRYEILTPNAIPRTFMDGKQASELMISAlELDKNLFRVGQSKVFFR 793
Cdd:cd14937 584 YKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
109-753 |
2.55e-91 |
|
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: 312.13 E-value: 2.55e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYR---GKKRHEMPPHIYAISEAAYRSMLQDREDQSIL 185
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 186 CTGESGAGKTENTKKVIQYLAHVASSHKGgtlgrkkeavqsmqygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 265
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT----------------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 266 INF-DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGG----SIPVPGQSD 340
Cdd:cd14878 145 LQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmredVSTAERSLN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 341 SENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIK 420
Cdd:cd14878 225 REKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 421 VGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAS---FIGILDIAGFEIFQLNSFEQLCINYT 497
Cdd:cd14878 305 FKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtlDIGILDIFGFEEFQKNEFEQLCVNMT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 498 NEKLQQLFNHTMFILEQEEYQREGIewnfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECWFPRATDRS 566
Cdd:cd14878 385 NEKMHHYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVEPN 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 567 FVEKLSG---EQGSHPKFFKSKQPRGE-------ADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSEL 636
Cdd:cd14878 452 LPKKLQSlleSSNTNAVYSPMKDGNGNvalkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 637 WKEvdrivgldqvssgessapvtfgaaglktkkgMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHL 716
Cdd:cd14878 532 FQS-------------------------------KLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFY 580
|
650 660 670
....*....|....*....|....*....|....*..
gi 1988774933 717 VLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEIL 753
Cdd:cd14878 581 VSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL 617
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
109-745 |
7.43e-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: 7.43e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYRGKKRHE-------MPPHIYAISEAAYRSMLQDRE 180
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 181 DQSILCTGESGAGKTENTKKVIQYLAHVASshkggtlgrkkeavqSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRF 260
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQT---------------DSQMTERIDKLIYINNILESMSNATTIKNNNSSRC 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 261 GKFIRINFD---------VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRAD-----------LLLG 320
Cdd:cd14884 146 GRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARrnlvrncgvygLLNP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 321 TADQYRFLSGGSIPVPG----------QSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFmkeknhdqasm 390
Cdd:cd14884 226 DESHQKRSVKGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAY----------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 391 pdntaaQKLCHLLGVNVLEFTRAILTPRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGA 470
Cdd:cd14884 295 ------KAAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 471 -----------SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDL 539
Cdd:cd14884 369 sdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 540 IERpanppgVLALLDE-----ECWFPRATDRSFVEKLSGE-----QGSHPKFFKS---------KQPRGEADFSIIHYAG 600
Cdd:cd14884 448 IAK------IFRRLDDitklkNQGQKKTDDHFFRYLLNNErqqqlEGKVSYGFVLnhdadgtakKQNIKKNIFFIRHYAG 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 601 KVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSElwkevdrivgldqvssgessapvtfgaAGLKTKKGMFRTVGQLYK 680
Cdd:cd14884 522 LVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE---------------------------ANNGGNKGNFLSVSKKYI 574
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774933 681 ESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 745
Cdd:cd14884 575 KELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
110-760 |
7.68e-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: 268.91 E-value: 7.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYknlpiytesiveMYRGKKRH-------EMPPHIYAISEAAYRSMLQDREDQ 182
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 183 SILCTGESGAGKTENTKKVIQYLAHVAsshkGGtlGRKKEAVqsmqygeleRQLLQANPILEAFGNAKTVKNDNSSRFGK 262
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVA----GG--GPETDAF---------KHLAAAFTVLRSLGSAKTATNSESSRIGH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 263 FIRINFdVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLG--TADQYRFLSGGSIPVPGQSD 340
Cdd:cd14881 135 FIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYLSHGDTRQNEAED 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 341 SENFTQTMDSMAIMGFtpeELMSMLKVISAVLQFGNISFMkEKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAiLTPRIK 420
Cdd:cd14881 214 AARFQAWKACLGILGI---PFLDVVRVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRG-LTTRTH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 421 -VGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALdrrqRQGAS--------FIGILDIAGFEIFQLNSFEQ 491
Cdd:cd14881 289 nARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSLK----RLGSTlgthatdgFIGILDMFGFEDPKPSQLEH 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 492 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPRATDRSFVEK 570
Cdd:cd14881 365 LCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 571 LSGEQGSHPKFFKSKQPRGEAdFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSdhfvselwkevdrivgldqvs 650
Cdd:cd14881 441 IKVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN--------------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 651 sgessapVTFGaaglktkkgmFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGI 730
Cdd:cd14881 499 -------CNFG----------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETV 561
|
650 660 670
....*....|....*....|....*....|
gi 1988774933 731 RICRQGFPNRIPFQEFRQRYEILTPNAIPR 760
Cdd:cd14881 562 NLMAGGYPHRMRFKAFNARYRLLAPFRLLR 591
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
110-793 |
3.04e-76 |
|
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: 268.50 E-value: 3.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLP-IYTESIVEMYrgKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVasshkggTLGRKKEavqsmqygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTT-------DLSRSKY---------LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 269 DVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLS-GGSIPVPGQSDSENFTQT 347
Cdd:cd14905 144 SLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNqGGSISVESIDDNRVFDRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 348 MDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKNhdQASMPDNTAAQKLCHLLGVNVLEFTRAILTPRIKVGREYVQ 427
Cdd:cd14905 224 KMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 428 KAqtkeqadfavEALAKATYERLFRWLVHRINRALdrRQRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 507
Cdd:cd14905 302 NR----------DSLARSLYSALFHWIIDFLNSKL--KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 508 TMFILEQEEYQREGIEW-NFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPRATDRSFVEKLSGEQGSHPKFfkSKQ 586
Cdd:cd14905 370 TVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLF--GKK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 587 PRgeaDFSIIHYAGKVDYKANDWLVKNMDPLNDNvASLLHQSS--DHFVSE--LWKEVDRIVGLDQVSSGESSA---PVT 659
Cdd:cd14905 441 PN---KFGIEHYFGQFYYDVRGFIIKNRDEILQR-TNVLHKNSitKYLFSRdgVFNINATVAELNQMFDAKNTAkksPLS 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 660 F-----------------------GAAGLKTKKGMFRTVGQLYKE-SLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPH 715
Cdd:cd14905 517 IvkvllscgsnnpnnvnnpnnnsgGGGGGGNSGGGSGSGGSTYTTySSTNKAINNSNCDFHFIRCIKPNSKKTHLTFDVK 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 716 LVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEILTPNAipRTFMDgkQASELMISALELDKNL---FRVGQSKVFF 792
Cdd:cd14905 597 SVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQN--LFEKLKENDINIDSILpppIQVGNTKIFL 672
|
.
gi 1988774933 793 R 793
Cdd:cd14905 673 R 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
109-793 |
1.03e-69 |
|
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: 247.86 E-value: 1.03e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 109 ASVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYrgkkrhemppHIYAISEAAYRSMLQDRED-QSILCT 187
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 188 GESGAGKTENTKKVIQYLAhvaSSHKGGTLGRKKEAVQSmqygelerqllqanpILEAFGNAKTVKNDNSSRFGKFIRIN 267
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPKSKVTTKHSSAIES---------------VFKSFGCAKTLKNDEATRFGCSIDLL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 268 FDvAGYIVGANIE-TYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDSENFTQ 346
Cdd:cd14874 133 YK-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 347 TMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKEKN----HDQASMPDNTAAQKLCHLLGVNVLEFTrAILTPRIKVG 422
Cdd:cd14874 212 LEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnveQDVVEIGNMSEVKWVAFLLEVDFDQLV-NFLLPKSEDG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 423 REYvqkaqTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQRQGAsfIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 502
Cdd:cd14874 291 TTI-----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 503 QLFNHTMFILEQEEYQREGIEWNF-IDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPRATDRSFVEKLSGEQGSHPKF 581
Cdd:cd14874 364 NLFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSY 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 582 FKSKQpRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELwkevdrivgldqVSSGESSApvtfg 661
Cdd:cd14874 442 GKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLL------------FESYSSNT----- 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 662 aaglktkKGMFRTVGQLYKESLTKLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRI 741
Cdd:cd14874 504 -------SDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKI 576
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774933 742 PFQEFRQRYEILTPNAIPRTfmdgKQASELMISALELD----KNLFRVGQSKVFFR 793
Cdd:cd14874 577 SKTTFARQYRCLLPGDIAMC----QNEKEIIQDILQGQgvkyENDFKIGTEYVFLR 628
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
112-792 |
7.26e-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: 242.57 E-value: 7.26e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 112 LHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKR----------HEMPPHIYAISEAAYRSMLQDRED 181
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 182 QSILCTGESGAGKTENTKKVIQYLAHVASshkgGTLGRKKEAVQSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFG 261
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGD----ETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 262 KFIRINFDVAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEET--RADLLLG-TADQYRFLSGGSIPVPGQ 338
Cdd:cd14893 160 KMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPtlRDSLEMNkCVNEFVMLKQADPLATNF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 339 S-DSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFM------KEKN-------HDQASMPDNTAAQKL--CHL 402
Cdd:cd14893 240 AlDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVpdpeggKSVGgansttvSDAQSCALKDPAQILlaAKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 403 LGVN--VLE---FTRAILTpriKVGREYVQ--KAQTKEQADFAVEALAKATYERLFRWLVHRINRAL----DRR------ 465
Cdd:cd14893 320 LEVEpvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYeksniv 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 466 -QRQGasfIGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQP 535
Cdd:cd14893 397 iNSQG---VHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 536 CIDLIERPanPPGVLALLDEECWFPRATDRSFVEKL-SGEQGSHpkffKSKQPRGEAD---------------FSIIHYA 599
Cdd:cd14893 474 CLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLfSGNEAVG----GLSRPNMGADttneylapskdwrllFIVQHHC 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 600 GKVDYKANDWLVKNMDPLNDNVASLLHQSSDhfvselwkEVDRIVGLDQVSSGESSAPVTfGAAGLKTKKGMFRTVGQLY 679
Cdd:cd14893 548 GKVTYNGKGLSSKNMLSISSTCAAIMQSSKN--------AVLHAVGAAQMAAASSEKAAK-QTEERGSTSSKFRKSASSA 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 680 KESLT--------------KLMATLRNTNPNFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 745
Cdd:cd14893 619 RESKNitdsaatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGH 698
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1988774933 746 FRQRYEILTPNaipRTFMDGKQASELMISALELDKnlFRVGQSKVFF 792
Cdd:cd14893 699 FFRRYKNVCGH---RGTLESLLRSLSAIGVLEEEK--FVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
110-753 |
9.44e-65 |
|
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: 233.86 E-value: 9.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGE 189
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 190 SGAGKTENTKKVIQYLAHVASSHKGGTlgrkkEAVQSmqygelerqllqANPILEAFGNAKTVKNDNSSRFGKFIRINFD 269
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRGAT-----GRVES------------SIKAILALVNAGTPLNADSTRCILQYQLTFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 270 VAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETR-ADLLLGTADQYRFLsggSIP--VPG--------- 337
Cdd:cd14882 145 STGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRlKEYNLKAGRNYRYL---RIPpeVPPsklkyrrdd 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 338 -QSDSENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMkeKNHDQASMPDNTAAQKLCHLLGVNVLEFTRAILT 416
Cdd:cd14882 222 pEGNVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFR--QNGGYAELENTEIASRVAELLRLDEKKFMWALTN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 417 PRIKVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALD-RRQRQGASF-IGILDIAGFEIFQLNSFEQLCI 494
Cdd:cd14882 300 YCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfPRAVFGDKYsISIHDMFGFECFHRNRLEQLMV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 495 NYTNEKLQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQPCIdlierpANPPGVLALLDEECWfPRATDRSFVEKL 571
Cdd:cd14882 380 NTLNEQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVDQLM------TKPDGLFYIIDDASR-SCQDQNYIMDRI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 572 SGEQGSHPKffkskqPRGEADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEvdrivglDQVSS 651
Cdd:cd14882 453 KEKHSQFVK------KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRN 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 652 gessapvtfgaagLKTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFLRCIIPNHEKRAGKLSPHLVLDQLRCNGVLE 728
Cdd:cd14882 520 -------------MRTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLD 580
|
650 660
....*....|....*....|....*
gi 1988774933 729 GIRICRQGFPNRIPFQEFRQRYEIL 753
Cdd:cd14882 581 TAKARQKGFSYRIPFQEFLRRYQFL 605
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
131-291 |
1.11e-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: 1.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 131 FCVVVNPYKNLPIYTESIV-EMYRGKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 209
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 210 SSHKGGTlGRKKEAVQSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRA 289
Cdd:cd01363 81 FNGINKG-ETEGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGFEIINESLNTLMNVLRA 159
|
..
gi 1988774933 290 TR 291
Cdd:cd01363 160 TR 161
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
110-791 |
1.92e-54 |
|
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: 204.68 E-value: 1.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 110 SVLHNLRERYYSGLIYTYSGLFCVVVNPYKNLPIYTESIVEMYR-GKKRHEMPPHIYAISEAAYRSMLQDREDQSILCTG 188
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 189 ESGAGKTENTKKVIQYLAHVASSHKGGTLG-------RKKEAVQSMQYGELERQLLQANPILEAFGNAKTVKNDNSSRFG 261
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNlndqeedNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 262 KFIRINFDvAGYIVGANIETYLLEKSRATRQAKDERTFHIFYQLLCGASEETRADLLLGTADQYRFLSGGSIPVPGQSDS 341
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 342 ENFTQTMDSMAIMGFTPEELMSMLKVISAVLQFGNISFMKE--------------------------KNHDQASMPDNTA 395
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAfrkksllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 396 AQKL-CHLLGVNVLEFTRAILTPRIkVGREYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINRALDRRQR--QGASF 472
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 473 IGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANppGVLAL 552
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 553 LDEECWFPRATDRSFVEKLSGEQGSH-PKFFKSKQPRG-EADFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSD 630
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSIIRKFSRnSKYIKKDDITGnKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 631 HFVSEL-----WKEVDRIVGLDQVSSGESSapvtfgaagLKTKKGMFRTVGQ----LYKESLTKLMATLRNTNPNFLRCI 701
Cdd:cd14938 558 EYMRQFcmfynYDNSGNIVEEKRRYSIQSA---------LKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCM 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 702 IPNHEKRA-GKLSPHLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEIltPNAiprtfmDGKQASELMISALELDK 780
Cdd:cd14938 629 KPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI--KNE------DLKEKVEALIKSYQISN 700
|
730
....*....|.
gi 1988774933 781 NLFRVGQSKVF 791
Cdd:cd14938 701 YEWMIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
991-1735 |
4.09e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 127.48 E-value: 4.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 991 LLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKreeq 1070
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ---- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1071 grlEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVE 1150
Cdd:TIGR02168 306 ---ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1151 NERGMRERAEKQRRDLSEELEALRTELEdtlDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSL 1230
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1231 QEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRsESERGRKRADNQLQELSARLAQADREREDREERMHKLQCE 1310
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ-ENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1311 IES-LSGNLSSSDSKSLRLAKE-ISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQI 1388
Cdd:TIGR02168 539 IEAaLGGRLQAVVVENLNAAKKaIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1389 QTHSQQL---------TELRKQSEEVNSAV-EAGDEIRRK--LQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTI 1456
Cdd:TIGR02168 619 SYLLGGVlvvddldnaLELAKKLRPGYRIVtLDGDLVRPGgvITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEK 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1457 ALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRL--- 1533
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEela 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1534 ----EMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEReISTNEEKG 1609
Cdd:TIGR02168 779 eaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE-LSEDIESL 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1610 EEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVT 1689
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1988774933 1690 RDDVISQ-SKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEI 1735
Cdd:TIGR02168 938 IDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1126-1946 |
8.41e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 126.32 E-value: 8.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1126 ARRAEAQRSLREA---LSQV----SELKEEVENERGMRERAEKQRrDLSEELEALRTELEdTLDSTAAQQELRsRREAEL 1198
Cdd:TIGR02168 172 ERRKETERKLERTrenLDRLedilNELERQLKSLERQAEKAERYK-ELKAELRELELALL-VLRLEELREELE-ELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1199 SELQRCVEEETRR---HETQLSELRVKHS---AALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSES 1272
Cdd:TIGR02168 249 KEAEEELEELTAElqeLEEKLEELRLEVSeleEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1273 ERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQ 1352
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1353 KMALASRVRALEEEKNGLmeRLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAiqrerq 1432
Cdd:TIGR02168 409 LERLEDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA------ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1433 keeekERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKF---DQCLAE--------EKAVSARLAEERDRAEADSR 1501
Cdd:TIGR02168 481 -----ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgiLGVLSElisvdegyEAAIEAALGGRLQAVVVENL 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1502 EKETRCLAlsrALQEAQDQK-----EELERANKQLRLEMEQLVNQQDDVGKN---VHELERARRTLETEAQNLRIQTQEL 1573
Cdd:TIGR02168 556 NAAKKAIA---FLKQNELGRvtflpLDSIKGTEIQGNDREILKNIEGFLGVAkdlVKFDPKLRKALSYLLGGVLVVDDLD 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1574 EEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEA 1653
Cdd:TIGR02168 633 NALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1654 QVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERD 1733
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1734 EIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNEL-------LTERLRKTALQVETLTVQLQGERTLAQKAE 1806
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAterrledLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1807 AA-------REQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQ 1879
Cdd:TIGR02168 873 SEleallneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT 952
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1880 AEDERRHADQYREQLDKSMVRLKQLKRQL-----------EEVEEENSRS---SAQKRKLQRELEELTDSSQTMNREISS 1945
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnlaaiEEYEELKERYdflTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
.
gi 1988774933 1946 L 1946
Cdd:TIGR02168 1033 R 1033
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
115-734 |
9.55e-27 |
|
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: 119.46 E-value: 9.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 115 LRERYYSGLIYTYSGLFCV-VVNPYKNL------PIYTESIVEMYRGKKRHE--MPPHIYAISE---------------- 169
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 170 ----AAYRSMLQDReDQSILCTGESGAGKTENTKKVIQYLAHVA---------------------------SSHKGGTLG 218
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetckvsgstrqpkiklftSSTKSTIQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 219 RKKEA--------------------------------------------------VQSMQYGELERQL------------ 236
Cdd:cd14894 166 RTEEArtialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfYEKLEHLEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 237 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVAGY---IVGANIETYLLEKSRATRQA------KDERTFHI 301
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 302 FYQLLCGASEETRADLL----------------LGTADqYRFLSGGSIPVPGQSDSENFTQTMDSMAIMGFTPEELMSML 365
Cdd:cd14894 326 LYAMVAGVNAFPFMRLLakelhldgidcsaltyLGRSD-HKLAGFVSKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 366 KVISAVLQFGNISFMKEKNHDQASMPDN---TAAQKLCHLLGVNVLE-FTRAILTPRIKV--GREYVQKAQTKEQADFAV 439
Cdd:cd14894 405 KVLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEkLERMLMTKSVSLqsTSETFEVTLEKGQVNHVR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 440 EALAKATYERLFRWLVHRINRAL-------DRRQRQ---------GASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQq 503
Cdd:cd14894 485 DTLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY- 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 504 lfnhtmfileQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPRATD--------------RSFVE 569
Cdd:cd14894 564 ----------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENmnaqqeekrnklfvRNIYD 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 570 KLSGEQGSHPKFFKSKQPRGEA-----DFSIIHYAGKVDYKANDWLVKNMDPLNDNVASLLHQSSDHFVSELWKEVDRI- 643
Cdd:cd14894 634 RNSSRLPEPPRVLSNAKRHTPVllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQLg 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 644 ----VGLDQVSSGESSapvtfgAAGLKTKKGMFRTVGQLYKESLTKLMatlrntnPNFLRCIIPNHEKRAGKLSPHLVLD 719
Cdd:cd14894 714 wspnTNRSMLGSAESR------LSGTKSFVGQFRSHVNVLTSQDDKNM-------PFYFHCIRPNAKKQPSLVNNDLVEQ 780
|
810
....*....|....*
gi 1988774933 720 QLRCNGVLEGIRICR 734
Cdd:cd14894 781 QCRSQRLIRQMEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1126-1719 |
1.47e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 115.80 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1126 ARRAEAQRSLREA---LSQVSELKEEVENERG----MRERAEK------------------QRRDLSEELEALRTELEDT 1180
Cdd:COG1196 172 ERKEEAERKLEATeenLERLEDILGELERQLEplerQAEKAERyrelkeelkeleaellllKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1181 LDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRvKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTS 1260
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEY-ELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1261 ELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLH 1340
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1341 DARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQ 1420
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1421 RELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRErqnctaLEKRQKKFDQCLAEEKAVSARLAEERDRAEADS 1500
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG------VEAAYEAALEAALAAALQNIVVEDDEVAAAAIE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1501 REKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDvgknVHELERARRTLETEAQNLRIQTQELEEELSEA 1580
Cdd:COG1196 565 YLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDL----READARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1581 ENSRLRLEVTLQAlkAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANR 1660
Cdd:COG1196 641 TLAGRLREVTLEG--EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774933 1661 GKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELA 1719
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
851-1682 |
2.49e-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: 115.15 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 851 LRNWQWWRLftkvkpLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEE 930
Cdd:TIGR02168 222 LRELELALL------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 931 MRARLASRKQeleevlgeletrleeeeergvQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLA 1010
Cdd:TIGR02168 296 EISRLEQQKQ---------------------ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1011 TAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQgrlEQEKFKRRMESEAMEAQ 1090
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED---RRERLQQEIEELLKKLE 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1091 E-QLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEE 1169
Cdd:TIGR02168 432 EaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1170 LE----------------------------ALRTELEDTLDSTAAQQ------------------ELRSRREAELSELQR 1203
Cdd:TIGR02168 512 LKnqsglsgilgvlselisvdegyeaaieaALGGRLQAVVVENLNAAkkaiaflkqnelgrvtflPLDSIKGTEIQGNDR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1204 CVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRA---RQSLEKAKATLEEERqnLTSELKSLQASRSESERGRKRAD 1280
Cdd:TIGR02168 592 EILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVddlDNALELAKKLRPGYR--IVTLDGDLVRPGGVITGGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1281 NQLQELSARLAQADREREDREERMHKLQCEIEslsgnlsssdskslRLAKEISSLESQLHDARELLQDESRQKMALASRV 1360
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALA--------------ELRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1361 RALEEEKNGLmerleeeEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERV 1440
Cdd:TIGR02168 736 ARLEAEVEQL-------EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1441 ERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREketrclaLSRALQEAQDQ 1520
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-------LESELEALLNE 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1521 KEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQeleeelseaensrlRLEVTLQALKAQF-- 1598
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE--------------GLEVRIDNLQERLse 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1599 -----EREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQ 1673
Cdd:TIGR02168 948 eysltLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
....*....
gi 1988774933 1674 GQMKEVLRE 1682
Cdd:TIGR02168 1028 REARERFKD 1036
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
989-1567 |
1.17e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 109.64 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 989 QRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKRE 1068
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1069 EQGRleqekfkrrmeseameaqeqlsdlgmlsSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEE 1148
Cdd:COG1196 308 EERR----------------------------RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1149 VENERGMRERAEKQRRDLSEELEALRTELedtLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSEL--RVKHSAA 1226
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEEL---LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEeaLAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1227 LDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHK 1306
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1307 LQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQ----KMALASRVRALEEEKnglmeRLEEEEERGK 1382
Cdd:COG1196 517 AGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAieylKAAKAGRATFLPLDK-----IRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1383 ELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEdmtIALQRER 1462
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS---LTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1463 QNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQ 1542
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580
....*....|....*....|....*
gi 1988774933 1543 DDVGKNVHELERARRTLETEAQNLR 1567
Cdd:COG1196 749 EEEALEELPEPPDLEELERELERLE 773
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
997-1753 |
8.61e-21 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 100.14 E-value: 8.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 997 TLETKVKSLETDLATAVEQRERLGKEKKQLEErlnevTDQLTEEEEKTKSLNKLKNKQEAViADLEERLKREEQGRLEQE 1076
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRREREKAER-----YQALLKEKREYEGYELLKEKEALE-RQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1077 KFKRRMESEAMEAQEQLSDLGMLSSELRgslAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENergmr 1156
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIK---DLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK----- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1157 erAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEEtrrhETQLSELRVKHSA---ALDSLQEQ 1233
Cdd:TIGR02169 327 --LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV----DKEFAETRDELKDyreKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1234 LDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIES 1313
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1314 LSGNLSSsdskslrLAKEISSLESQLHDARELLQDESRQKMALASRVR------------------ALEEEKNGLMERLE 1375
Cdd:TIGR02169 481 VEKELSK-------LQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryatAIEVAAGNRLNNVV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1376 EEEERGKELSRQIQTHSQ-------QLTELRKQSEEVNSAVEAG------------DEIRRKLQRELDSAIQRERQKEEE 1436
Cdd:TIGR02169 554 VEDDAVAKEAIELLKRRKagratflPLNKMRDERRDLSILSEDGvigfavdlvefdPKYEPAFKYVFGDTLVVEDIEAAR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1437 KERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFdqcLAEEKAVSARLAE---ERDRAEADSREKETRCLALSRA 1513
Cdd:TIGR02169 634 RLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSE---PAELQRLRERLEGlkrELSSLQSELRRIENRLDELSQE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1514 LQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRiqtQELEEELSEAENSRLRLEVTLQA 1593
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE---ARIEELEEDLHKLEEALNDLEAR 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1594 LKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQ-------VETANRGKEEAM 1666
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQiksiekeIENLNGKKEELE 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1667 KQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVS-SSSG 1745
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdEEIP 947
|
....*...
gi 1988774933 1746 KNVLSEEK 1753
Cdd:TIGR02169 948 EEELSLED 955
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
868-1406 |
4.93e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.70 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 868 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLG 947
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 948 ELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLE 1027
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1028 ERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSL 1107
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1108 AQKEKEITSLQGRLEEEGARR-AEAQRSLREALSQVSELKEEVENERGMRERAEKQR--RDLSEELEALRTELEDTLDST 1184
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALlLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNivVEDDEVAAAAIEYLKAAKAGR 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1185 AAQQEL---RSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQnLTSE 1261
Cdd:COG1196 574 ATFLPLdkiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE-VTLE 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1262 LKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIEslsgnlsssdskslRLAKEISSLESQLHD 1341
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE--------------EEERELAEAEEERLE 718
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774933 1342 ARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVN 1406
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVN 783
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
875-1426 |
6.98e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.31 E-value: 6.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 875 EIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGELETRLE 954
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 955 EEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVT 1034
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1035 DQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEI 1114
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1115 TSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGM-----RERAEKQRRDLSEELEALRT--ELEDTLDSTAAQ 1187
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFlegvkAALLLAGLRGLAGAVAVLIGveAAYEAALEAALA 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1188 QELRSRREAELSELQRCVEEETRRHETQLSELrvkhsAALDSLQEQLDNSKRARQSLEKAKATLEEERQnltsELKSLQA 1267
Cdd:COG1196 546 AALQNIVVEDDEVAAAAIEYLKAAKAGRATFL-----PLDKIRARAALAAALARGAIGAAVDLVASDLR----EADARYY 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1268 SRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQ 1347
Cdd:COG1196 617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE 696
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774933 1348 DesrQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSA 1426
Cdd:COG1196 697 E---ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
966-1820 |
1.27e-19 |
|
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: 96.58 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 966 EKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTK 1045
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1046 SLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLgmlsselrgslaqkEKEITSLQGRLEEEG 1125
Cdd:pfam02463 255 SSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL--------------ERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1126 ARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCV 1205
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1206 EEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQE 1285
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1286 LSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDAREL-LQDESRQKMALASRVRALE 1364
Cdd:pfam02463 481 KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENyKVAISTAVIVEVSATADEV 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1365 EEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQR 1444
Cdd:pfam02463 561 EERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKES 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1445 ERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEEL 1524
Cdd:pfam02463 641 AKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1525 ERANKQLRLEM----EQLVNQQDDVGKNVHELERARRTLETEaQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFER 1600
Cdd:pfam02463 721 ELLADRVQEAQdkinEELKLLKQKIDEEEEEEEKSRLKKEEK-EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1601 EISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVL 1680
Cdd:pfam02463 800 EEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEEL 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1681 RELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVL-SEEKRRLDAR 1759
Cdd:pfam02463 880 EEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKeKEENNKEEEE 959
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774933 1760 VNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELK 1820
Cdd:pfam02463 960 ERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
994-1554 |
5.13e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 94.34 E-value: 5.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 994 EKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLknkqEAVIADLEERLKREEQgrl 1073
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETL----EAEIEDLRETIAETER--- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1074 EQEKFKRRMEseamEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENER 1153
Cdd:PRK02224 273 EREELAEEVR----DLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1154 GMRERAEKQRRDLSEELEALRTELEDTldstaaqQELRSRREAELSELqrcvEEETRRHETQLSELRVKHSAALDSLQEQ 1233
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEA-------REAVEDRREEIEEL----EEEIEELRERFGDAPVDLGNAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1234 LDNSKRARQSLEKAKATLEEERQNLTSELKSLQASR----------SESERGRKRADNQLQELSARLAQADREREDREER 1303
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1304 MHKLQcEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKE 1383
Cdd:PRK02224 498 LERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1384 LSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQ 1463
Cdd:PRK02224 577 LNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKE 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1464 NC-TALEKRQKKFDQCLAEEKAVSARL-AEERDRAEADS-REKETRCLALSRALQEAQDQKEELERANKQLRLEMEQlvn 1540
Cdd:PRK02224 657 RAeEYLEQVEEKLDELREERDDLQAEIgAVENELEELEElRERREALENRVEALEALYDEAEELESMYGDLRAELRQ--- 733
|
570
....*....|....
gi 1988774933 1541 qqddvgKNVHELER 1554
Cdd:PRK02224 734 ------RNVETLER 741
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1328-1943 |
6.08e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.23 E-value: 6.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1328 LAKEISSLESQ---LHDARELLQD-ESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSE 1403
Cdd:COG1196 198 LERQLEPLERQaekAERYRELKEElKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1404 EVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEK 1483
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1484 AVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEA 1563
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1564 QNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREistnEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQ 1643
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL----EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1644 LEAELQEAEAQVETANRGKEEAMKQLR--RLQGQMKEVLRELDDskvTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVS 1721
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALeaALAAALQNIVVEDDE---VAAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1722 ERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTL 1801
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1802 AQKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKE--VMMQ 1879
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEeeLLEE 750
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774933 1880 AEDERRHADQYREQLDKsmvRLKQLKRQL--------------EEVEEENSRSSAQKRKLQRELEELTDSSQTMNREI 1943
Cdd:COG1196 751 EALEELPEPPDLEELER---ELERLEREIealgpvnllaieeyEELEERYDFLSEQREDLEEARETLEEAIEEIDRET 825
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1245-1848 |
3.02e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.92 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1245 EKAKATLEEERQNLT----------SELKSL--QASRSE-----SERGRKRadnQLQELSARLAQADREREDREERMHKL 1307
Cdd:COG1196 175 EEAERKLEATEENLErledilgeleRQLEPLerQAEKAEryrelKEELKEL---EAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1308 QCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQ 1387
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1388 IQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERqrerlreeiedmtiALQRERQNCTA 1467
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE--------------ELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1468 LEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGK 1547
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1548 nvhELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRRALSkQVRELEIQL 1627
Cdd:COG1196 478 ---ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL-AAALQNIVV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1628 EEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQG---------QMKEVLRELDDSKVTRDDVISQSK 1698
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAvdlvasdlrEADARYYVLGDTLLGRTLVAARLE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1699 DSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEmvssssgknVLSEEKRRLDARVNQLEEELEEEQTNNELLT 1778
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA---------LLEAEAELEELAERLAEEELELEEALLAEEE 704
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774933 1779 ERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARL-----GEMEGAVRGKHRMSVAALEAKIETM 1848
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEeealeELPEPPDLEELERELERLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1207-1951 |
3.86e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 91.66 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1207 EETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQ------SLEKAKATLEEERQNltSELKSLQASRSESERGRKRAD 1280
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAERYKElkaelrELELALLVLRLEELR--EELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1281 NQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRV 1360
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1361 RALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAV----EAGDEIRRKLQR---ELDSAIQRERQK 1433
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqleLQIASLNNEIERleaRLERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1434 EEEKERVERQRERLREEIEDMTIALQRErqnctALEKRQKKFDQCLAEEKAVSARLAEERdRAEADSREKETRCLALSRA 1513
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEELEE-----ELEELQEELERLEEALEELREELEEAE-QALDAAERELAQLQARLDS 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1514 LQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLET----EAQNLRIQTQELEEELSEAENSRLRLEV 1589
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAalggRLQAVVVENLNAAKKAIAFLKQNELGRV 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1590 TLQALKAQFEREISTNEekgeekrralskqvRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGkEEAMKQL 1669
Cdd:TIGR02168 574 TFLPLDSIKGTEIQGND--------------REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDL-DNALELA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1670 RRLQGQMKEVlrELDDSKVTRDDVIS-QSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNV 1748
Cdd:TIGR02168 639 KKLRPGYRIV--TLDGDLVRPGGVITgGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1749 LSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEG 1828
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1829 AVrGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQL 1908
Cdd:TIGR02168 797 EL-KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1988774933 1909 EEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLS 1951
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1393-1950 |
1.16e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.00 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1393 QQLTELRKQSEEVNSAVEAGDEIR-----------RKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRE 1461
Cdd:COG1196 200 RQLEPLERQAEKAERYRELKEELKeleaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1462 RQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQ 1541
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1542 QDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFER------EISTNEEKGEEKRRA 1615
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERleeeleELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1616 LSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETAnRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVIS 1695
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL-LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1696 QSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDA----RVNQLEEELEEEQ 1771
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKirarAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1772 TNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAV------RGKHRMSVAALEAKI 1845
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSaggsltGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1846 ETMEEQLEQerqeraiANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKL 1925
Cdd:COG1196 679 AELEELAER-------LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570 580
....*....|....*....|....*
gi 1988774933 1926 QRELEELTDSSQTMNREISSLRNQL 1950
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1040-1943 |
3.58e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.59 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1040 EEEKTKSLNKLK------NKQEAVIADLEERLKREEQGRLEQEKFK----RRMESEAMEAQEQLSDLGMLSSELRGSLAQ 1109
Cdd:TIGR02169 169 DRKKEKALEELEeveeniERLDLIIDEKRQQLERLRREREKAERYQallkEKREYEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1110 KEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENE-RGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQ 1188
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1189 ELRSRREAELSELQRCVEEETRRhetqlselRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQAS 1268
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKR--------RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1269 RSESERGRKRADNQLQELSARLAQadreredreermhkLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQD 1348
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELAD--------------LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1349 ESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAiq 1428
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVA-- 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1429 rerqkeeekerverqrerlreeiedmtiALQRERQNCTALEKRQKKFDQCLAEEKAVSAR---LAEERDRAEADSREKET 1505
Cdd:TIGR02169 545 ----------------------------AGNRLNNVVVEDDAVAKEAIELLKRRKAGRATflpLNKMRDERRDLSILSED 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1506 RCLALSRALQEAQDQKEELERANKQLRLEMEqlvnqqddvgknvhELERARRTLeteaqnlriqtqeleeelseaenSRL 1585
Cdd:TIGR02169 597 GVIGFAVDLVEFDPKYEPAFKYVFGDTLVVE--------------DIEAARRLM-----------------------GKY 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1586 RLeVTLQAL----------KAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQV 1655
Cdd:TIGR02169 640 RM-VTLEGElfeksgamtgGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI 718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1656 ETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSER-----QKRQAQQ 1730
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsRIPEIQA 798
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1731 ERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAARE 1810
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1811 QLEKQNKELKARLGEMEGAVRgKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEvMMQAEDERRHADQY 1890
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLR-ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE-DEEIPEEELSLEDV 956
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774933 1891 REQLDKSMVRLKQLK-------RQLEEVEEENSRSSAQKRKLQRELEEL---TDSSQTMNREI 1943
Cdd:TIGR02169 957 QAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAIlerIEEYEKKKREV 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1061-1732 |
4.64e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 88.27 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1061 LEERLKREEQGRLEQEkfkrrmeSEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREalS 1140
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEA-------RKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEE--A 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1141 QVSELKEEVENERGMRE--RAEKQRR--DLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHE--- 1213
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAEEvrKAEELRKaeDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEeer 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1214 -----TQLSELRVKHSAALDSLQ--------------EQLDNSKRARQSLEKAKAtleEERQNLTSELKSLQASRSESER 1274
Cdd:PTZ00121 1250 nneeiRKFEEARMAHFARRQAAIkaeearkadelkkaEEKKKADEAKKAEEKKKA---DEAKKKAEEAKKADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1275 GRKRAD------------NQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEI-SSLESQLHD 1341
Cdd:PTZ00121 1327 AKKKADaakkkaeeakkaAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkKKAEEDKKK 1406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1342 ARELLQDESRQKMALASRVRAlEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEA---------G 1412
Cdd:PTZ00121 1407 ADELKKAAAAKKKADEAKKKA-EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAkkkaeeakkA 1485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1413 DEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQClaeEKAVSARLAEE 1492
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL---KKAEELKKAEE 1562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1493 RDRAEADSREKETRCLALSRAlQEAqdQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQE 1572
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKA-EEA--KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1573 LEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAE 1652
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1653 aQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQER 1732
Cdd:PTZ00121 1720 -ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1129-1946 |
2.05e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.81 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1129 AEAQRSLREALSQVSELKEEVENERGMRERAEKQR-------RDLSEELEALRTELEDTLDSTAAQQELRSRREAELSEL 1201
Cdd:TIGR02169 152 PVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIerldliiDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1202 QRCVEEETRRHETQLSELRvKHSAALDSLQEQL-DNSKRARQSLE----KAKATLEEERQNLTSELKSLQASRSESERGR 1276
Cdd:TIGR02169 232 KEALERQKEAIERQLASLE-EELEKLTEEISELeKRLEEIEQLLEelnkKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1277 KRADNQLQELSARLAQADREredreerMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDES----RQ 1352
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAE-------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDkefaET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1353 KMALASRVRALE---EEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQR 1429
Cdd:TIGR02169 384 RDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1430 ERQKEEEkerverqrerlreeiedmtiaLQRERQNCTALEKRQKKFDQCLAEEKAvSARLAEERDRAEADSREketrclA 1509
Cdd:TIGR02169 464 LSKYEQE---------------------LYDLKEEYDRVEKELSKLQRELAEAEA-QARASEERVRGGRAVEE------V 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1510 LSRALQEAQDQKEELERANKQLRLEME--------QLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAE 1581
Cdd:TIGR02169 516 LKASIQGVHGTVAQLGSVGERYATAIEvaagnrlnNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSE 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1582 NSRLRLEVTLQALKAQFEREI-----STNEEKGEEKRRALSKQVR--ELEIQLEEE-------RSQRSQSVSSKKQLEAE 1647
Cdd:TIGR02169 596 DGVIGFAVDLVEFDPKYEPAFkyvfgDTLVVEDIEAARRLMGKYRmvTLEGELFEKsgamtggSRAPRGGILFSRSEPAE 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1648 LQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKvtrddviSQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQ 1727
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS-------RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1728 AQQERDEIADEMVSSSSGKNVLSEEKRRLDARV-----NQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLA 1802
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1803 QKAEAAREQLEKQNKELKARLGEMEGAvrgkhrmsVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAED 1882
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKE--------IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1883 ERRHADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKLQRE------LEELTDSSQTMNREISSL 1946
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRAL 970
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1119-1726 |
7.17e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.85 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1119 GRLEEEGARRAEAQRSLREALSQVSELKEEVENERgmrerAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAEL 1198
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQI-----EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETR 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1199 SELQRCVEEetrrHETQLSELRVKhSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKR 1278
Cdd:PRK02224 237 DEADEVLEE----HEERREELETL-EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1279 ADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALAS 1358
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1359 RVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGdeirrklQRELDSAIQRERQKEEEKE 1438
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA-------EALLEAGKCPECGQPVEGS 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1439 RVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSaRLAEERDRAEADSREKETRCLALSRALQEAQ 1518
Cdd:PRK02224 465 PHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE-RLEERREDLEELIAERRETIEEKRERAEELR 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1519 DQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRiqtqeleeelseaensRLRlevTLQALKAQF 1598
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE----------------RIR---TLLAAIADA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1599 EREIstneEKGEEKRRALSKQVRELEIQLEEersqrsqSVSSKKQLEAELQeaEAQVETANRGKEEAMKQLRRLQGQmke 1678
Cdd:PRK02224 605 EDEI----ERLREKREALAELNDERRERLAE-------KRERKRELEAEFD--EARIEEAREDKERAEEYLEQVEEK--- 668
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1988774933 1679 vLRELDDSkvtRDDVISQSKDSEKKIQTLEAevlhLTEEL-AVSERQKR 1726
Cdd:PRK02224 669 -LDELREE---RDDLQAEIGAVENELEELEE----LRERReALENRVEA 709
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
866-1293 |
2.67e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 866 LLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEV 945
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 946 LGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQ 1025
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1026 LEERLNEV--TDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRL--EQEKFKRRMESEAMEAQEQLSDLGMLSS 1101
Cdd:COG1196 503 YEGFLEGVkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVveDDEVAAAAIEYLKAAKAGRATFLPLDKI 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1102 ELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSE--LKEEVENERGMRERAEKQRRDLSEELEALRTELED 1179
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRtlVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1180 TLDSTAAQQELRSRREAELSELqrcvEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLT 1259
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEEL----AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
410 420 430
....*....|....*....|....*....|....
gi 1988774933 1260 SELKSLQASRSESERGRKRADNQLQELSARLAQA 1293
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
867-1314 |
3.53e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 867 LQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVL 946
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 947 GELETRLEeeeergvQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQL 1026
Cdd:COG1196 403 EELEEAEE-------ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1027 EERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGS 1106
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1107 LAQKEKEITSLQ----GRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRD----LSEELEALRTELE 1178
Cdd:COG1196 556 DEVAAAAIEYLKaakaGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLgdtlLGRTLVAARLEAA 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1179 DTLDSTAAQQELRSRREAE-LSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQN 1257
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEgGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774933 1258 LTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESL 1314
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
962-1265 |
5.01e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.19 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 962 QLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEE 1041
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1042 EKTKSLNKLKNKQEAVIADLEERLKREEQgRLEQEKFKrrmeseamEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRL 1121
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEA-RLSHSRIP--------EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1122 EEEGARRAEAQRSLREALSQVSELKEEVENERGmreraekQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSEL 1201
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG-------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774933 1202 QRCVEE---ETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKA--TLEEERQNLTSELKSL 1265
Cdd:TIGR02169 902 ERKIEEleaQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRAL 970
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
986-1567 |
6.35e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.41 E-value: 6.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 986 SARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEaviaDLEERL 1065
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1066 KREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRgSLAQKEKEITSLQGrLEEEGARRAEAQRSLREALSQVSEL 1145
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-ELEEKVKELKELKE-KAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1146 KEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQElrsrrEAELSELQRCVEEETRRHETQLSELrvkhsa 1225
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-----RHELYEEAKAKKEELERLKKRLTGL------ 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1226 aldslqeQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSEsergRKRADNQLQELSAR--LAQADREREDREER 1303
Cdd:PRK03918 385 -------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE----LKKAIEELKKAKGKcpVCGRELTEEHRKEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1304 MHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESrqkmaLASRVRALEEEKNGLMERLEEEEERGKE 1383
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE-----LAEQLKELEEKLKKYNLEELEKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1384 LSRQ-----------IQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELD----SAIQRERQKEEEKERVERQRERLR 1448
Cdd:PRK03918 529 KLKEkliklkgeiksLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfESVEELEERLKELEPFYNEYLELK 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1449 EEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAE-ERDRAEADSREKETRCLALSRALQEAQDQKEELERA 1527
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElEKKYSEEEYEELREEYLELSRELAGLRAELEELEKR 688
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1988774933 1528 NKQLRLEMEQLVNQQDDVGKNVHELERARRTLEtEAQNLR 1567
Cdd:PRK03918 689 REEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELR 727
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
864-1711 |
2.89e-13 |
|
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: 75.78 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 864 KPLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLAdQLQAEAELFAEAEEMRARLASRKQELE 943
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL-YLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 944 EVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEK 1023
Cdd:pfam02463 255 SSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1024 KQLEERLNE---VTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLS 1100
Cdd:pfam02463 335 EEIEELEKElkeLEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELA 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1101 SELRGSLAQKEKEITSLQGRLEEEGaRRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDT 1180
Cdd:pfam02463 415 RQLEDLLKEEKKEELEILEEEEESI-ELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1181 LDSTAAQQELRSRREAELSELQRCVEEETR----RHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQ 1256
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLALIKDGVGGRiisaHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1257 NLT----------SELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSL 1326
Cdd:pfam02463 574 PLGarklrllipkLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVS 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1327 RLAKEissLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTEL---RKQSE 1403
Cdd:pfam02463 654 LEEGL---AEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELladRVQEA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1404 EVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEK 1483
Cdd:pfam02463 731 QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1484 AVSARLAEERDRAEADSrEKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQddvgknvhELERARRTLETEA 1563
Cdd:pfam02463 811 KEEAELLEEEQLLIEQE-EKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL--------LQELLLKEEELEE 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1564 QNLRIQTQELEEELSEAENSRLRLEVTLQALkaqfEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQ 1643
Cdd:pfam02463 882 QKLKDELESKEEKEKEEKKELEEESQKLNLL----EEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEE 957
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1644 LEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVI--SQSKDSEKKIQTLEAEV 1711
Cdd:pfam02463 958 EEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIraIIEETCQRLKEFLELFV 1027
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
998-1545 |
4.96e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 74.77 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 998 LETKVKSLETDLATAVEQRE-RLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEER-----LKREEQG 1071
Cdd:pfam15921 322 LESTVSQLRSELREAKRMYEdKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRekelsLEKEQNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1072 RLEQ---------EKFKRRMESEAMEAQEQLSDLGMLSSELRGslaQKEKEITSLQGRLEE-EGARRAEAQ-RSLREALS 1140
Cdd:pfam15921 402 RLWDrdtgnsitiDHLRRELDDRNMEVQRLEALLKAMKSECQG---QMERQMAAIQGKNESlEKVSSLTAQlESTKEMLR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1141 QVSElkeEVENERGMRERAEKQRRDLSEELEalrtELEDTLDSTAAQ-QELRSRREAELSELQRCVEEET--RRHETQLS 1217
Cdd:pfam15921 479 KVVE---ELTAKKMTLESSERTVSDLTASLQ----EKERAIEATNAEiTKLRSRVDLKLQELQHLKNEGDhlRNVQTECE 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1218 ELRVKHSA---ALDSLQEQLDNSK-------RARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELS 1287
Cdd:pfam15921 552 ALKLQMAEkdkVIEILRQQIENMTqlvgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1288 ARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQ-KMALASRVRALEEE 1366
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQT 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1367 KNGLMERLEE---EEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGD-------EIRRKLQRELDSAIQRERQKEEE 1436
Cdd:pfam15921 712 RNTLKSMEGSdghAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANkekhflkEEKNKLSQELSTVATEKNKMAGE 791
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1437 KERVERQRERLREEIEDMTIAL--------------QRERQNCTALeKRQKKFD------QCLAEEKAVSARLAEERDRA 1496
Cdd:pfam15921 792 LEVLRSQERRLKEKVANMEVALdkaslqfaecqdiiQRQEQESVRL-KLQHTLDvkelqgPGYTSNSSMKPRLLQPASFT 870
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1988774933 1497 EADSREKETRCLA--LSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDV 1545
Cdd:pfam15921 871 RTHSNVPSSQSTAsfLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTV 921
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1080-1270 |
4.15e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.87 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1080 RRMESEAMEAQEQLSDLGMLSsELRGSLAQKEKEITSLqgRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERA 1159
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIR-ELAERYAAARERLAEL--EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1160 EKQRRDLSEELEALR-----------TELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALD 1228
Cdd:COG4913 315 EARLDALREELDELEaqirgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1988774933 1229 SLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRS 1270
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1469-1947 |
6.16e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.33 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1469 EKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANkQLRLEMEQLVNQQDDVGKN 1548
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKKK 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1549 VHELERARRTLETEAqnlriqtqeleeelseaensrlrlEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLE 1628
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEA------------------------EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA 1393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1629 EERSQRSQSVSSKKQleaELQEAEAQVETANRGKEEAMKQLRRLQGQMK-EVLRELDDSKVTRDDVISQSKDSEKKIQTL 1707
Cdd:PTZ00121 1394 DEAKKKAEEDKKKAD---ELKKAAAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1708 EAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQ 1787
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1788 VETLTVQLQGERTlaQKAEAAREQLEKQNKELkaRLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMR 1867
Cdd:PTZ00121 1551 LKKAEELKKAEEK--KKAEEAKKAEEDKNMAL--RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1868 KTE---KKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVE---EENSRSSAQKRK----LQRELEELTDSSQ 1937
Cdd:PTZ00121 1627 KAEeekKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKkkaEEAKKAEEDEKKaaeaLKKEAEEAKKAEE 1706
|
490
....*....|
gi 1988774933 1938 TMNREISSLR 1947
Cdd:PTZ00121 1707 LKKKEAEEKK 1716
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
928-1735 |
9.30e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 9.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 928 AEEMRARLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQ--DLEEQLEEEESARQRLLLEKVTLETKVKSL 1005
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkaEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1006 ETDLATAVEQRERLGK--EKKQLEERlnEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRME 1083
Cdd:PTZ00121 1276 EARKADELKKAEEKKKadEAKKAEEK--KKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1084 SEAMEAQEqlsdlgmlsselrgslAQKEKEITSLQgrlEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQR 1163
Cdd:PTZ00121 1354 AAADEAEA----------------AEEKAEAAEKK---KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1164 RDlSEELEALRTELEDTLDSTAAQQELRSRREAElsELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQS 1243
Cdd:PTZ00121 1415 AA-KKKADEAKKKAEEKKKADEAKKKAEEAKKAD--EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1244 LEKAKATLEEERQNLTSELKSLQASRSESergRKRADNQLQELSARLAQADREREDREErmhklqceieslsgnlsssdS 1323
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEE---AKKADEAKKAEEAKKADEAKKAEEKKK--------------------A 1548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1324 KSLRLAKEISSLEsQLHDARELLQDESRQKMAL--ASRVRALEEEK-NGLMERLEEEEERGKELSRQIQTHSQQLTELRK 1400
Cdd:PTZ00121 1549 DELKKAEELKKAE-EKKKAEEAKKAEEDKNMALrkAEEAKKAEEARiEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1401 QsEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQclA 1480
Cdd:PTZ00121 1628 A-EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK--A 1704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1481 EEkaVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKqlrlemeqlvnqqDDVGKNvhELERARRTLE 1560
Cdd:PTZ00121 1705 EE--LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK-------------DEEEKK--KIAHLKKEEE 1767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1561 TEAQNLRIQTQELEEELSEAENSRLRLEV--TLQALKAQFEreistNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSV 1638
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVdkKIKDIFDNFA-----NIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQ 1842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1639 SSKKQlEAELQEAEAQVETANRGKEEA--MKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAevlhLTE 1716
Cdd:PTZ00121 1843 LEEAD-AFEKHKFNKNNENGEDGNKEAdfNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDI----IDD 1917
|
810
....*....|....*....
gi 1988774933 1717 ELAVSERQKRQAQQERDEI 1735
Cdd:PTZ00121 1918 KLDKDEYIKRDAEETREEI 1936
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
932-1258 |
1.25e-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: 70.10 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 932 RARLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLAt 1011
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE- 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1012 avEQRERLGKEKKQLEERLNEVTDQLTEE-EEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQ 1090
Cdd:TIGR02169 769 --ELEEDLHKLEEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1091 EQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEEL 1170
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1171 EALRTELEDTLDSTAAQQELrsrREAELSElqRCVEEETRRHETQLSELRVKHSAALdslqEQLDNSKRARQSLEKAKAT 1250
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEI---PEEELSL--EDVQAELQRVEEEIRALEPVNMLAI----QEYEEVLKRLDELKEKRAK 997
|
....*...
gi 1988774933 1251 LEEERQNL 1258
Cdd:TIGR02169 998 LEEERKAI 1005
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
868-1426 |
2.00e-11 |
|
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: 69.43 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 868 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELfaeaeemRARLASRKQELEEVLG 947
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEA-------KRNVERQLSTLQAQLS 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 948 ELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDL------------------ 1009
Cdd:pfam01576 528 DMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLdhqrqlvsnlekkqkkfd 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1010 ----------ATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFK 1079
Cdd:pfam01576 608 qmlaeekaisARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSK 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1080 RRMESEAMEAQEQLSDlgmLSSELRGSLAQK---EKEITSLQGRLEEEGARRAEAQRSLREALS-QVSELKEEVENERGM 1155
Cdd:pfam01576 688 RALEQQVEEMKTQLEE---LEDELQATEDAKlrlEVNMQALKAQFERDLQARDEQGEEKRRQLVkQVRELEAELEDERKQ 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1156 RERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQL-----SELRVKH-SAALDS 1229
Cdd:pfam01576 765 RAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILaqskeSEKKLKNlEAELLQ 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1230 LQEQLDNSKRARQslekakaTLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQC 1309
Cdd:pfam01576 845 LQEDLAASERARR-------QAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTL 917
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1310 EIESLSGNLSSSDSKS------------------LRLAKE-----------ISSLESQLHDARELLQDESRQKMALASRV 1360
Cdd:pfam01576 918 QVEQLTTELAAERSTSqksesarqqlerqnkelkAKLQEMegtvkskfkssIAALEAKIAQLEEQLEQESRERQAANKLV 997
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774933 1361 RALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSA 1426
Cdd:pfam01576 998 RRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDA 1063
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
999-1685 |
2.88e-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: 68.94 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 999 ETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVT---DQLTEE-EEKTKSLNKLKNKQEAVIADLEERLKREEQGRLE 1074
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkrrDKLTEEyAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1075 QEKFKRRMES---EAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVEN 1151
Cdd:TIGR02169 394 LEKLKREINElkrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1152 ERGMRERAEKQRRDLSEELEALRTEL----EDTLDSTAAQQELRSRRE------AELSEL-------------------- 1201
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQAraseERVRGGRAVEEVLKASIQgvhgtvAQLGSVgeryataievaagnrlnnvv 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1202 -------QRCVEEETRRHETQ-----LSELRVKHS--------AALDSLQEQLDNSKRAR-------------QSLEKAK 1248
Cdd:TIGR02169 554 veddavaKEAIELLKRRKAGRatflpLNKMRDERRdlsilsedGVIGFAVDLVEFDPKYEpafkyvfgdtlvvEDIEAAR 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1249 ATLEEERQ-NLTSELKSLQASRSESERGRKRADNQLQELSARLAQadreredreermhkLQCEIESLSGNLSSsdskslr 1327
Cdd:TIGR02169 634 RLMGKYRMvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQR--------------LRERLEGLKRELSS------- 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1328 LAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNglmerleEEEERGKELSRQIQTHSQQLTELRKQSEEVNS 1407
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE-------KLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1408 AVEAGDEIRRKLQRELDSaiqrerqkeEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDqcLAEEKAVSA 1487
Cdd:TIGR02169 766 RIEELEEDLHKLEEALND---------LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT--LEKEYLEKE 834
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1488 RLAEERDRAEADSREKETRclalsRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLR 1567
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIE-----KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1568 IQTQELEEELseaensrLRLEVTLQALK---AQFEREISTNEE---------KGEEKRRALSKQVRELE------IQLEE 1629
Cdd:TIGR02169 910 AQIEKKRKRL-------SELKAKLEALEeelSEIEDPKGEDEEipeeelsleDVQAELQRVEEEIRALEpvnmlaIQEYE 982
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774933 1630 ERSQRSQSVSSKKQ-LEAELQEAEAQVETANRGKEEA-MKQLRRLQGQMKEVLRELDD 1685
Cdd:TIGR02169 983 EVLKRLDELKEKRAkLEEERKAILERIEEYEKKKREVfMEAFEAINENFNEIFAELSG 1040
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
871-1215 |
3.26e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 871 RQDEEIQTREAALQKAKEQLTRAEQDYTELDRkhAQLLEEKAVLADQLQAEAELFAEAEEMRARLAsRKQELEEVLGELE 950
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADE--AKKAAEAKKKADEAKKAEEAKKADEAKKAEEA-KKADEAKKAEEKK 1546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 951 TRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQrerlgkEKKQLEERL 1030
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE------AKKAEEAKI 1620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1031 NevTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQE--QLSDLGMLSSELRGSLA 1108
Cdd:PTZ00121 1621 K--AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEakKAEEDEKKAAEALKKEA 1698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1109 QKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENErgmRERAEKQRRDLSEELEALRTELEDTLDSTAAQQ 1188
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED---KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
330 340
....*....|....*....|....*..
gi 1988774933 1189 ELRSRREAELSElqrcvEEETRRHETQ 1215
Cdd:PTZ00121 1776 EKEAVIEEELDE-----EDEKRRMEVD 1797
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
871-1420 |
4.44e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.63 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 871 RQDEEIQTREAAlqKAKEQLTRAEQDYTELDRKHAQLL---------EEKAVLADQLQAEAELFAEAEEMRARLASR--- 938
Cdd:PTZ00121 1194 RKAEDARKAEAA--RKAEEERKAEEARKAEDAKKAEAVkkaeeakkdAEEAKKAEEERNNEEIRKFEEARMAHFARRqaa 1271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 939 -KQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRE 1017
Cdd:PTZ00121 1272 iKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1018 RLGKEKKQLEERLNEVTDQLTEEEEKTKSlNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLG 1097
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKA-DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK 1430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1098 MLSSELRGSlAQKEKEITSLQGRLEE-----------EGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDL 1166
Cdd:PTZ00121 1431 KKADEAKKK-AEEAKKADEAKKKAEEakkaeeakkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1167 SEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEK 1246
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1247 AKATLEEERQNLTSE--LKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESL---SGNLSSS 1321
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEkkMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENkikAAEEAKK 1669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1322 DSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNG---LMERLEEEEERGKELSRQIQTHSQQLTEL 1398
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
570 580
....*....|....*....|..
gi 1988774933 1399 RKQSEEVNSAVEAGDEIRRKLQ 1420
Cdd:PTZ00121 1750 KKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1137-1942 |
9.80e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 9.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1137 EALSQVSELKEEV-ENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQ 1215
Cdd:PTZ00121 1091 EATEEAFGKAEEAkKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1216 LSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRsESERGRKRADNQLQELSARLAQADR 1295
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAK-KAEAVKKAEEAKKDAEEAKKAEEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1296 EREDREERMHKLQCEIESLSGNLSSSDSkslRLAKEISSLEsQLHDARELLQDESRQKMALASRvRALEEEKnglmerle 1375
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEA---RKADELKKAE-EKKKADEAKKAEEKKKADEAKK-KAEEAKK-------- 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1376 eeeerGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAiqrerqkeeekerverqrerlreeiedmt 1455
Cdd:PTZ00121 1317 -----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA----------------------------- 1362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1456 ialqRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEM 1535
Cdd:PTZ00121 1363 ----EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1536 EQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRRA 1615
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1616 LSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEA--------QVETANRGKEEAMKQLRRlqgqmKEVLRELDDSk 1687
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaeekkKAEEAKKAEEDKNMALRK-----AEEAKKAEEA- 1592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1688 vtRDDVISQSKDSEKKiqtLEAEVLHLTEELAVSERQKRQAQQERDEIademvssSSGKNVLSEEKRRldarvnqleeel 1767
Cdd:PTZ00121 1593 --RIEEVMKLYEEEKK---MKAEEAKKAEEAKIKAEELKKAEEEKKKV-------EQLKKKEAEEKKK------------ 1648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1768 eeeqtnnellTERLRKTALQVETLTVQL-QGERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIE 1846
Cdd:PTZ00121 1649 ----------AEELKKAEEENKIKAAEEaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA 1718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1847 TMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQL--EEVEEENSRSSAQKRK 1924
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDK 1798
|
810
....*....|....*...
gi 1988774933 1925 LQRELEELTDSSQTMNRE 1942
Cdd:PTZ00121 1799 KIKDIFDNFANIIEGGKE 1816
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1101-1327 |
1.28e-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: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1101 SELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDT 1180
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1181 LDSTAAQ---QELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQN 1257
Cdd:COG4942 103 KEELAELlraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1258 LTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLR 1327
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
962-1754 |
1.35e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 66.92 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 962 QLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEErlnevtdqltEEE 1041
Cdd:TIGR00618 167 ELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE----------ALQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1042 EKTKSLNKLKNKQEaviadleerlKREEQGRLEQEKFKRRMESEAMEAQEQlsdlgmlsselRGSLAQKEKEITSLQGRL 1121
Cdd:TIGR00618 237 QTQQSHAYLTQKRE----------AQEEQLKKQQLLKQLRARIEELRAQEA-----------VLEETQERINRARKAAPL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1122 EEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRT---ELEDTLDSTAAQQELRSRREAEL 1198
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsQEIHIRDAHEVATSIREISCQQH 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1199 SELQRCVE-EETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQnLTSELKSLQASRSESERGRK 1277
Cdd:TIGR00618 376 TLTQHIHTlQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE-LQQRYAELCAAAITCTAQCE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1278 RADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKeisslESQLHDARELLQdeSRQKMALA 1357
Cdd:TIGR00618 455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLC-----GSCIHPNPARQD--IDNPGPLT 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1358 SRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSaIQRERQKEEEK 1437
Cdd:TIGR00618 528 RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR-LQDLTEKLSEA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1438 ERVERQRERLREEIEDMTIALQRERQNctalekrQKKFDQCLAEEKAVSARLAEERdraeadSREKETRCLALSRalqea 1517
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDLQDVRLH-------LQQCSQELALKLTALHALQLTL------TQERVREHALSIR----- 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1518 QDQKEELERanKQLRLEMEQlvnqqddvgknvHELERARRTLETEAQnlrIQTQELEEELSEAENSRLRLEVTLQALKAQ 1597
Cdd:TIGR00618 669 VLPKELLAS--RQLALQKMQ------------SEKEQLTYWKEMLAQ---CQTLLRELETHIEEYDREFNEIENASSSLG 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1598 feREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMK 1677
Cdd:TIGR00618 732 --SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIG 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1678 EVLRELDDSKVTRDDVISQSKDS-----EKKIQTLeAEVLHLTEELAVSERQKRQAQQERDEIAdEMVSSSSGKNVLSEE 1752
Cdd:TIGR00618 810 QEIPSDEDILNLQCETLVQEEEQflsrlEEKSATL-GEITHQLLKYEECSKQLAQLTQEQAKII-QLSDKLNGINQIKIQ 887
|
..
gi 1988774933 1753 KR 1754
Cdd:TIGR00618 888 FD 889
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
41-86 |
1.65e-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: 1.65e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1988774933 41 AAKRLVWVPSEKQGFESASIREERGDEVEVElTDSQRRVTLSREEV 86
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVE-TEDGKTVTVKKDDV 45
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1529-1835 |
1.72e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1529 KQLRLEME-QLVNQQDD---VGKNVHELERARRTLETEAQnlriQTQELEEELSEAENSRLRLEVT-LQALKAQFErEIS 1603
Cdd:TIGR02168 171 KERRKETErKLERTRENldrLEDILNELERQLKSLERQAE----KAERYKELKAELRELELALLVLrLEELREELE-ELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1604 TNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLREL 1683
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1684 DDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELA-------VSERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRL 1756
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774933 1757 DARVNQLEEELEEEQTNNELLTERLrkTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRGKHR 1835
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1023-1760 |
2.37e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 65.91 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1023 KKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQE----AVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDlgm 1098
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKfylrQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN--- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1099 LSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENE------------RGMRERAEKQRRDL 1166
Cdd:pfam15921 150 TVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmstmhfRSLGSAISKILREL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1167 SEELEALRTEL---EDTLDstAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAA---LDSLQEQLD----- 1235
Cdd:pfam15921 230 DTEISYLKGRIfpvEDQLE--ALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSArsqANSIQSQLEiiqeq 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1236 ----NSKRARQsLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEI 1311
Cdd:pfam15921 308 arnqNSMYMRQ-LSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1312 ESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMErleeeeergkelsRQIQTH 1391
Cdd:pfam15921 387 HKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQME-------------RQMAAI 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1392 SQQLTELRKQSeEVNSAVEAGDEIRRKLQRELDSaiqrerqkeeekerVERQRERLREEIEDMTIALQRERQNCTALEKR 1471
Cdd:pfam15921 454 QGKNESLEKVS-SLTAQLESTKEMLRKVVEELTA--------------KKMTLESSERTVSDLTASLQEKERAIEATNAE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1472 QKKFdqclaeEKAVSARLAE-ERDRAEADS-REKETRCLALSRALQEaQDQKEELERANKQlrlEMEQLVNQQddvGKNV 1549
Cdd:pfam15921 519 ITKL------RSRVDLKLQElQHLKNEGDHlRNVQTECEALKLQMAE-KDKVIEILRQQIE---NMTQLVGQH---GRTA 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1550 HELERARRTLETEAQNLRIQTQeLEEELSEAENSRLRlevTLQALKAQFEREISTNEEKGEEKRRALsKQVRELEIQLEE 1629
Cdd:pfam15921 586 GAMQVEKAQLEKEINDRRLELQ-EFKILKDKKDAKIR---ELEARVSDLELEKVKLVNAGSERLRAV-KDIKQERDQLLN 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1630 ErsqrsqSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEK------- 1702
Cdd:pfam15921 661 E------VKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKvamgmqk 734
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 1703 -------KIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKN-------VLSEEKRRLDARV 1760
Cdd:pfam15921 735 qitakrgQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNkmageleVLRSQERRLKEKV 806
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
866-1369 |
2.63e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 866 LLQVTRQDEEIQTREAalqkaKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEV 945
Cdd:PRK02224 189 LDQLKAQIEEKEEKDL-----HERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 946 LGELETRLEeeeergvqlanEKKKMQQNIQDLEEQLEEEESARQRlLLEKVTLEtkvkslETDLATAVEQRERLGKEKKQ 1025
Cdd:PRK02224 264 RETIAETER-----------EREELAEEVRDLRERLEELEEERDD-LLAEAGLD------DADAEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1026 LEERLNEVTDQLTEEEEKTKSLNKlknkqeaVIADLEERL--KREEQGRLeqekfkrrmESEAMEAQEQLSDlgmlsseL 1103
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLRE-------DADDLEERAeeLREEAAEL---------ESELEEAREAVED-------R 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1104 RGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALR-----TELE 1178
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1179 DT--LDSTAAQQELRSRREAELSELQRCVEEETRRHEtQLSELrVKHSAALDSLQEQLDNSKrarQSLEKAKATLEEERQ 1256
Cdd:PRK02224 463 GSphVETIEEDRERVEELEAELEDLEEEVEEVEERLE-RAEDL-VEAEDRIERLEERREDLE---ELIAERRETIEEKRE 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1257 NLTSELKSLQASRSESERGRKRAdnqlQELSARLAQADREREDREERMHKLQCEIESLsGNLSSSDSKSLRLAKEISSLE 1336
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAA----AEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLR 612
|
490 500 510
....*....|....*....|....*....|....
gi 1988774933 1337 SQLHDARElLQDESRQKMA-LASRVRALEEEKNG 1369
Cdd:PRK02224 613 EKREALAE-LNDERRERLAeKRERKRELEAEFDE 645
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1019-1363 |
3.46e-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: 64.32 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1019 LGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEerlkreeqgrleQEKfKRRMESEAMEAQEQLSdlgm 1098
Cdd:pfam19220 1 IGQRNELLRVRLGEMADRLEDLRSLKADFSQLIEPIEAILRELP------------QAK-SRLLELEALLAQERAA---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1099 lSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQ-------RRDLSEELE 1171
Cdd:pfam19220 64 -YGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQlaaeteqNRALEEENK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1172 ALRTEL----EDTLDSTAAQQELRSRR---EAELSELQRCVEE---ETRRHETQLSEL---RVKHSAALDSLQEQLDNSK 1238
Cdd:pfam19220 143 ALREEAqaaeKALQRAEGELATARERLallEQENRRLQALSEEqaaELAELTRRLAELetqLDATRARLRALEGQLAAEQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1239 RARQsleKAKATLEEERQNLTSELKSLqasrsesergrkraDNQLQELSARLAQADREREDREERMHKLQCEIESLSGNL 1318
Cdd:pfam19220 223 AERE---RAEAQLEEAVEAHRAERASL--------------RMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRL 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1988774933 1319 SSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRAL 1363
Cdd:pfam19220 286 KEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEML 330
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1189-1924 |
3.70e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1189 ELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQE--QLDNSKRARQSLEKAKATLEEERQNLTSELKSLQ 1266
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDarKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1267 ASRSESERgrkRADNQLQELSARLAQADREREDREERMHKLQCEieslsgnlSSSDSKSLRLAKEISSLESQLHDARELL 1346
Cdd:PTZ00121 1163 ARKAEEAR---KAEDAKKAEAARKAEEVRKAEELRKAEDARKAE--------AARKAEEERKAEEARKAEDAKKAEAVKK 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1347 QDESRQKmalASRVRALEEEKNGLMERLEEEEERGKELSRQ--IQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELD 1424
Cdd:PTZ00121 1232 AEEAKKD---AEEAKKAEEERNNEEIRKFEEARMAHFARRQaaIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAK 1308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1425 SAIQRERQKEEEKERVERQRERLREEIEDMtialqrerqnctalEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKE 1504
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKA--------------EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1505 TRclalSRALQEAQDQKEELERANkQLRLEMEQLVNQQDDVGKNVHELERARRtLETEAQNLRIQTQELEeelseaensr 1584
Cdd:PTZ00121 1375 EA----KKKADAAKKKAEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADE-AKKKAEEKKKADEAKK---------- 1438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1585 lrlevtlqalKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEE 1664
Cdd:PTZ00121 1439 ----------KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1665 AMKQLRRLQGQMKEVLRELDDSKVTRddvisQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSS 1744
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAK-----KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1745 GKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETlTVQLQGERTLAQKAEAAR--EQLEKQNKELKAR 1822
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE-EEKKKVEQLKKKEAEEKKkaEELKKAEEENKIK 1662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1823 LGEMEGAVRGKHRmsvAALEAKIEtmeeqleqerqeraianklmRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLK 1902
Cdd:PTZ00121 1663 AAEEAKKAEEDKK---KAEEAKKA--------------------EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
|
730 740
....*....|....*....|....*.
gi 1988774933 1903 QLKRQLEE----VEEENSRSSAQKRK 1924
Cdd:PTZ00121 1720 ELKKAEEEnkikAEEAKKEAEEDKKK 1745
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
868-1279 |
4.16e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 868 QVTRQDEEIQTREAalqKAKEQLTRAEQDYTELDRKHAQLLEEKA---VLADQLQAE-AELFAEAEEMRARLASRKQELE 943
Cdd:PTZ00121 1346 EAAKAEAEAAADEA---EAAEEKAEAAEKKKEEAKKKADAAKKKAeekKKADEAKKKaEEDKKKADELKKAAAAKKKADE 1422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 944 EVLGELETRLEEEEERGVQLAN---------EKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLET----DLA 1010
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKkadeakkkaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAkkkaDEA 1502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1011 TAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEA-VIADLEERLKREEQGRLEQEKFKRRMESEAMEA 1089
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK 1582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1090 QEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRE-----------R 1158
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEelkkaeeenkiK 1662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1159 AEKQRRDLSEE---LEALRTELEDtlDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLD 1235
Cdd:PTZ00121 1663 AAEEAKKAEEDkkkAEEAKKAEED--EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1988774933 1236 NSKRARQSLEKakatlEEERQNLTSELKSLQASRSESERGRKRA 1279
Cdd:PTZ00121 1741 EDKKKAEEAKK-----DEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
874-1280 |
5.59e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 874 EEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEaelfaeaeemRARLASRKQELEEVLGELETRL 953
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA----------REAVEDRREEIEELEEEIEELR 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 954 EEEEERGVQLANekkkmqqniqdleeqleeEESARQRLLLEKVTLETKVKSLETDLATAveqRERLGKEKKQLEERLNEV 1033
Cdd:PRK02224 398 ERFGDAPVDLGN------------------AEDFLEELREERDELREREAELEATLRTA---RERVEEAEALLEAGKCPE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1034 TDQLTEEEEKTKSLNKLKNKqeavIADLEERLkreEQGRLEQEKFKRRMES--EAMEAQEQLSDLGMLSSELRGSLAQKE 1111
Cdd:PRK02224 457 CGQPVEGSPHVETIEEDRER----VEELEAEL---EDLEEEVEEVEERLERaeDLVEAEDRIERLEERREDLEELIAERR 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1112 KEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEAL---RTELEDTLDSTAAQQ 1188
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLeriRTLLAAIADAEDEIE 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1189 ELRSRREAeLSELQRCVEEETRRHETQLSELRVKH-SAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQA 1267
Cdd:PRK02224 610 RLREKREA-LAELNDERRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
410
....*....|...
gi 1988774933 1268 SRSESERGRKRAD 1280
Cdd:PRK02224 689 ELEELEELRERRE 701
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
987-1427 |
6.67e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 6.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 987 ARQRLLLEKVTLETKvkslETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKtksLNKLKNKQEAVIADLEERLK 1066
Cdd:COG4913 272 AELEYLRAALRLWFA----QRRLELLEAELEELRAELARLEAELERLEARLDALREE---LDELEAQIRGNGGDRLEQLE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1067 REEQgRLEQEKfkRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELK 1146
Cdd:COG4913 345 REIE-RLEREL--EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1147 EEVENERgmrERAEKQRRDLSEELEALRTELEDTLDST----------------------AAQQELRSRR------EAEL 1198
Cdd:COG4913 422 RELEAEI---ASLERRKSNIPARLLALRDALAEALGLDeaelpfvgelievrpeeerwrgAIERVLGGFAltllvpPEHY 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1199 SELQRCVEE------------ETRRHETQLS---------ELRVKHSAALDSLQ---------------EQLDNSKRA-- 1240
Cdd:COG4913 499 AAALRWVNRlhlrgrlvyervRTGLPDPERPrldpdslagKLDFKPHPFRAWLEaelgrrfdyvcvdspEELRRHPRAit 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1241 --------------------RQSL------EKAKATLEEERQNLTSELKSLQASRSESERgRKRADNQLQELSARLAQAD 1294
Cdd:COG4913 579 ragqvkgngtrhekddrrriRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALEA-ELDALQERREALQRLAEYS 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1295 REREDREERMHKLQcEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLmerl 1374
Cdd:COG4913 658 WDEIDVASAEREIA-ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL---- 732
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1988774933 1375 eeEEERGKELSRQIQTHSQQLTELRKQseevnsavEAGDEIRRKLQRELDSAI 1427
Cdd:COG4913 733 --QDRLEAAEDLARLELRALLEERFAA--------ALGDAVERELRENLEERI 775
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1456-1709 |
7.33e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 63.99 E-value: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1456 IALQRERQ-NCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLE 1534
Cdd:pfam17380 342 MAMERERElERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1535 MEQLVNQQDDVGK---NVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVtlqalkaqfEREISTNEEKGEE 1611
Cdd:pfam17380 422 MEQIRAEQEEARQrevRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL---------EKEKRDRKRAEEQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1612 KRRALSKQVRE-LEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELD--DSKV 1688
Cdd:pfam17380 493 RRKILEKELEErKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSrlEAME 572
|
250 260
....*....|....*....|.
gi 1988774933 1689 TRDDVISQSKDSEKKIQTLEA 1709
Cdd:pfam17380 573 REREMMRQIVESEKARAEYEA 593
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1197-1946 |
1.01e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.98 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1197 ELSELQRCVEEETRRHETQLSELR---VKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELkslQASRSESE 1273
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRqsvIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHEL---EAAKCLKE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1274 RGRKRADNQLQEL-------SARLAQADREREDREERMHKLQCEIESLSG----NLSSSDSKSLR-LAKEISSLESQL-- 1339
Cdd:pfam15921 163 DMLEDSNTQIEQLrkmmlshEGVLQEIRSILVDFEEASGKKIYEHDSMSTmhfrSLGSAISKILReLDTEISYLKGRIfp 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1340 -HDARELLQDESRQKMAL-----ASRVRAL----EEEKNGLMERLEEEEERGKELSRQI-----QTHSQQLTELRKQSEE 1404
Cdd:pfam15921 243 vEDQLEALKSESQNKIELllqqhQDRIEQLisehEVEITGLTEKASSARSQANSIQSQLeiiqeQARNQNSMYMRQLSDL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1405 VNSAVEAGDEIRrKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTA-LEKRQKKfdqcLAEEK 1483
Cdd:pfam15921 323 ESTVSQLRSELR-EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAdLHKREKE----LSLEK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1484 AVSARLAEeRD----------RAEADSREKETRCL-ALSRALQ-EAQDQKEELERA--NKQLRLE-----MEQLVNQQDD 1544
Cdd:pfam15921 398 EQNKRLWD-RDtgnsitidhlRRELDDRNMEVQRLeALLKAMKsECQGQMERQMAAiqGKNESLEkvsslTAQLESTKEM 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1545 VGKNVHELERARRTLETEAQNLR-----IQTQELEEELSEAENSRLRLEVTLQALKAQFEReistNEEkgeEKRRALSKQ 1619
Cdd:pfam15921 477 LRKVVEELTAKKMTLESSERTVSdltasLQEKERAIEATNAEITKLRSRVDLKLQELQHLK----NEG---DHLRNVQTE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1620 VRELEIQLEEERSQRSQSvssKKQLEAELQEAEAQVETANRGKEEAMKqlrrLQGQMKEVLRELDDSKVTRDDVISQSKD 1699
Cdd:pfam15921 550 CEALKLQMAEKDKVIEIL---RQQIENMTQLVGQHGRTAGAMQVEKAQ----LEKEINDRRLELQEFKILKDKKDAKIRE 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1700 SEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEkrrldarvnqleeeleeeqtnNELLTE 1779
Cdd:pfam15921 623 LEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSED---------------------YEVLKR 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1780 RLRKTALQVETLTVQLQgertlaQKAEAAREQLEKQNKELKArlgeMEGAvrGKHRMSVAALEAKIETmeeqlEQERQER 1859
Cdd:pfam15921 682 NFRNKSEEMETTTNKLK------MQLKSAQSELEQTRNTLKS----MEGS--DGHAMKVAMGMQKQIT-----AKRGQID 744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1860 AIANKLmrkteKKLKEVMMQAEDERRHadqyreqldksmvrlkqLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTM 1939
Cdd:pfam15921 745 ALQSKI-----QFLEEAMTNANKEKHF-----------------LKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRL 802
|
....*..
gi 1988774933 1940 NREISSL 1946
Cdd:pfam15921 803 KEKVANM 809
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
961-1734 |
1.28e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 63.59 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 961 VQLANEKKKMQQNIQDLEEQLEEEESARQRLLL--EKVTLETKVKSLET-DLATAVEQRERLGKEKKQLEERLNEVTDQL 1037
Cdd:pfam05483 95 VSIEAELKQKENKLQENRKIIEAQRKAIQELQFenEKVSLKLEEEIQENkDLIKENNATRHLCNLLKETCARSAEKTKKY 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1038 TEEEEKTKSLN-KLKNKQEAVIADLEERLKREEQGRLEQEkFKRRMESEAMEAQEQlsdlgmlssELRGSLAQKEKEITS 1116
Cdd:pfam05483 175 EYEREETRQVYmDLNNNIEKMILAFEELRVQAENARLEMH-FKLKEDHEKIQHLEE---------EYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1117 LQGRLEEEGARRAEAQRSLREALSQVSELKEEVE-NERGMRERAEKQRRdLSEELEALRTELEDTLDSTAAQQE---LRS 1192
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLLEESRDKANQLEEKTKlQDENLKELIEKKDH-LTKELEDIKMSLQRSMSTQKALEEdlqIAT 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1193 RREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLdnsKRARQSLEKAkatlEEERQNLTSELKSLQASRSES 1272
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELL---RTEQQRLEKN----EDQLKIITMELQKKSSELEEM 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1273 ERGRKRADNQLQELSARLAQadreredreermhklqceieslsgnlsssdskslrlakeisslesqlhdaRELLQDESRQ 1352
Cdd:pfam05483 397 TKFKNNKEVELEELKKILAE--------------------------------------------------DEKLLDEKKQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1353 KMALASRVRALEEEKNGLMerleeeeergkelsrqiQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQ 1432
Cdd:pfam05483 427 FEKIAEELKGKEQELIFLL-----------------QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1433 KEEEKERVERQRERLREEIEDMTIALQRERQ---NCTALEKRQKKFDQCLaEEKAVSARLAEERDRAEADSREKETRCla 1509
Cdd:pfam05483 490 LTAHCDKLLLENKELTQEASDMTLELKKHQEdiiNCKKQEERMLKQIENL-EEKEMNLRDELESVREEFIQKGDEVKC-- 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1510 lsrALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEV 1589
Cdd:pfam05483 567 ---KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLEL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1590 TLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQL 1669
Cdd:pfam05483 644 ELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER 723
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774933 1670 RRLQGQMKEVLRELDDSKVTRddvisqskdsEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDE 1734
Cdd:pfam05483 724 DSELGLYKNKEQEQSSAKAAL----------EIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
987-1733 |
1.50e-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: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 987 ARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAV------IAD 1060
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIehnlskIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1061 LEERLKREEQGRLEQEKFKRRMESEAME----AQEQLSD----------------------LGMLSSELRgSLAQKEKEI 1114
Cdd:TIGR00606 267 LDNEIKALKSRKKQMEKDNSELELKMEKvfqgTDEQLNDlyhnhqrtvrekerelvdcqreLEKLNKERR-LLNQEKTEL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1115 TSLQGRLEEEGARRAEAQR---SLREALSQVSEL---KEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQ 1188
Cdd:TIGR00606 346 LVEQGRLQLQADRHQEHIRardSLIQSLATRLELdgfERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1189 ELRSRREAELSELQRCVEEETRRHETQLSELRVKHSaALDSLQEQLDNSKRARQSLEKAKATLEEERQN-----LTSELK 1263
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIK-ELQQLEGSSDRILELDQELRKAERELSKAEKNsltetLKKEVK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1264 SLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHK---------------------------LQCEIESLSG 1316
Cdd:TIGR00606 505 SLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKdeqirkiksrhsdeltsllgyfpnkkqLEDWLHSKSK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1317 NLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRV------RALEEEKNGLMERLEEEEERGKELSRQIQT 1390
Cdd:TIGR00606 585 EINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAV 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1391 HSQQLTELRKQSEEVNSAVEAGDEIRRKLQrELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNctALEK 1470
Cdd:TIGR00606 665 YSQFITQLTDENQSCCPVCQRVFQTEAELQ-EFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQS--IIDL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1471 RQKKFDQCLAEEKAVSARLAEERDRAEADSREKET---------RCLALSRALQEAQDQKEELERANKQLRLEMeqlvnQ 1541
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTimpeeesakVCLTDVTIMERFQMELKDVERKIAQQAAKL-----Q 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1542 QDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQfEREISTNEEKG---EEKRRALSK 1618
Cdd:TIGR00606 817 GSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE-KLQIGTNLQRRqqfEEQLVELST 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1619 QVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAM----KQLRRLQGQMKEVLRELDDSKvtrDDvi 1694
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVndikEKVKNIHGYMKDIENKIQDGK---DD-- 970
|
810 820 830
....*....|....*....|....*....|....*....
gi 1988774933 1695 sQSKDSEKKIQTLEAEvlhlteelaVSERQKRQAQQERD 1733
Cdd:TIGR00606 971 -YLKQKETELNTVNAQ---------LEECEKHQEKINED 999
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1100-1678 |
3.06e-09 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 62.08 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1100 SSELRGSLAQKEKeiTSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRdlsEELEALRTELED 1179
Cdd:pfam07111 52 SLELEGSQALSQQ--AELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQ---AEAEGLRAALAG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1180 tldSTAAQQELRSRREAELSELQRCveeetrrHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEE----- 1254
Cdd:pfam07111 127 ---AEMVRKNLEEGSQRELEEIQRL-------HQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQlaeaq 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1255 ------RQNLTSELKSLQASRSESERGRKRADNQL-------------QELSARLAQADREREDREERMHKLQCEIESLS 1315
Cdd:pfam07111 197 keaellRKQLSKTQEELEAQVTLVESLRKYVGEQVppevhsqtwelerQELLDTMQHLQEDRADLQATVELLQVRVQSLT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1316 GNLSSSDSKSLRLAKEISSLESQL-HDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKElsrQIQTHSQQ 1394
Cdd:pfam07111 277 HMLALQEEELTRKIQPSDSLEPEFpKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQE---QVTSQSQE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1395 LTELRKQSEEVNSAVEAGDEIRRKLQRELDSAiqrerqkeeeKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKK 1474
Cdd:pfam07111 354 QAILQRALQDKAAEVEVERMSAKGLQMELSRA----------QEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTR 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1475 FDQCLAEEKAVSARLAEERdRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQ------------- 1541
Cdd:pfam07111 424 VEQAVARIPSLSNRLSYAV-RKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREErnrldaelqlsah 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1542 --QDDVGKNVHELERARRTLETEAQNLRiqtQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKR---RAL 1616
Cdd:pfam07111 503 liQQEVGRAREQGEAERQQLSEVAQQLE---QELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEiygQAL 579
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 1617 SKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKE 1678
Cdd:pfam07111 580 QEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARK 641
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1036-1813 |
3.62e-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: 62.29 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1036 QLTEEEEK--TKSLNKLKNKQEAVIADLEeRLKREEQGR---LEQEKFKRRMESEAMEAQEQLSDLgmLSSELRGSLAQK 1110
Cdd:TIGR00618 108 QLYLEQKKgrGRILAAKKSETEEVIHDLL-KLDYKTFTRvvlLPQGEFAQFLKAKSKEKKELLMNL--FPLDQYTQLALM 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1111 EKEIT-SLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQE 1189
Cdd:TIGR00618 185 EFAKKkSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1190 LRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQ-------LDNSKRARQSLEKAKATLEEERQNLTSEL 1262
Cdd:TIGR00618 265 LRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQaqrihteLQSKMRSRAKLLMKRAAHVKQQSSIEEQR 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1263 KSLQASRSESERGRKRADNQLQELSARLAQadrerEDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDA 1342
Cdd:TIGR00618 345 RLLQTLHSQEIHIRDAHEVATSIREISCQQ-----HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1343 RELlqdesRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEvnsaveagdEIRRKLQRE 1422
Cdd:TIGR00618 420 RDL-----QGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ---------TKEQIHLQE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1423 LDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRErQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSRE 1502
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG-PLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQ 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1503 ketrclalsraLQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAEN 1582
Cdd:TIGR00618 565 -----------MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1583 SRlRLEVTLQALKAQFEREIstnEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGK 1662
Cdd:TIGR00618 634 LQ-QCSQELALKLTALHALQ---LTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1663 EEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQS-------KDSEKKIQTLEAEVLHLTEELAV----SERQKRQAQQE 1731
Cdd:TIGR00618 710 ETHIEEYDREFNEIENASSSLGSDLAAREDALNQSlkelmhqARTVLKARTEAHFNNNEEVTAALqtgaELSHLAAEIQF 789
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1732 RDEIADEMVSSSSGKNVLSEEKRRLDARVnQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQ 1811
Cdd:TIGR00618 790 FNRLREEDTHLLKTLEAEIGQEIPSDEDI-LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQ 868
|
..
gi 1988774933 1812 LE 1813
Cdd:TIGR00618 869 AK 870
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
868-1410 |
4.28e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 868 QVTRQDEEIQTREAALQKAKEQLTRAEqdytELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKqeleevlg 947
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAA----EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK-------- 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 948 eletrleeeeergvqlANEKKKMQQniqdleeqleeeesarqrllLEKVTLETKVKSLEtdLATAVEQRERLGKEKKQLE 1027
Cdd:PTZ00121 1387 ----------------AEEKKKADE--------------------AKKKAEEDKKKADE--LKKAAAAKKKADEAKKKAE 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1028 ERlnEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSL 1107
Cdd:PTZ00121 1429 EK--KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1108 AQKEK--EITSLQGRLEEEGARRAEAQRSLREAlsqvsELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTA 1185
Cdd:PTZ00121 1507 EAKKKadEAKKAEEAKKADEAKKAEEAKKADEA-----KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1186 AQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAAldslqEQLDNSKRARQSLEKAKATLEEERQNLTSELKSL 1265
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-----EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1266 QASRSESERGRKRADNQLQElsARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDAREL 1345
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKKK--AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774933 1346 LQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQltELRKQSEEVNSAVE 1410
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVD 1797
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1487-1951 |
4.63e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 61.73 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1487 ARLAEERDRAEADSREKETrclaLSRALQEAQDQKEELERANKQLRLE----------MEQLVNQQDDVGknvHELERAR 1556
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKK----MQQHIQDLEEQLDEEEAARQKLQLEkvtteakikkLEEDILLLEDQN---SKLSKER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1557 RTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKgEEKRRALSKQVRELEIQLEEERSQRSQ 1636
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQEL-EKAKRKLEGESTDLQEQIAELQAQIAE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1637 SVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTE 1716
Cdd:pfam01576 234 LRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1717 ELAVSERQKRQAQQERDEIademvssssgKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLR-------KTALQVE 1789
Cdd:pfam01576 314 TTAAQQELRSKREQEVTEL----------KKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKrnkanleKAKQALE 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1790 TLTVQLQGE-RTLAQ---KAEAAREQLEKQNKELKARLGEMEgAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKL 1865
Cdd:pfam01576 384 SENAELQAElRTLQQakqDSEHKRKKLEGQLQELQARLSESE-RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1866 MRKTEKKLKEVMMQAEDERRHADQYREQLdksmvrlkqlkRQLEEveeensrssaQKRKLQRELEELTDSSQTMNREISS 1945
Cdd:pfam01576 463 VSSLESQLQDTQELLQEETRQKLNLSTRL-----------RQLED----------ERNSLQEQLEEEEEAKRNVERQLST 521
|
....*.
gi 1988774933 1946 LRNQLS 1951
Cdd:pfam01576 522 LQAQLS 527
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
871-1289 |
4.98e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.90 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 871 RQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEaelfaeaeemRARLasrkqeleevlgele 950
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAA----------SDHL--------------- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 951 trleeeeergvQLANEKKKMQQNIQdleeqleeeesaRQRLLLEKvtLETKVKSLETDLATAVEQRERLGKEKKQLEERL 1030
Cdd:PRK04863 338 -----------NLVQTALRQQEKIE------------RYQADLEE--LEERLEEQNEVVEEADEQQEENEARAEAAEEEV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1031 NEVTDQLTE-----EEEKTKSLnklkNKQEAVIAdLEERLKREEQGRLEQEKFKRRMesEAMEAQEQLSDLGMLSSELRG 1105
Cdd:PRK04863 393 DELKSQLADyqqalDVQQTRAI----QYQQAVQA-LERAKQLCGLPDLTADNAEDWL--EEFQAKEQEATEELLSLEQKL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1106 SLAQKEKE--------ITSLQGRLEeegarRAEAQRSLREALSQVSELKEEVENERGMR------ERAEKQRRDLSEELE 1171
Cdd:PRK04863 466 SVAQAAHSqfeqayqlVRKIAGEVS-----RSEAWDVARELLRRLREQRHLAEQLQQLRmrlselEQRLRQQQRAERLLA 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1172 ALRTELEDTLDSTAAQQELRSRREAELSELQRCVEE------ETRRHETQLSELRVKHSA----------ALDSLQEQLD 1235
Cdd:PRK04863 541 EFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEarerrmALRQQLEQLQARIQRLAArapawlaaqdALARLREQSG 620
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1988774933 1236 NSKRARQSlekakatLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSAR 1289
Cdd:PRK04863 621 EEFEDSQD-------VTEYMQQLLERERELTVERDELAARKQALDEEIERLSQP 667
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
825-1293 |
5.11e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 825 RKAFLKKQQQLSALRVMQRNCAAYLKLRNWQwwRLFTKVKPLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKH 904
Cdd:COG4913 241 HEALEDAREQIELLEPIRELAERYAAARERL--AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 905 AQLLEEKAVLADQLQaeAELFAEAEEMRARLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEE 984
Cdd:COG4913 319 DALREELDELEAQIR--GNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 985 ESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEeektkslnkLKNKQEAV--IADLE 1062
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA---------LGLDEAELpfVGELI 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1063 ERLKREEQGRLEQEK----FKRRM------ESEAMEAQEQLSDLGMLSSE----LRGSLAQKEKEITSLQGRLE-EEGAR 1127
Cdd:COG4913 468 EVRPEEERWRGAIERvlggFALTLlvppehYAAALRWVNRLHLRGRLVYErvrtGLPDPERPRLDPDSLAGKLDfKPHPF 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1128 RAEAQRSLREALS-----QVSELKEE---------VENERGMRE---------------RAEKQRRDLSEELEALRTELE 1178
Cdd:COG4913 548 RAWLEAELGRRFDyvcvdSPEELRRHpraitragqVKGNGTRHEkddrrrirsryvlgfDNRAKLAALEAELAELEEELA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1179 DTLDSTAAQQELRSRREAELSELQRC------------VEEETRRHETQLSELRvKHSAALDSLQEQLDNSKRARQSLEK 1246
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRLaeyswdeidvasAEREIAELEAELERLD-ASSDDLAALEEQLEELEAELEELEE 706
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 1247 AKATLEEERQNLTSELKSLQASRSESER-----GRKRADNQLQELSARLAQA 1293
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEEELDELQDrleaaEDLARLELRALLEERFAAA 758
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
864-1278 |
6.42e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 864 KPLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAE-AELFAEAEEMRARLASRKQEL 942
Cdd:PRK03918 345 KKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEiEEEISKITARIGELKKEIKEL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 943 EEVLGELETRLEEEEERGVQLANEKKKMqqniqdleeqleeeesarqrlLLEKVTLEtkVKSLETDLATAVEQRERLGKE 1022
Cdd:PRK03918 425 KKAIEELKKAKGKCPVCGRELTEEHRKE---------------------LLEEYTAE--LKRIEKELKEIEEKERKLRKE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1023 KKQLEE---------RLNEVTDQLTEEEEKTKSLNKLKNKQEAViadlEERLKREEQGRLEQEkfKRRMESEAMEAQEQL 1093
Cdd:PRK03918 482 LRELEKvlkkeseliKLKELAEQLKELEEKLKKYNLEELEKKAE----EYEKLKEKLIKLKGE--IKSLKKELEKLEELK 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1094 SDLGMLSSELRgslaQKEKEITSLQGRLEEEGArraeaqRSLREALSQVSELkEEVENERGMRERAEKQRRDLSEELEAL 1173
Cdd:PRK03918 556 KKLAELEKKLD----ELEEELAELLKELEELGF------ESVEELEERLKEL-EPFYNEYLELKDAEKELEREEKELKKL 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1174 RTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRhetQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEE 1253
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE---ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE 701
|
410 420
....*....|....*....|....*...
gi 1988774933 1254 ERQNLTS---ELKSLQASRSESERGRKR 1278
Cdd:PRK03918 702 ELEEREKakkELEKLEKALERVEELREK 729
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1227-1951 |
7.78e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1227 LDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHK 1306
Cdd:TIGR04523 42 LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1307 LQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGL---MERLEEEEERGKE 1383
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIqknIDKIKNKLLKLEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1384 LSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELdsaiqrerqkeeekervERQRERLREEIEDMTIALQRERQ 1463
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI-----------------NEKTTEISNTQTQLNQLKDEQNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1464 NCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLalsralqeaQDQKEELERANKQLRlemeQLVNQQD 1543
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWN---------KELKSELKNQEKKLE----EIQNQIS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1544 DVGKNVHELERARRTLETEAQNLRiqtqeleeelseAENSRLRLEvtLQALKAQFEREISTNEEKGEEKRRaLSKQVREL 1623
Cdd:TIGR04523 332 QNNKIISQLNEQISQLKKELTNSE------------SENSEKQRE--LEEKQNEIEKLKKENQSYKQEIKN-LESQINDL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1624 EIQLEEersqrsqsvssKKQLEAELQEaeaQVETANRGKEEAMKQLRRLqgqmkevLRELDDSKVTRDDVISQSKDSEKK 1703
Cdd:TIGR04523 397 ESKIQN-----------QEKLNQQKDE---QIKKLQQEKELLEKEIERL-------KETIIKNNSEIKDLTNQDSVKELI 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1704 IQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNelltERLRK 1783
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI----EKLES 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1784 TALQVETLTVQLQGErTLAQKAEAAREQLEKQNKELKARLGEMegavrgKHrmsvaaleakietmeeqleqerqeraiAN 1863
Cdd:TIGR04523 532 EKKEKESKISDLEDE-LNKDDFELKKENLEKEIDEKNKEIEEL------KQ---------------------------TQ 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1864 KLMRKTEKKLKEVMMQAEDERrhaDQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREI 1943
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEK---KDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
....*...
gi 1988774933 1944 SSLRNQLS 1951
Cdd:TIGR04523 655 KEIRNKWP 662
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
872-1421 |
9.00e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 872 QDEEIQTReaaLQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGE--- 948
Cdd:PRK03918 187 RTENIEEL---IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKire 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 949 LETRLEEEEERGVQLaNEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQ---RERLGKEKKQ 1025
Cdd:PRK03918 264 LEERIEELKKEIEEL-EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERikeLEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1026 LEERLNEVTDQLTEEEEKTKSLNKLKNKQEAvIADLEERLKREEQGRLEQEkfKRRMESEAMEAQEQLSDLGMLSSELRG 1105
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAKAKKEE-LERLKKRLTGLTPEKLEKE--LEELEKAKEEIEEEISKITARIGELKK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1106 SLAQKEKEITSLQG----------RLEEEgaRRAEAQRSLREALSQVS-ELKEEVENERGMRERAEKQRRDLSEELEALR 1174
Cdd:PRK03918 420 EIKELKKAIEELKKakgkcpvcgrELTEE--HRKELLEEYTAELKRIEkELKEIEEKERKLRKELRELEKVLKKESELIK 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1175 teLEDTLDS-TAAQQELRSRREAELSElqrcVEEETRRHETQLSELRVKHSAALDSLqEQLDNSKRARQSLEKAKATLEE 1253
Cdd:PRK03918 498 --LKELAEQlKELEEKLKKYNLEELEK----KAEEYEKLKEKLIKLKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1254 ERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEIS 1333
Cdd:PRK03918 571 ELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1334 SLESQLHDarELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQThsqqLTELRKQSEEVNSAVEAGD 1413
Cdd:PRK03918 651 ELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE----REKAKKELEKLEKALERVE 724
|
....*...
gi 1988774933 1414 EIRRKLQR 1421
Cdd:PRK03918 725 ELREKVKK 732
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
868-1545 |
1.04e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 868 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQL---LEEKAVLADQLQaeaelfaeaeemrARLASRKQELEE 944
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELereIEEERKRRDKLT-------------EEYAELKEELED 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 945 VLGELEtrleEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQrerlgkeKK 1024
Cdd:TIGR02169 369 LRAELE----EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK-------IN 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1025 QLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLeerlkREEQGRLEQEKFKRRMESEAMEAQEQLSDLG------- 1097
Cdd:TIGR02169 438 ELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL-----KEEYDRVEKELSKLQRELAEAEAQARASEERvrggrav 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1098 --MLSSELR---GSLAQ----KEKEITSLQ----GRL-----EEEG--------ARRAEAQRS-------LREALSQVSE 1144
Cdd:TIGR02169 513 eeVLKASIQgvhGTVAQlgsvGERYATAIEvaagNRLnnvvvEDDAvakeaielLKRRKAGRAtflplnkMRDERRDLSI 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1145 LKEE---------VENERGMRERAEKQRRD--LSEELEALRTELED----TLDS--------------TAAQQELRSRRE 1195
Cdd:TIGR02169 593 LSEDgvigfavdlVEFDPKYEPAFKYVFGDtlVVEDIEAARRLMGKyrmvTLEGelfeksgamtggsrAPRGGILFSRSE 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1196 -AELSELQRCVEEETRRHETQLSELRvKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESER 1274
Cdd:TIGR02169 673 pAELQRLRERLEGLKRELSSLQSELR-RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1275 GRKRADNQLQELSARLAQadreredREERMHKLQCEIESLSGNLSSSDSKSLRlaKEISSLESQLHDARELLQDESRQKM 1354
Cdd:TIGR02169 752 EIENVKSELKELEARIEE-------LEEDLHKLEEALNDLEARLSHSRIPEIQ--AELSKLEEEVSRIEARLREIEQKLN 822
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1355 ALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKE 1434
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1435 EEKERVERQRERLREEIEDMTIALQRERQNCTALEkRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLA----- 1509
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLaiqey 981
|
730 740 750
....*....|....*....|....*....|....*...
gi 1988774933 1510 --LSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDV 1545
Cdd:TIGR02169 982 eeVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1014-1221 |
1.63e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.65 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1014 EQRERLGKEKKQLEERLNEVTDQLTEEEEKtksLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQL 1093
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAA---LEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1094 SDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVEN-ERGMRERAEKQRRDLSEELEA 1172
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAlRAQLQQEAQRILASLEAELEA 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774933 1173 LRT---ELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHET---QLSELRV 1221
Cdd:COG3206 325 LQAreaSLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESllqRLEEARL 379
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1036-1264 |
1.76e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1036 QLTEEEEKTKSLNKLKNKqeavIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEIT 1115
Cdd:COG4942 18 QADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1116 SLQGRLEEegaRRAEAQRSLREA--LSQVSELK--------EEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTA 1185
Cdd:COG4942 94 ELRAELEA---QKEELAELLRALyrLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774933 1186 AQQELRSRREAELSELQRCVEEETRRHETQLSELRvkhsAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKS 1264
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLE----KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1136-1675 |
1.88e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1136 REALSQVSELKEEVENERGMRERAEKQRR---------DLSEELEALRTELE------DTLDSTAAQQELR------SRR 1194
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqiellepirELAERYAAARERLAeleylrAALRLWFAQRRLElleaelEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1195 EAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESER 1274
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1275 G-----------RKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSL----RLAKEISSLESQL 1339
Cdd:COG4913 381 EfaalraeaaalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLalrdALAEALGLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1340 HDARELLQ---DESRQKMAL-----------------ASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLtelr 1399
Cdd:COG4913 461 PFVGELIEvrpEEERWRGAIervlggfaltllvppehYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSL---- 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1400 kqSEEVNSAV-EAGDEIRRKLQRELD--------------SAIQRERQKEEEKERVERQRERLREEI-------EDMTIA 1457
Cdd:COG4913 537 --AGKLDFKPhPFRAWLEAELGRRFDyvcvdspeelrrhpRAITRAGQVKGNGTRHEKDDRRRIRSRyvlgfdnRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1458 LQRERQNCTA-LEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRclALSRALQEAQDQKEELERAN---KQLRL 1533
Cdd:COG4913 615 LEAELAELEEeLAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA--SAEREIAELEAELERLDASSddlAALEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1534 EMEQLVNQQDDVGKNVHELERARRTLETEAQnlRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREIStnEEKGEEKR 1613
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELE--QAEEELDELQDRLEAAEDLARLELRALLEERFAAALG--DAVERELR 768
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774933 1614 RALSKQVRELEIQLEEERSQRSQSVSS-KKQLEAELQEAEAQVETAnrgkEEAMKQLRRLQGQ 1675
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESL----PEYLALLDRLEED 827
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1054-1293 |
2.04e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1054 QEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQR 1133
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1134 SLREALSQVSELkeevenergMRErAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEetrrhe 1213
Cdd:COG4942 98 ELEAQKEELAEL---------LRA-LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1214 tqLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQA 1293
Cdd:COG4942 162 --LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1106-1334 |
3.92e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1106 SLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVEnergmreRAEKQRRDLSEELEALRTELEDTLDSTA 1185
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-------ALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1186 AQQELRSRREAELSELQRCVEEETRRHETQL---SELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSEL 1262
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 1263 KSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISS 1334
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1060-1934 |
4.39e-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: 58.70 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1060 DLEERLKREEQGR-LEQEKFKRRMESEAMEAQ------EQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQ 1132
Cdd:pfam12128 213 PPKSRLNRQQVEHwIRDIQAIAGIMKIRPEFTklqqefNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1133 RSLREALSQV--------SELKEEVENERGMRERAEKQ-RRDLSEELEALRTELEDtLDSTAAQQELRSRREAELSELQR 1203
Cdd:pfam12128 293 RTLDDQWKEKrdelngelSAADAAVAKDRSELEALEDQhGAFLDADIETAAADQEQ-LPSWQSELENLEERLKALTGKHQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1204 CVEEETRRHETQLSElrvKHSAALDSLQEQLDNSKRARqslEKAKATLEEERQNLTSELKS-LQASRSESERGRKRADNQ 1282
Cdd:pfam12128 372 DVTAKYNRRRSKIKE---QNNRDIAGIKDKLAKIREAR---DRQLAVAEDDLQALESELREqLEAGKLEFNEEEYRLKSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1283 LQELSARLAQADREREDREERMHKlQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRA 1362
Cdd:pfam12128 446 LGELKLRLNQATATPELLLQLENF-DERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1363 LEEeknglmerleeeeergkelsrQIQTHSQQLTE-LRKQseevnsAVEAGDEIRRKLQRELdsaiqreRQKEEEKERVE 1441
Cdd:pfam12128 525 LEL---------------------QLFPQAGTLLHfLRKE------APDWEQSIGKVISPEL-------LHRTDLDPEVW 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1442 RQRERLREEIEDMTIALQRERQNctalekrqkkfdQCLAEEKAVSARLAeerdraeadsreketrclALSRALQEAQDQK 1521
Cdd:pfam12128 571 DGSVGGELNLYGVKLDLKRIDVP------------EWAASEEELRERLD------------------KAEEALQSAREKQ 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1522 EELErankqlrlemEQLVNQQDDVGKNVHELERARRTLETEAQNLRiqtqeleeelseaensrlRLEVTLQALKAQFERE 1601
Cdd:pfam12128 621 AAAE----------EQLVQANGELEKASREETFARTALKNARLDLR------------------RLFDEKQSEKDKKNKA 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1602 ISTNEEKGEEKRRALSKQVRELEIQL--------EEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKqlRRLQ 1673
Cdd:pfam12128 673 LAERKDSANERLNSLEAQLKQLDKKHqawleeqkEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAK--AELK 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1674 GQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEK 1753
Cdd:pfam12128 751 ALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQL 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1754 RRLDARVNQLEEEleeeqtnneLLTERLRKTALQVEtLTVQLQGERTLAQKAeaAREQLEKQNKELKARLGEMEGAV--- 1830
Cdd:pfam12128 831 ARLIADTKLRRAK---------LEMERKASEKQQVR-LSENLRGLRCEMSKL--ATLKEDANSEQAQGSIGERLAQLedl 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1831 RGKHRMSVAALEAKIETMEEQLEQERQERAIANKL-MRKTEKKLKEVMMQAEDERRHAdQYREQLDKSMVR-----LKQL 1904
Cdd:pfam12128 899 KLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWEsLREEDHYQNDKGIRLLDYRKLV-PYLEQWFDVRVPqsimvLREQ 977
|
890 900 910
....*....|....*....|....*....|....*...
gi 1988774933 1905 KRQLEEVEEE--------NSRSSAQKRKLQRELEELTD 1934
Cdd:pfam12128 978 VSILGVDLTEfydvladfDRRIASFSRELQREVGEEAF 1015
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1643-1932 |
5.11e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1643 QLEAELQEAEAQVETANRGKEeAMKQLRRLQGQ-----MKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEE 1717
Cdd:COG1196 197 ELERQLEPLERQAEKAERYRE-LKEELKELEAEllllkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1718 LAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARvnqlEEELEEEQTNnelLTERLRKTALQVETLTVQLQG 1797
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER----LEELEEELAE---LEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1798 ERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKK----- 1872
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELeelee 428
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774933 1873 -LKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKLQRELEEL 1932
Cdd:COG1196 429 aLAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1054-1564 |
5.87e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1054 QEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLsdlgmlsselRGSLAQKEKEITSLQGRLEEEGARRAEAQR 1133
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEE----------LKEAEEKEEEYAELQEELEELEEELEELEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1134 SLREALSQVSELKEEVENERGMRER--AEKQRRDLSEELEALRTELEDTLDstaaQQELRSRREAELSELQrcveeetRR 1211
Cdd:COG4717 110 ELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQ-------EE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1212 HETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLqasrsESERGRKRADNQLQELSARLA 1291
Cdd:COG4717 179 LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL-----ENELEAAALEERLKEARLLLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1292 QADReredreermhklqceIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNgLM 1371
Cdd:COG4717 254 IAAA---------------LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE-LE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1372 ERLEEEEERGKELSRQIQTHsqQLTELRKQSEEVNSAVEAGDEIRRKLQREldsaiqrerqkeEEKERVERQRERLREEI 1451
Cdd:COG4717 318 EEELEELLAALGLPPDLSPE--ELLELLDRIEELQELLREAEELEEELQLE------------ELEQEIAALLAEAGVED 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1452 EDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKEtrclaLSRALQEAQDQKEELERANKQL 1531
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE-----LEEELEELEEELEELREELAEL 458
|
490 500 510
....*....|....*....|....*....|...
gi 1988774933 1532 RLEMEQLVNqQDDVGKNVHELERARRTLETEAQ 1564
Cdd:COG4717 459 EAELEQLEE-DGELAELLQELEELKAELRELAE 490
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
874-1364 |
1.76e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 874 EEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLgeletrl 953
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRD------- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 954 EEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEV 1033
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1034 TDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFkrRMESEAMEAQEQLSDlgmlsSELRGSLAQKEKE 1113
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL--LEAGKCPECGQPVEG-----SPHVETIEEDRER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1114 ITSLQGRLEEegarrAEAQRSLREAlsQVSELKEEVENERGMRERAEkqRRDLSEEleaLRTELEDTLDSTAAQQELRSR 1193
Cdd:PRK02224 477 VEELEAELED-----LEEEVEEVEE--RLERAEDLVEAEDRIERLEE--RREDLEE---LIAERRETIEEKRERAEELRE 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1194 REAELSElqrcvEEETRRHETQLSELRV-KHSAALDSLQEQLDNSKRARQSLEKAkATLEEERQNLTSELKSLQASRSE- 1271
Cdd:PRK02224 545 RAAELEA-----EAEEKREAAAEAEEEAeEAREEVAELNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREAl 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1272 SERGRKRADnQLQELSAR---LAQADREREDREERMHKLQCE--IESLSGNLSSSDSKSLRLAKEISSLESQLhDARELL 1346
Cdd:PRK02224 619 AELNDERRE-RLAEKRERkreLEAEFDEARIEEAREDKERAEeyLEQVEEKLDELREERDDLQAEIGAVENEL-EELEEL 696
|
490
....*....|....*...
gi 1988774933 1347 QDEsrqKMALASRVRALE 1364
Cdd:PRK02224 697 RER---REALENRVEALE 711
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1466-1950 |
2.05e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1466 TALEKRQKKFDQCLAEEKAVSARLAEERDRAE--ADSREKETRCLALSRALQEA-QDQKEELERANKQLRLEMEQLVNQQ 1542
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEelEEERDDLLAEAGLDDADAEAvEARREELEDRDEELRDRLEECRVAA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1543 DDVGKNVHELERARRTLETEAQNLRiqtqeleeelseaeNSRLRLEVTLQALKAQFEREISTNEEKgEEKRRALSKQVRE 1622
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELR--------------EEAAELESELEEAREAVEDRREEIEEL-EEEIEELRERFGD 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1623 LEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAmkqlRRLQ--GQMKEVLRELDDSKVTrdDVISqskDS 1700
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA----EALLeaGKCPECGQPVEGSPHV--ETIE---ED 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1701 EKKIQTLEAEVLHLTEELAVSErqkrqaqqERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNelltER 1780
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERA----EE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1781 LRKTALQVETltvQLQGERTLAQKAEAAREQLEKQNKELKARLGEmegavrgkhrmsvaaLEAKIETMEEQLEQERQERA 1860
Cdd:PRK02224 542 LRERAAELEA---EAEEKREAAAEAEEEAEEAREEVAELNSKLAE---------------LKERIESLERIRTLLAAIAD 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1861 IANKLMRKTEKklKEVMMQAEDERrhadqyREQLDKSMVRlkqlKRQLEEVEEENSRSSAQKRKLQRE---------LEE 1931
Cdd:PRK02224 604 AEDEIERLREK--REALAELNDER------RERLAEKRER----KRELEAEFDEARIEEAREDKERAEeyleqveekLDE 671
|
490
....*....|....*....
gi 1988774933 1932 LTDSSQTMNREISSLRNQL 1950
Cdd:PRK02224 672 LREERDDLQAEIGAVENEL 690
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
989-1189 |
2.29e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.78 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 989 QRLLLEKVTLETKVKSLETdlataveQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKRe 1068
Cdd:COG1579 6 LRALLDLQELDSELDRLEH-------RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1069 eqgrleqekfkrrmeseameAQEQLSDlgmlsselrgslAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEE 1148
Cdd:COG1579 78 --------------------YEEQLGN------------VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1988774933 1149 VENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQE 1189
Cdd:COG1579 126 LAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1224-1427 |
3.50e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1224 SAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREER 1303
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1304 MHKLQCEIESL------SGNLSS-----SDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLME 1372
Cdd:COG4942 99 LEAQKEELAELlralyrLGRQPPlalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774933 1373 RLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAI 1427
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1016-1422 |
4.73e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1016 RERLGKEKKQLE-ERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLK-REEQGRLEQEKFKRRMESEAMEAQEQL 1093
Cdd:COG4717 48 LERLEKEADELFkPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEElEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1094 SDLGMLSSELRGSLA----------QKEKEITSLQGRLEEEGARRAEAQRSLREAL--------SQVSELKEEVENERGM 1155
Cdd:COG4717 128 LPLYQELEALEAELAelperleeleERLEELRELEEELEELEAELAELQEELEELLeqlslateEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1156 RERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELS--------------------------------ELQR 1203
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1204 CVEEETRRHETQLSEL--RVKHSAALDSLQEQldNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADN 1281
Cdd:COG4717 288 LLFLLLAREKASLGKEaeELQALPALEELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1282 Q--LQELSARLAQAD-------REREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEIS--SLESQLHDARELLQDES 1350
Cdd:COG4717 366 EelEQEIAALLAEAGvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELE 445
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 1351 RQKMALASRVRALEEEKNGLMERLEEEEERgkelsRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRE 1422
Cdd:COG4717 446 EELEELREELAELEAELEQLEEDGELAELL-----QELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
868-1269 |
8.52e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 868 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLleekavlaDQLQAEAELFAEAEEMRARLASrkqeleevLG 947
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL--------EKLLQLLPLYQELEALEAELAE--------LP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 948 ELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEeesARQRLLLEKvtlETKVKSLETDLATAVEQRERLGKEKKQLE 1027
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEE---LLEQLSLAT---EEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1028 ERLNEVTDQLTEEEEKTKSLNKLKNKQEA------------------------------------VIADLEERLKREE-- 1069
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEArlllliaaallallglggsllsliltiagvlflvlgLLALLFLLLAREKas 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1070 --QGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKE 1147
Cdd:COG4717 300 lgKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1148 EVENERGMRERAE--KQRRDLSEELEALRTELEDTLDSTAAQQELRSRR--EAELSELQRCVEEETRRHETQLSELrvkh 1223
Cdd:COG4717 380 GVEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREEL---- 455
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1988774933 1224 sAALDSLQEQLDNSKRARQsLEKAKATLEEERQNLTSELKSLQASR 1269
Cdd:COG4717 456 -AELEAELEQLEEDGELAE-LLQELEELKAELRELAEEWAALKLAL 499
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1491-1934 |
1.25e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1491 EERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLvNQQDDVGKNVHELERARRTLETEAQNLRiQT 1570
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLE-EL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1571 QELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQE 1650
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1651 AEAQVETANrgKEEAMKQLRRLQGQMKEVLrelddSKVTRDDVISQSKDSEKKIQTLEAEVLHLteELAVSERQKRQAQQ 1730
Cdd:COG4717 232 LENELEAAA--LEERLKEARLLLLIAAALL-----ALLGLGGSLLSLILTIAGVLFLVLGLLAL--LFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1731 ERDEIADEmvssSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLtvqlqgertlaqKAEAARE 1810
Cdd:COG4717 303 EAEELQAL----PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL------------EEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1811 QLEKQNKELKARLG-EMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEvmmQAEDERRHADQ 1889
Cdd:COG4717 367 ELEQEIAALLAEAGvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE---ELEELEEELEE 443
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1988774933 1890 YREQLDKSMVRLKQLKRQLEEVEEENsRSSAQKRKLQRELEELTD 1934
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDG-ELAELLQELEELKAELRE 487
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1058-1247 |
1.38e-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: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1058 IADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLS--SELRGSLAQKEKEITSLQGRLEEegarraeaqrsL 1135
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeySWDEIDVASAEREIAELEAELER-----------L 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1136 REALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDS-TAAQQELRSRREAELSELQRCVEEetRRHET 1214
Cdd:COG4913 681 DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEElDELQDRLEAAEDLARLELRALLEE--RFAAA 758
|
170 180 190
....*....|....*....|....*....|....
gi 1988774933 1215 QLSELRVKHSAALDSLQEQLDNSK-RARQSLEKA 1247
Cdd:COG4913 759 LGDAVERELRENLEERIDALRARLnRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1507-1747 |
1.51e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1507 CLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLR 1586
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1587 LEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRELEiQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAM 1666
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFL-DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1667 KQLRRLQGQMKEVLRELDDSKVTRDDVISQskdSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGK 1746
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
.
gi 1988774933 1747 N 1747
Cdd:COG4942 251 L 251
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1458-1950 |
1.88e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1458 LQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKEtRCLALSRALQEAQDQKEELERANKQLRLEMEQ 1537
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1538 LVNQQDDVGKNVHELERARR---TLETEAQNLRIQTQELEEELSEAENSRLRLEvTLQALKAQFEREISTNEEKgEEKRR 1614
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKelkELKEKAEEYIKLSEFYEEYLDELREIEKRLS-RLEEEINGIEERIKELEEK-EERLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1615 ALSKQVRELEIQLEEeRSQRSQSVSSKKQLEAELQEAEAqvETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVI 1694
Cdd:PRK03918 342 ELKKKLKELEKRLEE-LEERHELYEEAKAKKEELERLKK--RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1695 SQSKDSEKKIQTLE--------------------------AEVLHLTEELAVSERQKRQAQQERDEIADEMVSSS--SGK 1746
Cdd:PRK03918 419 KEIKELKKAIEELKkakgkcpvcgrelteehrkelleeytAELKRIEKELKEIEEKERKLRKELRELEKVLKKESelIKL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1747 NVLSEEKRRLDARVNQLEEELEEEQTNN-ELLTERLRKTALQVETLTVQLQGERTLAQKaeaaREQLEKQNKELKARLGE 1825
Cdd:PRK03918 499 KELAEQLKELEEKLKKYNLEELEKKAEEyEKLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAE 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1826 MEGAVRGKHRMSVAALEAKIETMEEQLEQERQeraianklMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLK 1905
Cdd:PRK03918 575 LLKELEELGFESVEELEERLKELEPFYNEYLE--------LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELR 646
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774933 1906 RQLEEV-----EEENSRSSAQKRKLQRE-------LEELTDSSQTMNREISSLRNQL 1950
Cdd:PRK03918 647 KELEELekkysEEEYEELREEYLELSRElaglraeLEELEKRREEIKKTLEKLKEEL 703
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
867-1404 |
2.27e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.05 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 867 LQVTRQDEEIQTREAALQKAKEQLTRA-------EQDYTELDRKHAQLLEE------KAVLADQLQAEAELFAEAEEMRA 933
Cdd:TIGR00618 235 LQQTQQSHAYLTQKREAQEEQLKKQQLlkqlrarIEELRAQEAVLEETQERinrarkAAPLAAHIKAVTQIEQQAQRIHT 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 934 RLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQniQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAV 1013
Cdd:TIGR00618 315 ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ--EIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLT 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1014 EQRERLGKEKKQLEERLNEVTDQLTEE----------------EEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEK 1077
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATIDTRTSAFrdlqgqlahakkqqelQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKERE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1078 FK--------RRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEI---------TSLQGRLEEEGARRAEAQRSLR---- 1136
Cdd:TIGR00618 473 QQlqtkeqihLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnpgplTRRMQRGEQTYAQLETSEEDVYhqlt 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1137 EALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQqelrsrreaelSELQRCVEEETRRHETQL 1216
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL-----------SEAEDMLACEQHALLRKL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1217 SELRVKHSAALDSLQEQldnskrarQSLEKAKATLEEERQNLTSE--LKSLQASRSESERGRKRADNQLQELSARLAQAD 1294
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCS--------QELALKLTALHALQLTLTQErvREHALSIRVLPKELLASRQLALQKMQSEKEQLT 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1295 REREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQD-ESRQKMALASRV----RALEEEKNG 1369
Cdd:TIGR00618 694 YWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLKARTeahfNNNEEVTAA 773
|
570 580 590
....*....|....*....|....*....|....*..
gi 1988774933 1370 LMERLEEE--EERGKELSRQIQTHSQQLTELRKQSEE 1404
Cdd:TIGR00618 774 LQTGAELShlAAEIQFFNRLREEDTHLLKTLEAEIGQ 810
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1083-1293 |
2.58e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1083 ESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENER---GMRERA 1159
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReelGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1160 EKQRRDLSEELEAL--RTELEDTLDSTAAQQELRSRREAELSELQRcVEEETRRHETQLSELRVKHSAALDSLQEQLDNS 1237
Cdd:COG3883 95 LYRSGGSVSYLDVLlgSESFSDFLDRLSALSKIADADADLLEELKA-DKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774933 1238 KRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQA 1293
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1310-1829 |
2.69e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1310 EIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQ 1389
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1390 THSQQLTELRKQSEEVNSAVEAGDEIRR--KLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTA 1467
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEYIKlsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1468 LEKRQ---KKFDQCLAEEKAVSARLAEERDRAEADSREKetrclaLSRALQEAQDQKEELERANKQLRLEMEQLVNQQDD 1544
Cdd:PRK03918 350 LEKRLeelEERHELYEEAKAKKEELERLKKRLTGLTPEK------LEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1545 VGKNVHELERARRTLETeaqnlriqtqeleeelseaeNSRLRLEVTLQALKAQFEREISTNEE---KGEEKRRALSKQVR 1621
Cdd:PRK03918 424 LKKAIEELKKAKGKCPV--------------------CGRELTEEHRKELLEEYTAELKRIEKelkEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1622 ELEIQLEEERSQRSQSVSSK--KQLEAELQEAEAQ-VETANRGKEEAMKQLRRLQGQMKEVLRELDDSKvtrdDVISQSK 1698
Cdd:PRK03918 484 ELEKVLKKESELIKLKELAEqlKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE----ELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1699 DSEKKIQTLE---AEVLHLTEELAVSERQKRQAQ-QERDEIADEMVSSSSGKNVLSEEKRRLDA---RVNQLEEELEEEQ 1771
Cdd:PRK03918 560 ELEKKLDELEeelAELLKELEELGFESVEELEERlKELEPFYNEYLELKDAEKELEREEKELKKleeELDKAFEELAETE 639
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1772 TNNELLTERL------------RKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGA 1829
Cdd:PRK03918 640 KRLEELRKELeelekkyseeeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1338-1910 |
2.98e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1338 QLHDARELLQDESRQKMALAsRVRALEEEKNGLMERLEEEEERGKElsRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRR 1417
Cdd:COG4913 236 DLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1418 KLQRELDsaiqrerqkeeekerverqrerlreeiedmtiALQRERQNCTAlEKRQKKFDQclaeekavSARLAEERDRAE 1497
Cdd:COG4913 313 RLEARLD--------------------------------ALREELDELEA-QIRGNGGDR--------LEQLEREIERLE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1498 ADSREKETRCLALSRALQ----EAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRiqtqel 1573
Cdd:COG4913 352 RELEERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE------ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1574 eEELSEAENSRLRLEVTLQALKAQFEREISTNEE-----------KGEEKR-----------RALS--------KQVRE- 1622
Cdd:COG4913 426 -AEIASLERRKSNIPARLLALRDALAEALGLDEAelpfvgelievRPEEERwrgaiervlggFALTllvppehyAAALRw 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1623 ---------LEIQLEEERSQRSQSVSSKKQ----------------LEAELQEAE--AQVETanrgkEEAMKQLRR---L 1672
Cdd:COG4913 505 vnrlhlrgrLVYERVRTGLPDPERPRLDPDslagkldfkphpfrawLEAELGRRFdyVCVDS-----PEELRRHPRaitR 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1673 QGQMKE--VLRELDD-SKVTRDDVISQskDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEmvssssgKNVL 1749
Cdd:COG4913 580 AGQVKGngTRHEKDDrRRIRSRYVLGF--DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQER-------REAL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1750 SEEKRRLDARVNQLEEELEEEQTNNELltERLRKTALQVETLTVQLqgertlaQKAEAAREQLEKQNKELKARLGEmega 1829
Cdd:COG4913 651 QRLAEYSWDEIDVASAEREIAELEAEL--ERLDASSDDLAALEEQL-------EELEAELEELEEELDELKGEIGR---- 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1830 vrgkhrmsvaaLEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLE 1909
Cdd:COG4913 718 -----------LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAE 786
|
.
gi 1988774933 1910 E 1910
Cdd:COG4913 787 E 787
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1641-1956 |
3.06e-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: 52.38 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1641 KKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDdviSQSKDSEKKIQTLEAEVLHLTEELAV 1720
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKRE---YEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1721 SERQKRQAQQERDEIADEMVSSssgKNVLSEEKRRLDARVNQLEEEleeeqtnnelLTERLRKTALQVETLtvqlqgERT 1800
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEI---EQLLEELNKKIKDLGEEEQLR----------VKEKIGELEAEIASL------ERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1801 LAQKAEAArEQLEKQNKELKARLGEMEGAVRGkhrmsvaaLEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQA 1880
Cdd:TIGR02169 310 IAEKEREL-EDAEERLAKLEAEIDKLLAEIEE--------LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774933 1881 EDERRHADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLSFPEWR 1956
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1102-1538 |
3.53e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.26 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1102 ELRGSLAQKEKEITSLQGRLEE---EGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRrdlsEELEALRTELE 1178
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEmarELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQ----EDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1179 DTLDSTAAQQELRSRREAELSElqrcVEEETRRHETQLSELRvkhsAALDSLQEQLDNSKRARQSLEKAKATLEEERQNL 1258
Cdd:COG3096 365 EQEEVVEEAAEQLAEAEARLEA----AEEEVDSLKSQLADYQ----QALDVQQTRAIQYQQAVQALEKARALCGLPDLTP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1259 TSELKSLQASRSESERgrkrADNQLQELSARLAQADreredreerMHKLQCE-----IESLSGNLSSSDSKSlrlakeis 1333
Cdd:COG3096 437 ENAEDYLAAFRAKEQQ----ATEEVLELEQKLSVAD---------AARRQFEkayelVCKIAGEVERSQAWQ-------- 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1334 slesqlhDARELLQDESRQKmALASRVRALEeeknglmerleeeeergkelsrqiqthsQQLTELRKQSEEVNSAVEAGD 1413
Cdd:COG3096 496 -------TARELLRRYRSQQ-ALAQRLQQLR----------------------------AQLAELEQRLRQQQNAERLLE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1414 EIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMtIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEER 1493
Cdd:COG3096 540 EFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQR-SELRQQLEQLRARIKELAARAPAWLAAQDALERLREQS 618
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1988774933 1494 DRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQL 1538
Cdd:COG3096 619 GEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1480-1950 |
4.27e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1480 AEEKAVSARLAEERDRAEADSR-------EKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHEL 1552
Cdd:pfam05483 99 AELKQKENKLQENRKIIEAQRKaiqelqfENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYER 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1553 ERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTL-------QALKAQFEREISTNEekgeekrralsKQVRELEI 1625
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLkedhekiQHLEEEYKKEINDKE-----------KQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1626 QLEEERSQRSQSVSskkqLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKevlRELDDSKVTRDDVISQSKDSEKKIQ 1705
Cdd:pfam05483 248 QITEKENKMKDLTF----LLEESRDKANQLEEKTKLQDENLKELIEKKDHLT---KELEDIKMSLQRSMSTQKALEEDLQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1706 TLEAEVLHLTEELAVSERQKRQAQQERDEIADEM-VSSSSGKNVLSEEKRRLDarvnqleeeleEEQTNNELLTERLRKT 1784
Cdd:pfam05483 321 IATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFeATTCSLEELLRTEQQRLE-----------KNEDQLKIITMELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1785 ALQVETLT-------VQLQGERTLAQKAEA---AREQLEKQNKELKARLGEMEGAVRGKHRmSVAALEAKIETMEEQLEQ 1854
Cdd:pfam05483 390 SSELEEMTkfknnkeVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREK-EIHDLEIQLTAIKTSEEH 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1855 ERqeraianklmrkteKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKR-------QLEEVEEENSRSSAQKRKLQR 1927
Cdd:pfam05483 469 YL--------------KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQeasdmtlELKKHQEDIINCKKQEERMLK 534
|
490 500
....*....|....*....|...
gi 1988774933 1928 ELEELTDSSQTMNREISSLRNQL 1950
Cdd:pfam05483 535 QIENLEEKEMNLRDELESVREEF 557
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1512-1951 |
4.62e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1512 RALQEAQDQKEELE--RANKQLRLEMEQLVNQQDDVGK--NVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRL 1587
Cdd:COG4913 242 EALEDAREQIELLEpiRELAERYAAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1588 EVTLQALKAQ-----------FEREISTNEEKGEEKRRA---LSKQVRELEIQLEEErsqrsqsvssKKQLEAELQEAEA 1653
Cdd:COG4913 322 REELDELEAQirgnggdrleqLEREIERLERELEERERRrarLEALLAALGLPLPAS----------AEEFAALRAEAAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1654 QVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEvlhLTEELAVSERQKR------- 1726
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA---LAEALGLDEAELPfvgelie 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1727 -QAQQERDEIADEMVSSSSGKNVLSEEKRRLDA----------------RVNQLEEELEEEQTNNELLTERL-------- 1781
Cdd:COG4913 469 vRPEEERWRGAIERVLGGFALTLLVPPEHYAAAlrwvnrlhlrgrlvyeRVRTGLPDPERPRLDPDSLAGKLdfkphpfr 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1782 ---------RKTALQVE------------TLTVQLQGERTLAQK---------------AEAAREQLEKQNKELKARLge 1825
Cdd:COG4913 549 awleaelgrRFDYVCVDspeelrrhpraiTRAGQVKGNGTRHEKddrrrirsryvlgfdNRAKLAALEAELAELEEEL-- 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1826 megavrgkhrmsvAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKevMMQAEDERRHADQYREQLDKSMVRLKQLK 1905
Cdd:COG4913 627 -------------AEAEERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERLDASSDDLAALE 691
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1988774933 1906 RQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLS 1951
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
855-1370 |
5.02e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 855 QWWRLFTKVKPLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVL-----ADQLQAEAELFAEAE 929
Cdd:TIGR00618 383 TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELcaaaiTCTAQCEKLEKIHLQ 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 930 EMRARLASRKQeleevlgeletrleeeeergvQLANEKKKMQQNIQ-DLEEQLEEEESARQRLLLEKVTLETKVKSLETD 1008
Cdd:TIGR00618 463 ESAQSLKEREQ---------------------QLQTKEQIHLQETRkKAVVLARLLELQEEPCPLCGSCIHPNPARQDID 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1009 LATAVEQR-ERLGKEKKQLEERLNEVTDQLTEEeekTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAM 1087
Cdd:TIGR00618 522 NPGPLTRRmQRGEQTYAQLETSEEDVYHQLTSE---RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1088 EAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENE----RGMRERAEKQR 1163
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHalsiRVLPKELLASR 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1164 RDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQS 1243
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKA 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1244 LEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERmhkLQCEIESLSGNLSSSDS 1323
Cdd:TIGR00618 759 RTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLS 835
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1988774933 1324 KSLRLAKEISSLESQLHDARELLQdESRQKMALASRVRALEEEKNGL 1370
Cdd:TIGR00618 836 RLEEKSATLGEITHQLLKYEECSK-QLAQLTQEQAKIIQLSDKLNGI 881
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
872-1095 |
5.10e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 872 QDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEaeeMRARLASRKQELEEVLGELET 951
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA---LEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 952 RLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLN 1031
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774933 1032 EVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSD 1095
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1514-1932 |
8.34e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.11 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1514 LQEAQDQKEELERANKQLRLEMEQLVNQQDDVGknvhELERARRTLETEAQnlriqtqeleeelseAENSRLRLevTLQA 1593
Cdd:COG3096 284 SERALELRRELFGARRQLAEEQYRLVEMARELE----ELSARESDLEQDYQ---------------AASDHLNL--VQTA 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1594 LKAQfereistneEKGEEKRRALSkqvrELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRG---KEEAMKQLR 1670
Cdd:COG3096 343 LRQQ---------EKIERYQEDLE----ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQladYQQALDVQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1671 RLQGQMKEVLRELDDSK-------VTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSE---RQKRQAQQERDEIADEMV 1740
Cdd:COG3096 410 TRAIQYQQAVQALEKARalcglpdLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADaarRQFEKAYELVCKIAGEVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1741 SS---SSGKNVLsEEKRRLDARVNQLEEELEEEQTNNELLtERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNK 1817
Cdd:COG3096 490 RSqawQTARELL-RRYRSQQALAQRLQQLRAQLAELEQRL-RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLE 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1818 ELKARLGEmEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLmrktekklkevmmqaederrhADQYREQLDKS 1897
Cdd:COG3096 568 ELEEQAAE-AVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERL---------------------REQSGEALADS 625
|
410 420 430
....*....|....*....|....*....|....*...
gi 1988774933 1898 ---MVRLKQLKRQLEEVEEENSRSSAQKRKLQRELEEL 1932
Cdd:COG3096 626 qevTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
975-1286 |
9.78e-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: 50.28 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 975 QDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQ--------------LTEE 1040
Cdd:pfam07888 55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEkdallaqraahearIREL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1041 EEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGR 1120
Cdd:pfam07888 135 EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1121 LEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSE----------ELEALRTELEDT----LDSTAA 1186
Cdd:pfam07888 215 ITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrtqaELHQARLQAAQLtlqlADASLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1187 QQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAaldsLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQ 1266
Cdd:pfam07888 295 LREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEER----LQEERMEREKLEVELGREKDCNRVQLSESRRELQELK 370
|
330 340
....*....|....*....|
gi 1988774933 1267 ASRSESERGRKRADNQLQEL 1286
Cdd:pfam07888 371 ASLRVAQKEKEQLQAEKQEL 390
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1037-1285 |
1.05e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.51 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1037 LTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEK--------FKRRMESEAMEAQEQLSDLGMLSSELRGSLA 1108
Cdd:pfam17380 265 MTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKeekareveRRRKLEEAEKARQAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1109 QKEKEITSLqgRLEEegaRRAEAQRSLREALSQvsELKEEVENERGMRERAEKQRRdLSEELEALRTE--LEDTLDSTAA 1186
Cdd:pfam17380 345 ERERELERI--RQEE---RKRELERIRQEEIAM--EISRMRELERLQMERQQKNER-VRQELEAARKVkiLEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1187 QQ-----ELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKA---KATLEEERQN- 1257
Cdd:pfam17380 417 QQkvemeQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEkrdRKRAEEQRRKi 496
|
250 260
....*....|....*....|....*...
gi 1988774933 1258 LTSELKSLQASRSESERGRKRADNQLQE 1285
Cdd:pfam17380 497 LEKELEERKQAMIEEERKRKLLEKEMEE 524
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1141-1947 |
1.26e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.43 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1141 QVSELKEEVENERGMRERAEKQRRDLSE---ELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLS 1217
Cdd:TIGR00606 225 QITSKEAQLESSREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLN 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1218 ELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLA----QA 1293
Cdd:TIGR00606 305 DLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfER 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1294 DREREDREERMHKLQCEIESlsgnlsssdSKSLRLAKEISSLESQLHDARELLqDESRQKMALASRVRALEEEKnglMER 1373
Cdd:TIGR00606 385 GPFSERQIKNFHTLVIERQE---------DEAKTAAQLCADLQSKERLKQEQA-DEIRDEKKGLGRTIELKKEI---LEK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1374 LEEEEERGKELSRQIQTHSQQL----TELRKQSEEV-----NSAVEAGDEIRRKLQRE---LDSAIQRERQKEEEKERVE 1441
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRIleldQELRKAERELskaekNSLTETLKKEVKSLQNEkadLDRKLRKLDQEMEQLNHHT 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1442 RQRERLREEIEDMTIALQRERQNctalEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQK 1521
Cdd:TIGR00606 532 TTRTQMEMLTKDKMDKDEQIRKI----KSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNK 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1522 EELeraNKQLRLEMEQLVNQQD-------------DVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLE 1588
Cdd:TIGR00606 608 NHI---NNELESKEEQLSSYEDklfdvcgsqdeesDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQ 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1589 VTLQALKA--QFEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAM 1666
Cdd:TIGR00606 685 RVFQTEAElqEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1667 KQLRRLQGQMKEVLRELDDSKVTRDDVI------SQSKDSEKKIQTLEAEVlhLTEELAVSERQKRQAQQERDEIADEMV 1740
Cdd:TIGR00606 765 NDIEEQETLLGTIMPEEESAKVCLTDVTimerfqMELKDVERKIAQQAAKL--QGSDLDRTVQQVNQEKQEKQHELDTVV 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1741 SSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQgerTLAQKAEAAREQLEKQNKELK 1820
Cdd:TIGR00606 843 SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQ---SLIREIKDAKEQDSPLETFLE 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1821 ARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKL-------MRKTEKKLKEVMMQAEDERRHADQYREQ 1893
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIqdgkddyLKQKETELNTVNAQLEECEKHQEKINED 999
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1988774933 1894 LdksmvRLKQLKRQLEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLR 1947
Cdd:TIGR00606 1000 M-----RLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
868-1070 |
1.43e-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: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 868 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEaelfaeaeemRARLASRKQELEEVLG 947
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ----------KEELAELLRALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 948 ELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLE 1027
Cdd:COG4942 119 QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1988774933 1028 ERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQ 1070
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1073-1366 |
1.54e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.15 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1073 LEQEKfkRRMESEAMEAQEQLSdlgmlsSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENE 1152
Cdd:pfam00038 23 LEQQN--KLLETKISELRQKKG------AEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1153 RGMRERAEKQRRDLSEELEAL---RTELEDTLDSTaaQQELRSRR---EAELSELQRCVEEETRRHETQLSeLRVKHSAA 1226
Cdd:pfam00038 95 LNLRTSAENDLVGLRKDLDEAtlaRVDLEAKIESL--KEELAFLKknhEEEVRELQAQVSDTQVNVEMDAA-RKLDLTSA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1227 LDSLQEQLDN-SKRARQSLEKA-KATLEEERQNLTSELKSLQASRSESERGRKradnQLQELSARLAQADREREDREERM 1304
Cdd:pfam00038 172 LAEIRAQYEEiAAKNREEAEEWyQSKLEELQQAAARNGDALRSAKEEITELRR----TIQSLEIELQSLKKQKASLERQL 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 1305 HKLQceiESLSGNLSSSDSKslrlakeISSLESQLHDARELLQDESRQKMALASRVRALEEE 1366
Cdd:pfam00038 248 AETE---ERYELQLADYQEL-------ISELEAELQETRQEMARQLREYQELLNVKLALDIE 299
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1131-1350 |
1.73e-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: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1131 AQRSLREALSQVSELKEE---VENERGMRERAEKQRRDLSEE----LEAL---RTELEDTlDSTAAQQELRSRREAeLSE 1200
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQddaAQNALADKERAEADRQRLEQEkqqqLAAIsgsQSQLEST-DQNALETNGQAQRDA-ILE 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1201 LQRCVEEETRRHETQLSELRVKHSAA---------------LDSLQEQLDNSKR-ARQSLEKAKATLEEERQNLTSELKS 1264
Cdd:NF012221 1614 ESRAVTKELTTLAQGLDALDSQATYAgesgdqwrnpfagglLDRVQEQLDDAKKiSGKQLADAKQRHVDNQQKVKDAVAK 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1265 LQASRSESERGRKRADNQLQElsarlAQADREREDREERMHKLQCEIESLSGNLSSSDSKSlRLAKEISSLESQLH---- 1340
Cdd:NF012221 1694 SEAGVAQGEQNQANAEQDIDD-----AKADAEKRKDDALAKQNEAQQAESDANAAANDAQS-RGEQDASAAENKANqaqa 1767
|
250
....*....|
gi 1988774933 1341 DARELLQDES 1350
Cdd:NF012221 1768 DAKGAKQDES 1777
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1087-1262 |
2.39e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1087 MEAQEQLSDLGMLSSELRGSLAQKE---KEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQR 1163
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKelpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1164 RDLS--EELEALRTELEdtldstaAQQELRSRREAELSELqrcvEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRAR 1241
Cdd:COG1579 83 GNVRnnKEYEALQKEIE-------SLKRRISDLEDEILEL----MERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|.
gi 1988774933 1242 QSLEKAKATLEEERQNLTSEL 1262
Cdd:COG1579 152 AELEAELEELEAEREELAAKI 172
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
997-1180 |
2.56e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 997 TLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKS-LNKLKNKQEAVIADLEERLKREEQGRLEQ 1075
Cdd:PHA02562 185 TLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAeIEELTDELLNLVMDIEDPSAALNKLNTAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1076 EKFKRRMESEAMEAQ------------EQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARR---AEAQRSLREALS 1140
Cdd:PHA02562 265 AKIKSKIEQFQKVIKmyekggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMdefNEQSKKLLELKN 344
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1988774933 1141 QVSELKEEVENERGMR-------ERAEKQRRDLSEELEALRTELEDT 1180
Cdd:PHA02562 345 KISTNKQSLITLVDKAkkvkaaiEELQAEFVDNAEELAKLQDELDKI 391
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1480-1731 |
2.63e-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: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1480 AEEKAVSARLAEERDRAEADSREKETrclaLSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTL 1559
Cdd:pfam05667 226 WNSQGLASRLTPEEYRKRKRTKLLKR----IAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1560 ETE----AQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFErEISTNEEKGEEKRRALSKQVRELEIQLEEERSQRS 1635
Cdd:pfam05667 302 HTEklqfTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLE-DLESSIQELEKEIKKLESSIKQVEEELEELKEQNE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1636 QSVSS---KKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEV-------LRELDDSKVTRDDVISQSKDsekKIQ 1705
Cdd:pfam05667 381 ELEKQykvKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHrvplieeYRALKEAKSNKEDESQRKLE---EIK 457
|
250 260
....*....|....*....|....*.
gi 1988774933 1706 TLEAEVLHLTEELAVSERQKRQAQQE 1731
Cdd:pfam05667 458 ELREKIKEVAEEAKQKEELYKQLVAE 483
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1592-1823 |
2.69e-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: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1592 QALKAQFEREISTNEEKGEEKRRALS---KQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQ 1668
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAalkKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1669 LRRLQGQMKEVLRELDD-SKVTRDDVISQSKD---SEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSS 1744
Cdd:COG4942 99 LEAQKEELAELLRALYRlGRQPPLALLLSPEDfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774933 1745 GKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLqgERTLAQKAEAAREQLEKQNKELKARL 1823
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI--ARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1023-1292 |
2.93e-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: 49.19 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1023 KKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQgrleqekfKRRMESEAMEAQEQLSdlgmlSSE 1102
Cdd:COG5185 256 EKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTK--------SIDIKKATESLEEQLA-----AAE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1103 LRGSLAQKEKEITSLQGRLEEEGARRaeaQRSLREALSQVSELKEEVENERGMRERAEKQrRDLSEELEALRTEL-EDTL 1181
Cdd:COG5185 323 AEQELEESKRETETGIQNLTAEIEQG---QESLTENLEAIKEEIENIVGEVELSKSSEEL-DSFKDTIESTKESLdEIPQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1182 DSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKhSAALDSLQEQLDnsKRARQSLEKAKATLEEERQNLTSE 1261
Cdd:COG5185 399 NQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEV-SKLLNELISELN--KVMREADEESQSRLEEAYDEINRS 475
|
250 260 270
....*....|....*....|....*....|.
gi 1988774933 1262 LKSlqaSRSESERGRKRADNQLQELSARLAQ 1292
Cdd:COG5185 476 VRS---KKEDLNEELTQIESRVSTLKATLEK 503
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1679-1951 |
3.10e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1679 VLRELDDSKVTRDDVISQ-----SKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEiADEMVSSSSGKNvlsEEK 1753
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQieekeEKDLHERLNGLESELAELDEEIERYEEQREQARETRDE-ADEVLEEHEERR---EEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1754 RRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRgK 1833
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLE-E 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1834 HRMSVAALEAKIETMEEQLeqerqeraianklmRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEE 1913
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDA--------------DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270
....*....|....*....|....*....|....*...
gi 1988774933 1914 ENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLS 1951
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1106-1338 |
3.33e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1106 SLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVEnergmreRAEKQRRDLSEELEALRTELEdtldstA 1185
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-------ELQAELEALQAEIDKLQAEIA------E 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1186 AQQELRSRREaELSELQRcVEEETRRHETQLSELRVKHSAA-----LDSLQEQLDNSKRARQSLEKAKATLEEERQNLTS 1260
Cdd:COG3883 77 AEAEIEERRE-ELGERAR-ALYRSGGSVSYLDVLLGSESFSdfldrLSALSKIADADADLLEELKADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774933 1261 ELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQ 1338
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1116-1356 |
4.02e-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: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1116 SLQGRLEEEGARRAEAQRSLREALSQvseLKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRRE 1195
Cdd:pfam05667 230 GLASRLTPEEYRKRKRTKLLKRIAEQ---LRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1196 AELSELQRCVEEETRRHETQlSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERG 1275
Cdd:pfam05667 307 QFTNEAPAATSSPPTKVETE-EELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1276 RKR----------ADNQLQELSARLAQADREREDREERMHK----LQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHD 1341
Cdd:pfam05667 386 YKVkkktldllpdAEENIAKLQALVDASAQRLVELAGQWEKhrvpLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKE 465
|
250
....*....|....*
gi 1988774933 1342 ArellQDESRQKMAL 1356
Cdd:pfam05667 466 V----AEEAKQKEEL 476
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1658-1875 |
4.05e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1658 ANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKI-------QTLEAEVLHLTEELAVSERQKRQAQQ 1730
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIaalarriRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1731 ERDEIADEMvssSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAARE 1810
Cdd:COG4942 98 ELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774933 1811 QLEKQNKELKARLGEMEGAVRGKHRMsVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKE 1875
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKL-LARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
962-1149 |
4.53e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 962 QLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQL---- 1037
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaell 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1038 ---------------------TEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDL 1096
Cdd:COG4942 111 ralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1988774933 1097 GMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEV 1149
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
986-1287 |
5.40e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 48.39 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 986 SARQRLLLEKVTLETKvKSLETDLATAVEQRERlGKEKKQLEERLnevtdQLTEEEEKTKSL-NKLKNKQEAVIAdLEER 1064
Cdd:PLN03188 1012 SARKRNSLLKLTYSCE-PSQAPPLNTIPESTDE-SPEKKLEQERL-----RWTEAESKWISLaEELRTELDASRA-LAEK 1083
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1065 LKREeqgrLEQEKFKRRMESEAMEAQ--------EQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAqRSLR 1136
Cdd:PLN03188 1084 QKHE----LDTEKRCAEELKEAMQMAmegharmlEQYADLEEKHIQLLARHRRIQEGIDDVKKAAARAGVRGAES-KFIN 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1137 EALSQVSELKEEvenergmrerAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSR-REAE--LSELQRC---VEEETR 1210
Cdd:PLN03188 1159 ALAAEISALKVE----------REKERRYLRDENKSLQAQLRDTAEAVQAAGELLVRlKEAEeaLTVAQKRamdAEQEAA 1228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774933 1211 RHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSEL-KSLQASRSESERGRKRADNQLQELS 1287
Cdd:PLN03188 1229 EAYKQIDKLKRKHENEISTLNQLVAESRLPKEAIRPACNDDCMAKYDAGEPLsEGDQQWREEFEPFYKKEDGELSKLA 1306
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
887-1552 |
5.76e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.30 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 887 KEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEemrARLASRKQELEEVLGELETRLEEEEERGVQLANE 966
Cdd:pfam12128 215 KSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAE---LRLSHLHFGYKSDETLIASRQEERQETSAELNQL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 967 KKKMQQNIQDLeeqleeeesaRQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEK----KQLEERLNEVTDQLTEEEE 1042
Cdd:pfam12128 292 LRTLDDQWKEK----------RDELNGELSAADAAVAKDRSELEALEDQHGAFLDADietaAADQEQLPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1043 KTKSL----NKLKNKQEAVIADLEERLKREEQGrLEQEKFKRRmESEAMEAQEQLSDLGMLSSELRGSLAQKEKEItslq 1118
Cdd:pfam12128 362 RLKALtgkhQDVTAKYNRRRSKIKEQNNRDIAG-IKDKLAKIR-EARDRQLAVAEDDLQALESELREQLEAGKLEF---- 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1119 grlEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRrdlsEELEALRTELEDTLDSTAAqqeLRSRREAEL 1198
Cdd:pfam12128 436 ---NEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAR----EEQEAANAEVERLQSELRQ---ARKRRDQAS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1199 SELQRCvEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRA-RQSLEKAKATLEEERQNLTSELKSLQASRSESERGRK 1277
Cdd:pfam12128 506 EALRQA-SRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDwEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1278 RADNQL---------QELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDskslrlaKEISSLESQLHDARELLQD 1348
Cdd:pfam12128 585 LDLKRIdvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS-------REETFARTALKNARLDLRR 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1349 ESRQKMALASRV-RALEEEKNGLMERLEEEEERGKELSRQIQTHSQ----QLTELRKQSEEVNSAVE-AGDEIRRKLQRE 1422
Cdd:pfam12128 658 LFDEKQSEKDKKnKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeqkeQKREARTEKQAYWQVVEgALDAQLALLKAA 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1423 LDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAE-EKAVSARLAEERDRAEADSR 1501
Cdd:pfam12128 738 IAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRyFDWYQETWLQRRPRLATQLS 817
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1988774933 1502 EKETrclALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHEL 1552
Cdd:pfam12128 818 NIER---AISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGL 865
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1043-1198 |
5.82e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.65 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1043 KTKSLNKLkNKQeavIADLEERLKREEQGrleqekfkrrmeSEAMEAQeqlsdlgmlSSELRGSLAQKEKEITSLQGRLE 1122
Cdd:PRK09039 51 KDSALDRL-NSQ---IAELADLLSLERQG------------NQDLQDS---------VANLRASLSAAEAERSRLQALLA 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774933 1123 EEGARRAEAQRslrealsQVSELKEEVENERGMRERAEKQRRDLSEELEALRTEL---EDTLDSTAAQQELRSRREAEL 1198
Cdd:PRK09039 106 ELAGAGAAAEG-------RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLaalEAALDASEKRDRESQAKIADL 177
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1150-1408 |
5.85e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1150 ENERGMRERAEKQRRDLSEELEALRTELEdtldstAAQQELRS-RREAELSELqrcvEEETRRHETQLSELRvkhsAALD 1228
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELE------EAEAALEEfRQKNGLVDL----SEEAKLLLQQLSELE----SQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1229 SLQEQLDNSKRARQSLEKAKATLEEERQNLTselkslqasrsesergrkrADNQLQELSARLAQADReredreermhklq 1308
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPELL-------------------QSPVIQQLRAQLAELEA------------- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1309 cEIESLSGNLSSSDSKSLRLAKEISSLESQLHD-ARELLQDESRQKMALASRVRALEEEKNGL---MERLEEEEERGKEL 1384
Cdd:COG3206 278 -ELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLearLAELPELEAELRRL 356
|
250 260
....*....|....*....|....
gi 1988774933 1385 SRQIQTHSQQLTELRKQSEEVNSA 1408
Cdd:COG3206 357 EREVEVARELYESLLQRLEEARLA 380
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1718-1951 |
6.58e-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: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1718 LAVSERQKRQAQQERDEiademvssssgknvLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQLQG 1797
Cdd:COG4942 15 AAAQADAAAEAEAELEQ--------------LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1798 ERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIaNKLMRKTEKKLKEVM 1877
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774933 1878 MQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEEN----SRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLS 1951
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERqkllARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1468-1954 |
7.11e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1468 LEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERAN-KQLRLEMEQLVNQQDDVG 1546
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHqRTVREKERELVDCQRELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1547 KNVHEL-ERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFERE----------ISTNEEKGEEKRRA 1615
Cdd:TIGR00606 330 KLNKERrLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpfserqiknfHTLVIERQEDEAKT 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1616 LSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLREldDSKVTRDDVIS 1695
Cdd:TIGR00606 410 AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL--DQELRKAEREL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1696 QSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADE------MVSSSSGKNVLSEEKRRLDARVNQLEEELEE 1769
Cdd:TIGR00606 488 SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHtttrtqMEMLTKDKMDKDEQIRKIKSRHSDELTSLLG 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1770 EQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAV------------------- 1830
Cdd:TIGR00606 568 YFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsqdeesdlerlkee 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1831 ---RGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKsmvRLKQLKRQ 1907
Cdd:TIGR00606 648 iekSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTES---ELKKKEKR 724
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1988774933 1908 LEEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLSFPE 1954
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE 771
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
875-1696 |
7.48e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 875 EIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGELETRLE 954
Cdd:TIGR00606 313 TVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 955 EEEERGV--QLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNE 1032
Cdd:TIGR00606 393 KNFHTLVieRQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1033 VtdqLTEEEEKTKSLNKLKNKQEAviADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDlgmlsSELRGSLAQKEK 1112
Cdd:TIGR00606 473 I---LELDQELRKAERELSKAEKN--SLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH-----TTTRTQMEMLTK 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1113 EITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRS 1192
Cdd:TIGR00606 543 DKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLS 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1193 RREAELSELQRCVEEETRrhetqlselrvkhsaaLDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSES 1272
Cdd:TIGR00606 623 SYEDKLFDVCGSQDEESD----------------LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRV 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1273 ERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLH----DARELLQD 1348
Cdd:TIGR00606 687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQkvnrDIQRLKND 766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1349 ESRQKMALASRVRALEEEKN-----GLMERLEEEEERGKELSRQIQTHSQQlTELRKQSEEVNSAVEAGDEIRRKLQREL 1423
Cdd:TIGR00606 767 IEEQETLLGTIMPEEESAKVcltdvTIMERFQMELKDVERKIAQQAAKLQG-SDLDRTVQQVNQEKQEKQHELDTVVSKI 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1424 DSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREK 1503
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1504 ETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDD---------------VGKNVHELERARRTLETEAQNLR- 1567
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgkddylkqketelntVNAQLEECEKHQEKINEDMRLMRq 1005
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1568 -IQTQELEEELSEAENSRLRLEVTLQALK---AQFEREIstNEEKGEEKRRALSKQVRELE-IQLEEERSQRSQSVSSKK 1642
Cdd:TIGR00606 1006 dIDTQKIQERWLQDNLTLRKRENELKEVEeelKQHLKEM--GQMQVLQMKQEHQKLEENIDlIKRNHVLALGRQKGYEKE 1083
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1988774933 1643 QLEAELQEAEAQVETANRGKEEAMKQLRrlqgQMKEVLRELDDSKVTRDDVISQ 1696
Cdd:TIGR00606 1084 IKHFKKELREPQFRDAEEKYREMMIVMR----TTELVNKDLDIYYKTLDQAIMK 1133
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
987-1150 |
7.82e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 987 ARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKtksLNKLKNKQEAVIADLEERLK 1066
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNVRNNKEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1067 REEQGRLEQEkfkrrmESEAMEAQEqlsdlgmlssELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELK 1146
Cdd:COG1579 102 KRRISDLEDE------ILELMERIE----------ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....
gi 1988774933 1147 EEVE 1150
Cdd:COG1579 166 EELA 169
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1011-1366 |
7.97e-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: 47.89 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1011 TAVEQRER-LGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKfkrRMESeameA 1089
Cdd:pfam10174 334 TAKEQRAAiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQK---KIEN----L 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1090 QEQLSDlgmlsselrgslaqKEKEITSLQGR---LEEEGARRAEAQRSLREALSqvsELKEEVENERGMRERAEKQRRdl 1166
Cdd:pfam10174 407 QEQLRD--------------KDKQLAGLKERvksLQTDSSNTDTALTTLEEALS---EKERIIERLKEQREREDRERL-- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1167 sEELEALRTELEDTLDSTAAQQELRSRREAELSELQrcveeetrRHETQLSELRVKHSAALDSL----QEQLDNSKRARQ 1242
Cdd:pfam10174 468 -EELESLKKENKDLKEKVSALQPELTEKESSLIDLK--------EHASSLASSGLKKDSKLKSLeiavEQKKEECSKLEN 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1243 SLEKAKATLEEERQN--LTSELKSLqasrsESERGRKRAD-NQLQELSARLAQADREREDREERMHKLQCEIESLSGNLS 1319
Cdd:pfam10174 539 QLKKAHNAEEAVRTNpeINDRIRLL-----EQEVARYKEEsGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQM 613
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1988774933 1320 SSDSKSLRLAKEISSLESQlhDARELLQDESRQKMALASRVRALEEE 1366
Cdd:pfam10174 614 KEQNKKVANIKHGQQEMKK--KGAQLLEEARRREDNLADNSQQLQLE 658
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
999-1273 |
8.52e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 47.44 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 999 ETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEK--TKSLNKLKNKQEAVIADLEERLK-------REE 1069
Cdd:pfam09731 160 KAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQseEEAAPPLLDAAPETPPKLPEHLDnveekveKAQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1070 QGRLEQEKFKRRMESEAMEAQEQLS------------DLGMLSSELRGSLAQKEKEITSLQGRL------EEEGARRA-- 1129
Cdd:pfam09731 240 SLAKLVDQYKELVASERIVFQQELVsifpdiipvlkeDNLLSNDDLNSLIAHAHREIDQLSKKLaelkkrEEKHIERAle 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1130 ---EAQRSLREALSQ-------VSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAeLS 1199
Cdd:pfam09731 320 kqkEELDKLAEELSArleevraADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREF-LQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1200 ELQRCVEEETRRHETQLSEL--RVKH-SAALDSLQEQLDNSKRARQ---SLEKAKATLE-----EERQNLTSELKSLQAS 1268
Cdd:pfam09731 399 DIKEKVEEERAGRLLKLNELlaNLKGlEKATSSHSEVEDENRKAQQlwlAVEALRSTLEdgsadSRPRPLVRELKALKEL 478
|
....*
gi 1988774933 1269 RSESE 1273
Cdd:pfam09731 479 ASDDE 483
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
679-703 |
8.68e-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: 8.68e-05
10 20
....*....|....*....|....*
gi 1988774933 679 YKESLTKLMATLRNTNPNFLRCIIP 703
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1000-1339 |
9.06e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1000 TKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEqgrleqekfk 1079
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK---------- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1080 rrmeseamEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEegarraeAQRSLREALSQVSELKEEVENERGMRERA 1159
Cdd:TIGR04523 215 --------SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN-------TQTQLNQLKDEQNKIKKQLSEKQKELEQN 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1160 EKQRRDLSEELEALRTELEDTldSTAAQQELRSRREAELSELQRCVEE---ETRRHETQLSELR---------VKHSAAL 1227
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDL--NNQKEQDWNKELKSELKNQEKKLEEiqnQISQNNKIISQLNeqisqlkkeLTNSESE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1228 DS-LQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHK 1306
Cdd:TIGR04523 358 NSeKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
330 340 350
....*....|....*....|....*....|...
gi 1988774933 1307 LQCEIESLSGNLSSSDSKSLRLAKEISSLESQL 1339
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1038-1293 |
9.77e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1038 TEEEEKTKSLNKLKNKQEAVIADLEErlkreeqgrleqekfkrrMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSL 1117
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDA------------------LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1118 QGRLEEEGARRAEAQRSLREALSQVSELK--------EEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQE 1189
Cdd:COG3883 78 EAEIEERREELGERARALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1190 LRSRREAELSELQRCVEEETRRHETQLSELrvkhSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASR 1269
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQL----SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
250 260
....*....|....*....|....
gi 1988774933 1270 SESERGRKRADNQLQELSARLAQA 1293
Cdd:COG3883 234 AAAAAAAAAAASAAGAGAAGAAGA 257
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
962-1271 |
1.29e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 962 QLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEvTDQLTEEE 1041
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE-GDHLRNVQ 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1042 EKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRL 1121
Cdd:pfam15921 548 TECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1122 EEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALR-------TELEDTLDS-----TAAQQE 1189
Cdd:pfam15921 628 SDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKrnfrnksEEMETTTNKlkmqlKSAQSE 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1190 LRSRREAELSelqrcvEEETRRHETQLSELRVKHSAA----LDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSL 1265
Cdd:pfam15921 708 LEQTRNTLKS------MEGSDGHAMKVAMGMQKQITAkrgqIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTV 781
|
....*.
gi 1988774933 1266 QASRSE 1271
Cdd:pfam15921 782 ATEKNK 787
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
998-1293 |
1.61e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 998 LETKVKSLETDLATA---VEQRERLGKEKKQLEERLNEVTDQLTEeeeKTKSLNKLKNKQEAVIAdleERLKREEQGRLE 1074
Cdd:PRK11281 54 LEAEDKLVQQDLEQTlalLDKIDRQKEETEQLKQQLAQAPAKLRQ---AQAELEALKDDNDEETR---ETLSTLSLRQLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1075 QEKFKRRmeSEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEegarraeaqrsLREALSQVSELKEEVENERG 1154
Cdd:PRK11281 128 SRLAQTL--DQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ-----------IRNLLKGGKVGGKALRPSQR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1155 MRERAEKQRRDLSEELEalRTELEdtlDSTAAQQELRSRREaELSELQRCVEeetrrHETQLselrvkhsaaldsLQEQL 1234
Cdd:PRK11281 195 VLLQAEQALLNAQNDLQ--RKSLE---GNTQLQDLLQKQRD-YLTARIQRLE-----HQLQL-------------LQEAI 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774933 1235 dNSKRARQSLEKAKatlEEERQNLTSELKSLQASRSESERGRKradnqlqeLSARLAQA 1293
Cdd:PRK11281 251 -NSKRLTLSEKTVQ---EAQSQDEAARIQANPLVAQELEINLQ--------LSQRLLKA 297
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1543-1738 |
1.66e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1543 DDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENsRLRLEVtLQALKAQFEREistneeKGEEKRRALSKQVRE 1622
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAA-RERLAE-LEYLRAALRLW------FAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1623 LEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMK-QLRRLQGQMKEVLRELDD-----------SKVTR 1690
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLErEIERLERELEERERRRARleallaalglpLPASA 379
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1988774933 1691 DDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADE 1738
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1586-1956 |
1.72e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1586 RLEVTLQALKAQFE--REISTNEEKGEEKRRALSKQVRELEIQLE--EERSQRSQSVSSKKQLEAELQEAEAQVETAnrg 1661
Cdd:COG4717 75 ELEEELKEAEEKEEeyAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEEL--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1662 kEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQ-SKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMV 1740
Cdd:COG4717 152 -EERLEELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1741 SSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLTERLRKTALQVETLTVQL--------QGERTLAQKAEAAREQL 1812
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLlallflllAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1813 EKQNKELKARLGEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKK-----LKEVMMQAEDERRHA 1887
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeiaalLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1888 DQYREQLDKSMVRLKQLKRQL----------------EEVEEENSRSSAQKRKLQRELEELTDSSQTMNREISSLRNQLS 1951
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLeellgeleellealdeEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
....*
gi 1988774933 1952 FPEWR 1956
Cdd:COG4717 471 LAELL 475
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1232-1950 |
1.74e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.89 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1232 EQLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASrsesergrkradnqLQELSARLAQADREREDREERMHKLQCEI 1311
Cdd:TIGR00618 184 MEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHER--------------KQVLEKELKHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1312 ESLSGNLSSSD--SKSLRLAKEISSLESQLHDARELLqDESRQKMALASRVRALEE---EKNGLMERLEEEEERGKELSR 1386
Cdd:TIGR00618 250 EAQEEQLKKQQllKQLRARIEELRAQEAVLEETQERI-NRARKAAPLAAHIKAVTQieqQAQRIHTELQSKMRSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1387 QIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELdsaiqrerQKEEEKERVERQRERLREEIEDMTIALQRERQNCT 1466
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT--------SIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1467 ALEK---RQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQd 1543
Cdd:TIGR00618 401 ELDIlqrEQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE- 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1544 dvgkNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEEKGEEKRR------ALS 1617
Cdd:TIGR00618 480 ----QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDvyhqltSER 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1618 KQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDsKVTRDDVISQS 1697
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP-EQDLQDVRLHL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1698 KDSEKKIQTLEAEVLHLTEELAvserQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELL 1777
Cdd:TIGR00618 635 QQCSQELALKLTALHALQLTLT----QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1778 TERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAALEAKIEtmeeqLEQERQ 1857
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE-----LSHLAA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1858 ERAIANKLMRKTEKKLKEVMMQAEDERRHADQYRE-QLDKSMVRLKQLKRQLEEveeeNSRSSAQKRKLQRELEELTDSS 1936
Cdd:TIGR00618 786 EIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLEE----KSATLGEITHQLLKYEECSKQL 861
|
730
....*....|....
gi 1988774933 1937 QTMNREISSLRNQL 1950
Cdd:TIGR00618 862 AQLTQEQAKIIQLS 875
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1012-1329 |
1.90e-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: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1012 AVEQRERLGKEKKQL---EERLNEVTDQLTEEEEKTKSL-----------NKLKN---KQEAV------IADLEERLkrE 1068
Cdd:COG3096 287 ALELRRELFGARRQLaeeQYRLVEMARELEELSARESDLeqdyqaasdhlNLVQTalrQQEKIeryqedLEELTERL--E 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1069 EQG---------RLEQEKFKRRMESEAMEAQEQLSD----LGMLSS-------------ELRGSLAQKEKEITSLQGRLE 1122
Cdd:COG3096 365 EQEevveeaaeqLAEAEARLEAAEEEVDSLKSQLADyqqaLDVQQTraiqyqqavqaleKARALCGLPDLTPENAEDYLA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1123 EEGARRAEAQRSLREALSQVSELKEEV-ENERGM-----------RERAEKQRRDL----------SEELEALRTELEDt 1180
Cdd:COG3096 445 AFRAKEQQATEEVLELEQKLSVADAARrQFEKAYelvckiageveRSQAWQTARELlrryrsqqalAQRLQQLRAQLAE- 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1181 ldstaAQQELRSRREAE--LSELQRCVEEEtRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNL 1258
Cdd:COG3096 524 -----LEQRLRQQQNAErlLEEFCQRIGQQ-LDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKEL 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1259 TSE----------LKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRL 1328
Cdd:COG3096 598 AARapawlaaqdaLERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRLLAL 677
|
.
gi 1988774933 1329 A 1329
Cdd:COG3096 678 A 678
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
963-1724 |
2.09e-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: 46.65 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 963 LANEKKKMQQNIQDLeeqleeeesarqrllleKVTLETKVKSLETdlataveqrerlgkeKKQLEErlnevtDQLTEEEE 1042
Cdd:pfam15921 129 MADIRRRESQSQEDL-----------------RNQLQNTVHELEA---------------AKCLKE------DMLEDSNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1043 KTKSLNKLKNKQEAVIADLEERLKreeqgRLEQEKFKRRMESEAMEAQEQLSdlgmLSSELRGSLAQKEKEITSLQGRL- 1121
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSILV-----DFEEASGKKIYEHDSMSTMHFRS----LGSAISKILRELDTEISYLKGRIf 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1122 ---EEEGARRAEAQRSLREALSQVSELKEEVENER-----GMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSR 1193
Cdd:pfam15921 242 pveDQLEALKSESQNKIELLLQQHQDRIEQLISEHeveitGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1194 REAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEqldnSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESE 1273
Cdd:pfam15921 322 LESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTE----ARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1274 RGRKR-----------ADNQLQELSARLAQADREREDREERMHKLQCEIESlsgNLSSSDSKSLRLAKeISSLESQLHDA 1342
Cdd:pfam15921 398 EQNKRlwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMER---QMAAIQGKNESLEK-VSSLTAQLEST 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1343 RELL----QDESRQKMALASRVRALEEEKNGLmerleeeeergKELSRQIQTHSQQLTELRKQS----EEVNSAVEAGDE 1414
Cdd:pfam15921 474 KEMLrkvvEELTAKKMTLESSERTVSDLTASL-----------QEKERAIEATNAEITKLRSRVdlklQELQHLKNEGDH 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1415 IrRKLQRELDSaiqrerqKEEEKERVERQRERLREEIEDMTIALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERD 1494
Cdd:pfam15921 543 L-RNVQTECEA-------LKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKD 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1495 RAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQ----QDDVGKNVHELERARRTLETEAQNLRIQT 1570
Cdd:pfam15921 615 KKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEvktsRNELNSLSEDYEVLKRNFRNKSEEMETTT 694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1571 QELEEELSEAENSRLRLEVTLQALKAQ--FEREISTNEEKGEEKRRAlskQVRELEIQLEEERSQRSQSVSSKKQLEAEL 1648
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTLKSMEGSdgHAMKVAMGMQKQITAKRG---QIDALQSKIQFLEEAMTNANKEKHFLKEEK 771
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774933 1649 QEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEV--LHLTEELAVSERQ 1724
Cdd:pfam15921 772 NKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESvrLKLQHTLDVKELQ 849
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1012-1285 |
2.13e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.01 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1012 AVEQRERLgkekKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQgRLEQEKFKRRMESE------ 1085
Cdd:pfam02029 15 AREERRRQ----KEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTA-KREERRQKRLQEALerqkef 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1086 ---AMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGAR---RAEAQRSLREALSQVSELKEEVENERGMRERA 1159
Cdd:pfam02029 90 dptIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEireKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1160 EKQR-RDLSEELEALRTELEDTLDSTAAQQELRSRRE-----AELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQ 1233
Cdd:pfam02029 170 PTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEvksqnGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQK 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 1234 LDNSKRARQSLEKAKAT-LEEERQNLTSELKSLQASR-------SESERGRK--RADNQLQE 1285
Cdd:pfam02029 250 LEELRRRRQEKESEEFEkLRQKQQEAELELEELKKKReerrkllEEEEQRRKqeEAERKLRE 311
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
868-1673 |
2.31e-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: 46.58 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 868 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLleeKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLG 947
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEI---KALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 948 ELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLE 1027
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1028 ERL--NEVTDQLTEEEEKTKSLNKLKNKQEAviadlEERLKREEQGRLEQEK--FKRRMESEAMEAQEQLSDLGMLSSEL 1103
Cdd:TIGR00606 389 ERQikNFHTLVIERQEDEAKTAAQLCADLQS-----KERLKQEQADEIRDEKkgLGRTIELKKEILEKKQEELKFVIKEL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1104 RgSLAQKEKEITSLqgrleEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEdtlds 1183
Cdd:TIGR00606 464 Q-QLEGSSDRILEL-----DQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTT----- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1184 TAAQQELRSRREAELSElqrcveeetrrhetQLSELRVKHSAALDSLQEQLDNSKRARQ---SLEKAKATLEEERQNLTS 1260
Cdd:TIGR00606 533 TRTQMEMLTKDKMDKDE--------------QIRKIKSRHSDELTSLLGYFPNKKQLEDwlhSKSKEINQTRDRLAKLNK 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1261 ELKSLQASRSESERGRKRADNQLQELSARLAQAdREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLH 1340
Cdd:TIGR00606 599 ELASLEQNKNHINNELESKEEQLSSYEDKLFDV-CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQ 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1341 DARELLQDESRQKMALASRVRALEeekNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQ 1420
Cdd:TIGR00606 678 SCCPVCQRVFQTEAELQEFISDLQ---SKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1421 ---RELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRERQnctaLEKRQKKFDQCLAEEKAVSARLAEERDRAE 1497
Cdd:TIGR00606 755 kvnRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQME----LKDVERKIAQQAAKLQGSDLDRTVQQVNQE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1498 ADSREKETRclALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHEleraRRTLETEAQNLRIQTQELEEEL 1577
Cdd:TIGR00606 831 KQEKQHELD--TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR----RQQFEEQLVELSTEVQSLIREI 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1578 SEAENSRLRLEVTLQALKAQFEREISTNEE---KGEEKRRALSKQVRELEIQLEE-ERSQRSQSVSSKKQLEAELQEAEA 1653
Cdd:TIGR00606 905 KDAKEQDSPLETFLEKDQQEKEELISSKETsnkKAQDKVNDIKEKVKNIHGYMKDiENKIQDGKDDYLKQKETELNTVNA 984
|
810 820
....*....|....*....|
gi 1988774933 1654 QVETANRGKEEAMKQLRRLQ 1673
Cdd:TIGR00606 985 QLEECEKHQEKINEDMRLMR 1004
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1076-1543 |
2.52e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.89 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1076 EKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGM 1155
Cdd:pfam05557 12 SQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1156 RERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHeTQLSELRVKHSAALDSLQEQLD 1235
Cdd:pfam05557 92 LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKA-SEAEQLRQNLEKQQSSLAEAEQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1236 NSKRARQSLEkakatLEEERQNLTSELKSLQASRSESERGRKRadnqLQELSARLAQADREREDREERMHKLQCEIESLS 1315
Cdd:pfam05557 171 RIKELEFEIQ-----SQEQDSEIVKNSKSELARIPELEKELER----LREHNKHLNENIENKLLLKEEVEDLKRKLEREE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1316 GnlssSDSKSLRLAKEISSLESQLHDARELLQD---ESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHS 1392
Cdd:pfam05557 242 K----YREEAATLELEKEKLEQELQSWVKLAQDtglNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1393 QQLTELRKQSEEVNSAVEAGDEIRRKLQRELD---------SAIQRERQKEEEKERVERQRERLREEIEDMTIALQR--- 1460
Cdd:pfam05557 318 QELAQYLKKIEDLNKKLKRHKALVRRLQRRVLlltkerdgyRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAhne 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1461 --ERQNCTALEKRQKKFDQCLAEEKAVSARLAEErdrAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQL 1538
Cdd:pfam05557 398 emEAQLSVAEEELGGYKQQAQTLERELQALRQQE---SLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERR 474
|
....*
gi 1988774933 1539 VNQQD 1543
Cdd:pfam05557 475 CLQGD 479
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
871-1128 |
2.66e-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: 45.88 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 871 RQDEEIQTREAALQKAK-EQLTRAEQDYTELDRKHAQLLEekAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGEL 949
Cdd:pfam17380 360 RELERIRQEEIAMEISRmRELERLQMERQQKNERVRQELE--AARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 950 ETRLEEEEERGVQLANEKKKMQQNIQdlEEQLEEEESARQRLLLEKVtletkvkslETDLATAVEQRerlgkeKKQLEER 1029
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVE--RLRQQEEERKRKKLELEKE---------KRDRKRAEEQR------RKILEKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1030 LNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRmeseamEAQEQLsdlgMLSSELRGSLAQ 1109
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR------RIQEQM----RKATEERSRLEA 570
|
250
....*....|....*....
gi 1988774933 1110 KEKEITSLQGRLEEEGARR 1128
Cdd:pfam17380 571 MEREREMMRQIVESEKARA 589
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
999-1249 |
3.04e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 999 ETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREeqgrleQEKF 1078
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER------REEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1079 KRRMESeameAQEQLSDLGMLSSeLRGSlaqkeKEITSLQGRLEeegaRRAEAQRSLREALSQVSELKEEVENERgmrER 1158
Cdd:COG3883 89 GERARA----LYRSGGSVSYLDV-LLGS-----ESFSDFLDRLS----ALSKIADADADLLEELKADKAELEAKK---AE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1159 AEKQRrdlsEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSK 1238
Cdd:COG3883 152 LEAKL----AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250
....*....|.
gi 1988774933 1239 RARQSLEKAKA 1249
Cdd:COG3883 228 AAAAAAAAAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
868-1053 |
3.25e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 868 QVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRK----HAQLLEEKAVLADQLQAEAELFAEAEEMR-------ARLA 936
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEiaelRAELEAQKEELAELLRALYRLGRQPPLALllspedfLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 937 SRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQR 1016
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
170 180 190
....*....|....*....|....*....|....*..
gi 1988774933 1017 ERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNK 1053
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
872-1219 |
3.37e-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: 45.27 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 872 QDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLASRKQELEEVLGELET 951
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 952 RLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLn 1031
Cdd:pfam07888 123 QRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSL- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1032 evtdqlteeEEKTKSLNKLKNKqeavIADLEERLKREEQGRLEQEKFKRRMES--EAMEAQEQLSDLgmLSSELRGSLAQ 1109
Cdd:pfam07888 202 ---------AQRDTQVLQLQDT----ITTLTQKLTTAHRKEAENEALLEELRSlqERLNASERKVEG--LGEELSSMAAQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1110 KEKEITSL-QGRLE--EEGARRAEAQRSLREALSQVSELKE------EVENERGMRERAEKQRRD--LSEEL---EALRT 1175
Cdd:pfam07888 267 RDRTQAELhQARLQaaQLTLQLADASLALREGRARWAQEREtlqqsaEADKDRIEKLSAELQRLEerLQEERmerEKLEV 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1988774933 1176 ELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSEL 1219
Cdd:pfam07888 347 ELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1031-1682 |
3.71e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1031 NEVTDQLTEEEEKTKSLNKLKNK---QEAVIADLEERL-KREEQGRLEQEKFKrRMESEAMEAQEQL-----------SD 1095
Cdd:TIGR04523 26 NIANKQDTEEKQLEKKLKTIKNElknKEKELKNLDKNLnKDEEKINNSNNKIK-ILEQQIKDLNDKLkknkdkinklnSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1096 LGMLSSELRGSLAQK---EKEITSLQGRLEEEgarraeaQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEA 1172
Cdd:TIGR04523 105 LSKINSEIKNDKEQKnklEVELNKLEKQKKEN-------KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1173 LRTELEDTLDSTAAQQELRSRREAELSELQRCVEEEtrrhetqlselrvkhsaalDSLQEQLDNSKRARQSLEKAKATLE 1252
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-------------------KSLESQISELKKQNNQLKDNIEKKQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1253 EERQNLTSELKSLQASRSESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLR----- 1327
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKselkn 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1328 LAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNS 1407
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLES 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1408 AVEAGDEIRRKLQRELDSaiqrerqkeeekerverqrerlreeiedmtiaLQRERQnctALEKRQKKFdqclaeeKAVSA 1487
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKK--------------------------------LQQEKE---LLEKEIERL-------KETII 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1488 RLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLR 1567
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1568 IQTQELEEELSEaensrlrlevtLQALKAQFEREISTNEEKGEE-----KRRALSKQVRELEIQLEEERSQRSQSVSSKK 1642
Cdd:TIGR04523 517 KKISSLKEKIEK-----------LESEKKEKESKISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1988774933 1643 QLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRE 1682
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1492-1683 |
4.09e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1492 ERDRAEADSREK--ETRCLALSRALQEAQDQKEELERANK--QLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLR 1567
Cdd:COG3206 167 ELRREEARKALEflEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1568 IQTQELEEELSEAENSRL--RLEVTLQALKAQfEREISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQsvsskkQLE 1645
Cdd:COG3206 247 AQLGSGPDALPELLQSPViqQLRAQLAELEAE-LAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA------SLE 319
|
170 180 190
....*....|....*....|....*....|....*...
gi 1988774933 1646 AELQEAEAQVETANRGKEEAMKQLRRLQGQMKEvLREL 1683
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAE-LRRL 356
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1131-1367 |
5.05e-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: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1131 AQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRcveeetr 1210
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1211 rhetQLSELRvkhsAALDSLQEQLDNSKRARQSLEKA-KATLEEERQNLTSELKSLQASRSESERGRKRADnQLQELSAR 1289
Cdd:COG4942 91 ----EIAELR----AELEAQKEELAELLRALYRLGRQpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774933 1290 LAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQKMALASRVRALEEEK 1367
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1103-1615 |
5.39e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1103 LRGSLAQKEKEITSLQGRLEEEGARRAEAQRS-LREALSQVSELKEEVENergmRERAEKQRRDLSEELEALRTELEDtl 1181
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEeLKEAEEKEEEYAELQEE----LEELEEELEELEAELEELREELEK-- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1182 dstAAQQELRSRREAELSELQRCVEEETRRhetqlselrvkhsaaLDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSE 1261
Cdd:COG4717 121 ---LEKLLQLLPLYQELEALEAELAELPER---------------LEELEERLEELRELEEELEELEAELAELQEELEEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1262 LKSLQAsrsESERGRKRADNQLQELSARLAQADREREDREERMHKLQCEIESLSGNLsssdskslrlakEISSLESQLHD 1341
Cdd:COG4717 183 LEQLSL---ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL------------EAAALEERLKE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1342 ARELLqdesrqkmALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQR 1421
Cdd:COG4717 248 ARLLL--------LIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1422 ELDSAIQRERQKEEEKERVERQRERLREeiedmtiALQRERQNCTALEKRqkkfdqclAEEKAVSARLAEERDRAEADSR 1501
Cdd:COG4717 320 ELEELLAALGLPPDLSPEELLELLDRIE-------ELQELLREAEELEEE--------LQLEELEQEIAALLAEAGVEDE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1502 EKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDvgknvHELERARRTLETEAQNLRIQTQELEEELSEAE 1581
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEELEELREELAELE 459
|
490 500 510
....*....|....*....|....*....|....*.
gi 1988774933 1582 N--SRLRLEVTLQALKAQFEREISTNEEKGEEKRRA 1615
Cdd:COG4717 460 AelEQLEEDGELAELLQELEELKAELRELAEEWAAL 495
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1106-1274 |
5.52e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1106 SLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRD------LSEELEALRTELED 1179
Cdd:PRK12705 23 VLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREeerlvqKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1180 TLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLT 1259
Cdd:PRK12705 103 LENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNIL 182
|
170
....*....|....*
gi 1988774933 1260 SELKSLQASRSESER 1274
Cdd:PRK12705 183 AQAMQRIASETASDL 197
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1225-1370 |
6.09e-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: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1225 AALDSLQE---QLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSARLA--QADRERED 1299
Cdd:COG1579 7 RALLDLQEldsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyEEQLGNVR 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774933 1300 REERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLQDESRQ----KMALASRVRALEEEKNGL 1370
Cdd:COG1579 87 NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekKAELDEELAELEAELEEL 161
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1158-1538 |
6.11e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1158 RAEKQRRDLSEELEALRTELEDTLDSTAAQQELrsrreaeLSELQRCVEEETRRhetqLSELRVKHSAALDSL------- 1230
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYR-------LVEMARELAELNEA----ESDLEQDYQAASDHLnlvqtal 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1231 --QEQLdnsKRARQSLEKAKATLEEerQNLTSELKSLQasRSESERGRKRADNQLQELSARLA----------------- 1291
Cdd:PRK04863 345 rqQEKI---ERYQADLEELEERLEE--QNEVVEEADEQ--QEENEARAEAAEEEVDELKSQLAdyqqaldvqqtraiqyq 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1292 QADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKEISSLESQLHDARELLqDESRQKMALA-------SRVRALE 1364
Cdd:PRK04863 418 QAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAH-SQFEQAYQLVrkiagevSRSEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1365 EEKNGLmerleEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQR 1444
Cdd:PRK04863 497 VARELL-----RRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1445 ERLREEIEDMTiALQRERQNCTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEEL 1524
Cdd:PRK04863 572 ESVSEARERRM-ALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDEL 650
|
410
....*....|....
gi 1988774933 1525 ERANKQLRLEMEQL 1538
Cdd:PRK04863 651 AARKQALDEEIERL 664
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
989-1222 |
6.33e-04 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 43.86 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 989 QRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIAD-------L 1061
Cdd:pfam04849 90 QSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHgcvqldaL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1062 EERLKR--EEQGRLEQEKFKRRMESEAMEAQEQlsdlgMLSSELRGSLAQKEKEItslqGRLEEEGARRAEAQRSLREA- 1138
Cdd:pfam04849 170 QEKLRGleEENLKLRSEASHLKTETDTYEEKEQ-----QLMSDCVEQLSEANQQM----AELSEELARKMEENLRQQEEi 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1139 ---LSQVSELkeevenergmreraEKQRRDLSEELEALRTELEDTLDstaAQQELRSrreaELSELQ-RCVEEETRRHET 1214
Cdd:pfam04849 241 tslLAQIVDL--------------QHKCKELGIENEELQQHLQASKE---AQRQLTS----ELQELQdRYAECLGMLHEA 299
|
250
....*....|
gi 1988774933 1215 Q--LSELRVK 1222
Cdd:pfam04849 300 QeeLKELRKK 309
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1327-1728 |
6.61e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1327 RLAKEISSLESQLHDARELLQ--DESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEE 1404
Cdd:COG4717 92 ELQEELEELEEELEELEAELEelREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1405 VNSAVEAGDEIRRKLQRELDSAIQRERQKEEEKERVERQRERLREEIEDMTIALQRER---QNCTALEKRQKKFDQCLAE 1481
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELeqlENELEAAALEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1482 EKAVSARLAEERDRAEADSREKE-------------TRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGkn 1548
Cdd:COG4717 252 LLIAAALLALLGLGGSLLSLILTiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALG-- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1549 vheLERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKAQFEREISTNEE------KGEEKRRALSKQVRE 1622
Cdd:COG4717 330 ---LPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelraalEQAEEYQELKEELEE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1623 LEIQLEEER--SQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVL--RELDDSKVTRDDVISQSK 1698
Cdd:COG4717 407 LEEQLEELLgeLEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELR 486
|
410 420 430
....*....|....*....|....*....|
gi 1988774933 1699 DSEKKIQTLEAEVLHLTEELAVSERQKRQA 1728
Cdd:COG4717 487 ELAEEWAALKLALELLEEAREEYREERLPP 516
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1183-1412 |
7.02e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1183 STAAQQELRSRREAELSELQRCVEEETRRHETQLSElRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSEL 1262
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1263 KSLQASRSESERGRKRADNQLQELSAR-----------LAQADREREDREERMHKLQCEIESLSGNLSSSDSKSLRLAKE 1331
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1332 ISSLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHSQQLTELRKQSEEVNSAVEA 1411
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
.
gi 1988774933 1412 G 1412
Cdd:COG4942 253 G 253
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1081-1234 |
7.64e-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: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1081 RMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRE--- 1157
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyea 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1158 ------RAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQ 1231
Cdd:COG1579 94 lqkeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
...
gi 1988774933 1232 EQL 1234
Cdd:COG1579 174 PEL 176
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1032-1200 |
9.15e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.24 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1032 EVTDQLTEE----------EEKTKSlnklknkQEAVIADLEERLKREEQGRLEQEKFKRRMESEameaqeqlsdlgmlss 1101
Cdd:PTZ00491 639 EPVDERTRDslqksvqlaiEITTKS-------QEAAARHQAELLEQEARGRLERQKMHDKAKAE---------------- 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1102 ELRGSLAQKEKEITSlqgrLEEEGARRAEAqrslrEALSQVSELKEEVENERGmRERAEKQRRDLSEELEALRTELEDTL 1181
Cdd:PTZ00491 696 EQRTKLLELQAESAA----VESSGQSRAEA-----LAEAEARLIEAEAEVEQA-ELRAKALRIEAEAELEKLRKRQELEL 765
|
170
....*....|....*....
gi 1988774933 1182 DSTAAQQELRSRREAELSE 1200
Cdd:PTZ00491 766 EYEQAQNELEIAKAKELAD 784
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
883-1261 |
9.66e-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: 9.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 883 LQKAKEQLTRAEQDYTElDRKHAQLLEEKAVLADQLQAEAELFAEAEEMRARLasRKQELEEVLGELETRLEEEEERGVQ 962
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE-KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEM--DRQAAIYAEQERMAMERERELERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 963 LANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKsletdlatavEQRERLGKEKKQLEERLNEVTDQLTEEEE 1042
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVR----------QELEAARKVKILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1043 KTKSLNKLKNKQEAVIAdlEERLKREEQGRLEQekfkrrmeseaMEAQEQLSDLgmlsselrgslaqkekeitslqgRLE 1122
Cdd:pfam17380 425 IRAEQEEARQREVRRLE--EERAREMERVRLEE-----------QERQQQVERL-----------------------RQQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1123 EEGARRAeaqrslrealsqvselKEEVENERGMRERAEKQRRD-LSEELEALRTE-LEDTLDSTAAQQELRSRREAELSE 1200
Cdd:pfam17380 469 EEERKRK----------------KLELEKEKRDRKRAEEQRRKiLEKELEERKQAmIEEERKRKLLEKEMEERQKAIYEE 532
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774933 1201 LQRCVEEETRRHETQLSELRvkhsaaldSLQEQLDNSKRARQSLEKAKATLEEERQNLTSE 1261
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERR--------RIQEQMRKATEERSRLEAMEREREMMRQIVESE 585
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
880-1288 |
9.81e-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: 44.56 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 880 EAALQKAKEQLTRAEQDYTELDRKHAQLLEEKAVLADQLQAEaelfaeaeemRARLAsrkqeleevlgeletrleeeeer 959
Cdd:COG3096 291 RRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAA----------SDHLN----------------------- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 960 GVQLAnekKKMQQNIQdleeqleeeesaRQRLLLEKvtLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTE 1039
Cdd:COG3096 338 LVQTA---LRQQEKIE------------RYQEDLEE--LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1040 -----EEEKTKSLnklkNKQEAVIAdLEERLKREEQGRLEQEKFKRRMesEAMEAQEQLSDLGMLSSELRGSLAQKEKE- 1113
Cdd:COG3096 401 yqqalDVQQTRAI----QYQQAVQA-LEKARALCGLPDLTPENAEDYL--AAFRAKEQQATEEVLELEQKLSVADAARRq 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1114 -------ITSLQGRLEeegarRAEAQRSLREALSQVSELKEEVENERGMR------ERAEKQRRDLSEELEAL----RTE 1176
Cdd:COG3096 474 fekayelVCKIAGEVE-----RSQAWQTARELLRRYRSQQALAQRLQQLRaqlaelEQRLRQQQNAERLLEEFcqriGQQ 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1177 LEDTLDSTAAQQELRSRREAELSELQRCVEE--ETRRHETQL----SELRVKH------SAALDSLQEQLDnskrarQSL 1244
Cdd:COG3096 549 LDAAEELEELLAELEAQLEELEEQAAEAVEQrsELRQQLEQLrariKELAARApawlaaQDALERLREQSG------EAL 622
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1988774933 1245 EKAKAtLEEERQNLTSELKSLQASRSESERGRKRADNQLQELSA 1288
Cdd:COG3096 623 ADSQE-VTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1062-1193 |
1.07e-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: 43.21 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1062 EERLKREEQGRLEQEKFKRRMESEAMEAQEQLSdlgmlSSELRgslaqkeKEITSLQGRLEEEGARRAEAQRSLREALSQ 1141
Cdd:pfam09787 55 ERDLLREEIQKLRGQIQQLRTELQELEAQQQEE-----AESSR-------EQLQELEEQLATERSARREAEAELERLQEE 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 1142 VSELKEEVENERGMREraeKQRRDLSEELEALRTELEDTLDSTAAQQELRSR 1193
Cdd:pfam09787 123 LRYLEEELRRSKATLQ---SRIKDREAEIEKLRNQLTSKSQSSSSQSELENR 171
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
962-1178 |
1.14e-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: 43.86 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 962 QLANEKKKMQQNIQDLEEQLEEEESARQRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEE 1041
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1042 EKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRL 1121
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL 547
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774933 1122 EE--EGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELE 1178
Cdd:TIGR04523 548 NKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1025-1158 |
1.16e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1025 QLEERLNEVTDQLTEEEEKtkslnklKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELR 1104
Cdd:PRK11637 174 ELKQTREELAAQKAELEEK-------QSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLR 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1988774933 1105 GSLAQKEKEItslQGRLEEEgARRAEAQRSLREALSQVSELKEEVENERGMRER 1158
Cdd:PRK11637 247 DSIARAEREA---KARAERE-AREAARVRDKQKQAKRKGSTYKPTESERSLMSR 296
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
996-1169 |
1.16e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 996 VTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNklknkQEAVIADLEERLKREEQGRLEQ 1075
Cdd:COG3206 208 VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL-----QSPVIQQLRAQLAELEAELAEL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1076 EKFKRRMESEAMEAQEQLSDL-GMLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQ---RSLREALSQVSELKEEVEN 1151
Cdd:COG3206 283 SARYTPNHPDVIALRAQIAALrAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEarlAELPELEAELRRLEREVEV 362
|
170
....*....|....*...
gi 1988774933 1152 ERGMRERAEKQRRDLSEE 1169
Cdd:COG3206 363 ARELYESLLQRLEEARLA 380
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1610-1738 |
1.27e-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: 42.60 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1610 EEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQG--QMKEVLRELDDSK 1687
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLK 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1988774933 1688 VTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADE 1738
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1602-1932 |
1.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1602 ISTNEEKGEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLR 1681
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1682 ELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVN 1761
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1762 QLEEELEEEQTNNELLTERLRKTALQVETLTVQLQGERTLAQKAEAAREQLEKQNKELKARLGEMEGAVRGKHRMSVAAL 1841
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1842 EAKIETMEEQLEQERQERAIANKLMRKTEKKLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQ 1921
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
330
....*....|.
gi 1988774933 1922 KRKLQRELEEL 1932
Cdd:COG4372 349 GLLDNDVLELL 359
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1644-1950 |
1.47e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1644 LEAELQEAEAQVETANRGKEEAMKQLrrlqGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSER 1723
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETR----DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1724 QKRQAQQERDEIADEMVSSSSGKNVLSEEKRRLDARVNQLEEELEEEQTNNELLT---ERLRKTALQVETLTVQLQGE-R 1799
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNeeaESLREDADDLEERAEELREEaA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1800 TLAQKAEAAREQLEKQN---KELKARLGEMEGAV--------------------RGKHRMSVAALEAKIETMEEQLEQER 1856
Cdd:PRK02224 367 ELESELEEAREAVEDRReeiEELEEEIEELRERFgdapvdlgnaedfleelreeRDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1857 QERAianklmrktEKKLKEVMMQAEDERR--HADQYREQLDKSMVRLKQLKRQLEEVEEENSRSSAQKrKLQRELEELTD 1934
Cdd:PRK02224 447 ALLE---------AGKCPECGQPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEE 516
|
330
....*....|....*.
gi 1988774933 1935 SSQTMNREISSLRNQL 1950
Cdd:PRK02224 517 RREDLEELIAERRETI 532
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1010-1264 |
1.49e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.74 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1010 ATAVEQRERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEaVIADLEERLKREEQGRLEQEKFKRRMESEAMEA 1089
Cdd:PLN02939 152 LQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVE-ILEEQLEKLRNELLIRGATEGLCVHSLSKELDV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1090 --QEQLS---DLGMLSSEL------RGSLAQKEKEITSLQGRLEEEGARRAEAQrslrEALSQVSELK-----EEVENER 1153
Cdd:PLN02939 231 lkEENMLlkdDIQFLKAELievaetEERVFKLEKERSLLDASLRELESKFIVAQ----EDVSKLSPLQydcwwEKVENLQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1154 GMRERAEK----------QRRDLSEELEALRTELEDTLDSTAA-------QQELRSRREaelsELQRCveeetrrHETQL 1216
Cdd:PLN02939 307 DLLDRATNqvekaalvldQNQDLRDKVDKLEASLKEANVSKFSsykvellQQKLKLLEE----RLQAS-------DHEIH 375
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1988774933 1217 SELRVKHsaalDSLQEQLDNSKRARQslEKAKATLEEERQNLTSELKS 1264
Cdd:PLN02939 376 SYIQLYQ----ESIKEFQDTLSKLKE--ESKKRSLEHPADDMPSEFWS 417
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
967-1246 |
1.62e-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: 42.88 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 967 KKKMQQNIQDLEEQLEEEESARqRLLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEVTDQLTEeeeKTKS 1046
Cdd:pfam15905 62 KKKSQKNLKESKDQKELEKEIR-ALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLE---LTRV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1047 LNKLKNKQEAviadlEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGRLEEEGA 1126
Cdd:pfam15905 138 NELLKAKFSE-----DGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1127 RRAEAQrslrealSQVSELKEEVENERGMRERAEKQRRD---LSEELEALRTELEDTLDSTAAQQELRSRREAELSELQR 1203
Cdd:pfam15905 213 EKIEEK-------SETEKLLEYITELSCVSEQVEKYKLDiaqLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCK 285
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1988774933 1204 CVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEK 1246
Cdd:pfam15905 286 LLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1001-1254 |
1.75e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1001 KVKSLETDLATAVEQ--------RERLGKEKkqLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEE---RLK--- 1066
Cdd:COG2268 98 KVNSDPEDIANAAERflgrdpeeIEELAEEK--LEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKnglELEsva 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1067 ----REEQGRLEQEKFKRRMESEAMEAQEQlsdlgmlsselrgSLAQKEKEITSLQGRLEEEGARrAEAQRslrealsqv 1142
Cdd:COG2268 176 itdlEDENNYLDALGRRKIAEIIRDARIAE-------------AEAERETEIAIAQANREAEEAE-LEQER--------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1143 selkeEVENERGMRERAEKQRRDLSEELEALRTELEdtldstaAQQELRSRREAELSELQRCVEEETRRHETQLSELRVK 1222
Cdd:COG2268 233 -----EIETARIAEAEAELAKKKAEERREAETARAE-------AEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAE 300
|
250 260 270
....*....|....*....|....*....|..
gi 1988774933 1223 HSaaldslQEQLDNSKRARQSLEKAKATLEEE 1254
Cdd:COG2268 301 RE------EAELEADVRKPAEAEKQAAEAEAE 326
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1157-1951 |
1.90e-03 |
|
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: 43.50 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1157 ERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQrCVEEETRRHETQLSEL--RVKHSAALDSLQEQL 1234
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLE-SSREIVKSYENELDPLknRLKEIEHNLSKIMKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1235 DNSKRARQSLEKakatleeERQNLTSELKSLQasrsesERGRKRADNQLQELSARLAQADREREDREERMHKlqcEIESL 1314
Cdd:TIGR00606 268 DNEIKALKSRKK-------QMEKDNSELELKM------EKVFQGTDEQLNDLYHNHQRTVREKERELVDCQR---ELEKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1315 SGNLSSSDSKSLRLAKEIS--SLESQLHDARELLQDESRQKMALASRVRALEEEKNGLMERLEEEEERGKELSRQIQTHS 1392
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGrlQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1393 QQLTELrkqSEEVNSAVEAGDEIRRKlQRELDSAIQRERQKEEEKERVERQRErlreeiedmtialqRERQNCTALEKRQ 1472
Cdd:TIGR00606 412 QLCADL---QSKERLKQEQADEIRDE-KKGLGRTIELKKEILEKKQEELKFVI--------------KELQQLEGSSDRI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1473 KKFDQCLAEEKAvsaRLAEERDRAEADSREKETRCLalsralqeaQDQKEELERANKQLRLEMEQLvNQQDDVGKNVHEL 1552
Cdd:TIGR00606 474 LELDQELRKAER---ELSKAEKNSLTETLKKEVKSL---------QNEKADLDRKLRKLDQEMEQL-NHHTTTRTQMEML 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1553 ERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALkaqfereiSTNEEKGEEKRRALSKQVRELE-----IQL 1627
Cdd:TIGR00606 541 TKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSK--------SKEINQTRDRLAKLNKELASLEqnknhINN 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1628 EEERSQRSQSVSSKKQLEA-ELQEAEAQVETANRGKEEAMKQLRRLQGQM---KEVLRELDDSKVTRDDVISQSKDSEKK 1703
Cdd:TIGR00606 613 ELESKEEQLSSYEDKLFDVcGSQDEESDLERLKEEIEKSSKQRAMLAGATavySQFITQLTDENQSCCPVCQRVFQTEAE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1704 IQT----LEAEVLHLTEELAVSERQKRQAQQERDEIadeMVSSSSGKNVLSEEKRRLDArvnqleeeleeeqtnnelLTE 1779
Cdd:TIGR00606 693 LQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEM---LGLAPGRQSIIDLKEKEIPE------------------LRN 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1780 RLRKTALQVETLTVQLQGERTLAQKAEAAreqlEKQNKELKARLGEMEgavrgKHRMSVAALEAKIETMEEQLEQERQER 1859
Cdd:TIGR00606 752 KLQKVNRDIQRLKNDIEEQETLLGTIMPE----EESAKVCLTDVTIME-----RFQMELKDVERKIAQQAAKLQGSDLDR 822
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1860 AIANKLMRKTEK--KLKEVMMQAEDERRHADQYREQLDKSMVRLKQLKRQLEEVEEensrSSAQKRKLQRELEELTDSSQ 1937
Cdd:TIGR00606 823 TVQQVNQEKQEKqhELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGT----NLQRRQQFEEQLVELSTEVQ 898
|
810
....*....|....
gi 1988774933 1938 TMNREISSLRNQLS 1951
Cdd:TIGR00606 899 SLIREIKDAKEQDS 912
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1033-1253 |
1.92e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.02 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1033 VTDQLTEEEEKTKSLNK---LKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQ 1109
Cdd:pfam15709 305 VTGNMESEEERSEEDPSkalLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1110 KEKEITSLQGRLEEEGARRAEAQRSLRealsqvseLKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQE 1189
Cdd:pfam15709 385 RFEEIRLRKQRLEEERQRQEEEERKQR--------LQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKE 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774933 1190 LRSRREAELSELQRCVEEEtrrhetQLSELRVKHSAALDSLQEQldnSKRARQSLEKAKATLEE 1253
Cdd:pfam15709 457 LEMQLAEEQKRLMEMAEEE------RLEYQRQKQEAEEKARLEA---EERRQKEEEAARLALEE 511
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1506-1819 |
1.97e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1506 RCLALSRALQEAQDQKEEL----ERANKQLRLEMEQLVNQQDDVGKNVHELERARRTLETEAQNLRIQTQELEEELSEAE 1581
Cdd:pfam07888 28 RAELLQNRLEECLQERAELlqaqEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1582 NSRLRLEVTLQALKAQFEREISTNEEKgEEKRRALSKQVRELEIQLEEERSQRSQSVSSKKQLEAE---LQEAEAQVETA 1658
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIREL-EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAErkqLQAKLQQTEEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1659 NRGKEEAMKQLRRLQGQMKEVLRELDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSERQkrqAQQERDEIADE 1738
Cdd:pfam07888 187 LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERK---VEGLGEELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1739 MVSSSSGKNVLseEKRRLDArvnqleeeleeeqtnnELLTERLRKTALQVETLTVQLQGER-TLAQKAEAAREQLEKQNK 1817
Cdd:pfam07888 264 AAQRDRTQAEL--HQARLQA----------------AQLTLQLADASLALREGRARWAQEReTLQQSAEADKDRIEKLSA 325
|
..
gi 1988774933 1818 EL 1819
Cdd:pfam07888 326 EL 327
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
830-1201 |
2.27e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 830 KKQQQLSALRVMQRNCAAYLKLRNWQWWRLFTKVkpLLQVTRQDEEIQTREAALQKAKEQLTRAEQDYTELDRKHAQLLE 909
Cdd:COG4717 164 ELEELEAELAELQEELEELLEQLSLATEEELQDL--AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 910 EKAVlaDQLQAEAELFAEAEEMRARLASRKQELEEVLGELETRLEEEEERGVQLANEKKKMQQNIQDLEEQLEEEESARQ 989
Cdd:COG4717 242 EERL--KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 990 RL--LLEKVTLETKV-KSLETDLATAVEQRERLGKEKKQLEERLnevtDQLTEEEEKTKSLNKLKNKQEAVIADLEERLK 1066
Cdd:COG4717 320 ELeeLLAALGLPPDLsPEELLELLDRIEELQELLREAEELEEEL----QLEELEQEIAALLAEAGVEDEEELRAALEQAE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1067 REEQGRLEQEKFKRRMESEAMEAQEQLSDLgmlsselrgSLAQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELK 1146
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEAL---------DEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774933 1147 E--EVENERGMRERAEKQRRDLSEELEALRTeLEDTLDstAAQQELRSRREAELSEL 1201
Cdd:COG4717 467 EdgELAELLQELEELKAELRELAEEWAALKL-ALELLE--EAREEYREERLPPVLER 520
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1049-1182 |
2.93e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1049 KLKNKQEAVIADLEERLKREEQGRLEQEKFKRrmeSEAMEAQEQLSdlgmlssELRGSLAQKEKEITSLQGRLEEEgarr 1128
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKK---EQDEASFERLA-------ELRDELAELEEELEALKARWEAE---- 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1988774933 1129 aeaqrslREALSQVSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLD 1182
Cdd:COG0542 467 -------KELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1465-1684 |
3.06e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1465 CTALEKRQKKFDQCLAEEKAVSARLAEERDRAEADSREKETRCLALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDD 1544
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1545 VGKNVHELERARRTLETEAQNLRIQTQELEEELSEAENSRLRLEVTLQALKaQFEREISTNEEKGEEKRRALSKQVRELE 1624
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1625 IQLEEERSQRSQSVSSKKQLEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVLRELD 1684
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1509-1932 |
3.21e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1509 ALSRALQEAQDQKEELERANKQLRLEMEQLVNQQDDVGknvhELERARRTLETEAQNlriqtqeleeelseaenSRLRLE 1588
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQA-----------------ASDHLN 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1589 VTLQALKAQfereistneEKGEEKRRALSkqvrELEIQLEEERSQRSQSVSSKKQLEAELQEAEAQVET-----ANRGKE 1663
Cdd:PRK04863 339 LVQTALRQQ---------EKIERYQADLE----ELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDElksqlADYQQA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1664 EAMKQLRRLQ-GQMKEVLRE----LDDSKVTRDDVISQSKDSEKKIQTLEAEVLHLTEELAVSE---RQKRQAQQERDEI 1735
Cdd:PRK04863 406 LDVQQTRAIQyQQAVQALERakqlCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQaahSQFEQAYQLVRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1736 ADEMVSS---SSGKNVL--SEEKRRLDARVNQLEEELEEEQTNNELL--TERLRKTALQVetLTVQLQGERTLAQKAEAA 1808
Cdd:PRK04863 486 AGEVSRSeawDVARELLrrLREQRHLAEQLQQLRMRLSELEQRLRQQqrAERLLAEFCKR--LGKNLDDEDELEQLQEEL 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1809 REQLEKQNKELkarlgEMEGAVRGKHRMSVAALEAKIETMEEQLEQERQERAIANKLMRKTEKKLKEvmmqaederrhad 1888
Cdd:PRK04863 564 EARLESLSESV-----SEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFED------------- 625
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1988774933 1889 qyREQLDKSMvrlKQLKRQLEEVEEENSRSSAQKRKLQRELEEL 1932
Cdd:PRK04863 626 --SQDVTEYM---QQLLERERELTVERDELAARKQALDEEIERL 664
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1108-1271 |
4.13e-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: 41.94 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1108 AQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKEEVENERGMRERAEKQRR------DLSEELEALRTELEDTL 1181
Cdd:pfam05667 331 QQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKvkkktlDLLPDAEENIAKLQALV 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1182 DSTAAQ-QELRSRREA----------ELSELQRCVEEETRRhetQLSELRvkhsaaldSLQEQLdnskraRQSLEKAKAT 1250
Cdd:pfam05667 411 DASAQRlVELAGQWEKhrvplieeyrALKEAKSNKEDESQR---KLEEIK--------ELREKI------KEVAEEAKQK 473
|
170 180
....*....|....*....|...
gi 1988774933 1251 lEEERQNLTSELKSL--QASRSE 1271
Cdd:pfam05667 474 -EELYKQLVAEYERLpkDVSRSA 495
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1016-1123 |
4.85e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1016 RERLGKEKKQLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERL----KREEQGRLEQE-KFKRRMESEAMEAQ 1090
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKeklqEEEDKLLEEAEkEAQQAIKEAKKEAD 587
|
90 100 110
....*....|....*....|....*....|...
gi 1988774933 1091 EQLSDLGMLssELRGSLAQKEKEITSLQGRLEE 1123
Cdd:PRK00409 588 EIIKELRQL--QKGGYASVKAHELIEARKRLNK 618
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1011-1235 |
4.99e-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: 40.86 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1011 TAVEQRERLGKEKKQlEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQ 1090
Cdd:pfam06008 24 LTKQLQEYLSPENAH-KIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEIN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1091 EQLSDLGMLSSELRGS-LAQKEKEITSLQGRLEEE--GARRAEAQRSLREA---LSQVSELKEEVENE-RGMRERAEKQR 1163
Cdd:pfam06008 103 EKVATLGENDFALPSSdLSRMLAEAQRMLGEIRSRdfGTQLQNAEAELKAAqdlLSRIQTWFQSPQEEnKALANALRDSL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774933 1164 RDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVeEETRRHETQLSELRVKHSAALDSLQEQLD 1235
Cdd:pfam06008 183 AEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKK-EEVSEQKNQLEETLKTARDSLDAANLLLQ 253
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1128-1288 |
5.09e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1128 RAEAQRSLREALSQVSELKEEVENErgmreraekqrrdLSEELEALRTELEdtldstaaqQELRSRREaelsELQRcVEE 1207
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALLE-------------AKEEIHKLRNEFE---------KELRERRN----ELQK-LEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1208 ETRRHEtqlselrvkhsaaldslqEQLDNSKrarQSLEKAKATLEEERQNLTSELKSLQASRSESERGRKRADNQLQELS 1287
Cdd:PRK12704 90 RLLQKE------------------ENLDRKL---ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIS 148
|
.
gi 1988774933 1288 A 1288
Cdd:PRK12704 149 G 149
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
931-1366 |
5.34e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 931 MRARLASRKQELEEVLGELETRLeeeeergvqlanekkKMQQNIQDLEEQLEEEESARQRLllekVTLETKVKSLETDLa 1010
Cdd:pfam10174 142 MELRIETQKQTLGARDESIKKLL---------------EMLQSKGLPKKSGEEDWERTRRI----AEAEMQLGHLEVLL- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1011 tavEQRErlgKEKKQLEERLNEvTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEqgrLEQEKFKRRMESEAMEAQ 1090
Cdd:pfam10174 202 ---DQKE---KENIHLREELHR-RNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTEDRE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1091 EQLSDLGMLSS----------ELRGSLAQKEKEITSLQGRLEEEGARRAEAQRS---LREAL-----------SQVSELK 1146
Cdd:pfam10174 272 EEIKQMEVYKShskfmknkidQLKQELSKKESELLALQTKLETLTNQNSDCKQHievLKESLtakeqraailqTEVDALR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1147 EEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTaaqqELRSRREAELSELQRCVEEETRRHETQLSELRvkhsAA 1226
Cdd:pfam10174 352 LRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDML----DVKERKINVLQKKIENLQEQLRDKDKQLAGLK----ER 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1227 LDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSELKSL-QASRSESERGRKradnQLQELSARLAQADREREDREERMH 1305
Cdd:pfam10174 424 VKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREdRERLEELESLKK----ENKDLKEKVSALQPELTEKESSLI 499
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774933 1306 KLQCEIESL--SGNLSSSDSKSLRLA-----KEISSLESQLHDARElLQDESRQKMALASRVRALEEE 1366
Cdd:pfam10174 500 DLKEHASSLasSGLKKDSKLKSLEIAveqkkEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQE 566
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1614-1739 |
5.51e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.19 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1614 RALSKQVRELEIQLEEERSQRSQSVSSKKQlEAELQEAEAQVETANRGKEEAMKQLRRLQGQMKEVL---RELDDSKVTR 1690
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAvsqQELDEARAAL 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1988774933 1691 DDVISQSKDSEKKIQTLEAEVLhLTEELAVSERQKRQAQQERDEIADEM 1739
Cdd:COG1566 158 DAAQAQLEAAQAQLAQAQAGLR-EEEELAAAQAQVAQAEAALAQAELNL 205
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1089-1235 |
5.95e-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: 39.55 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1089 AQEQLSDLGMLSSELRGSLAQKEKEIT-SLQGRLEEEGARRAEAQRSLREALSQ-VSELKEEVENE-RGMRERAEKQRRD 1165
Cdd:pfam01442 13 AEELQEQLGPVAQELVDRLEKETEALReRLQKDLEEVRAKLEPYLEELQAKLGQnVEELRQRLEPYtEELRKRLNADAEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1166 LSEELEA----LRTELEDTLDSTAAQ-----QELRSRREAELSELQRCVEEETRRHETQLS----ELRVKHSAALDSLQE 1232
Cdd:pfam01442 93 LQEKLAPygeeLRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAEEVQAQLSqrlqELREKLEPQAEDLRE 172
|
...
gi 1988774933 1233 QLD 1235
Cdd:pfam01442 173 KLD 175
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1134-1293 |
6.71e-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: 39.55 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1134 SLREALSQVSELKEEVENERGMRERAEKQRrdLSEELEALRTELEDtlDSTAAQQELRSRREAELSELQRCVEEETRRHE 1213
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDR--LEKETEALRERLQK--DLEEVRAKLEPYLEELQAKLGQNVEELRQRLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1214 TQLSELRVKHSAALDSLQEQLDNS-----KRARQSLEKAKATL----EEERQNLTSELKSLQAS-RSESERGRKRADNQL 1283
Cdd:pfam01442 77 PYTEELRKRLNADAEELQEKLAPYgeelrERLEQNVDALRARLapyaEELRQKLAERLEELKESlAPYAEEVQAQLSQRL 156
|
170
....*....|
gi 1988774933 1284 QELSARLAQA 1293
Cdd:pfam01442 157 QELREKLEPQ 166
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1026-1147 |
7.40e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1026 LEERLNEVTDQLTEEEEKTKSLNKLKnkQEAVIADLEERLKREEqGRLEQ-EKFKRRMESEAMEAQEQLSDLGMLSSELR 1104
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEH--EERELTEEEEEIRRLE-EQVERlEAEVEELEAELEEKDERIERLERELSEAR 454
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1988774933 1105 GSL---AQKEKEITSLQGRLEEEGARRAEAQRSLREALSQVSELKE 1147
Cdd:COG2433 455 SEErreIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1487-1688 |
7.52e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.01 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1487 ARLAEERDRAEADSrEKETRcLALSRALQEAQDQKEELERANKQLRLEMEQlvnqqddvgknvHELERARRTLETEAQNL 1566
Cdd:COG2268 195 AEIIRDARIAEAEA-ERETE-IAIAQANREAEEAELEQEREIETARIAEAE------------AELAKKKAEERREAETA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1567 RIQTQELEEELSEaensRLRLEVTLQALKAQFEREISTNEEKGEEKRRALSKQVRE------LEIQLEEERSQRSQSVSS 1640
Cdd:COG2268 261 RAEAEAAYEIAEA----NAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKpaeaekQAAEAEAEAEAEAIRAKG 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1988774933 1641 KKQLEAELQEAEAQVETANRGKEEAM-KQLRRLQGQMKEVLRELDDSKV 1688
Cdd:COG2268 337 LAEAEGKRALAEAWNKLGDAAILLMLiEKLPEIAEAAAKPLEKIDKITI 385
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
874-1262 |
7.84e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 874 EEIQTREAALQKAkEQLTRAEQdytelDRKHAQLLEEKAvladqlqaeaelfaeaeemrarlasrkqeleevlgeletrl 953
Cdd:PTZ00121 1610 EEAKKAEEAKIKA-EELKKAEE-----EKKKVEQLKKKE----------------------------------------- 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 954 eeeeergvqlANEKKKMQQniqdleeqleeeesarqrllLEKVTLETKVKSLEtdLATAVEQRERLGKEKKQLEERLNEV 1033
Cdd:PTZ00121 1643 ----------AEEKKKAEE--------------------LKKAEEENKIKAAE--EAKKAEEDKKKAEEAKKAEEDEKKA 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1034 TDQLTEEEEKTKSLNKLKNKQEAVIADLEERLKREEQGRLEQEKFKRRMESEAMEAQEqlsdlgmlsselrgslAQKEKE 1113
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE----------------AKKDEE 1754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1114 ITSLQGRLEEEGARRAEAQRSLREALSQvSELKEEVENERGMRERAEKQRRDLSEELEALRTELEDTLDSTAAQQELRSR 1193
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIE-EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIK 1833
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774933 1194 REAELSELQRCVEEETRRHETQLSELRVKHSAALDSLQEQLDNSKRARQSLEKAKATLEEERQNLTSEL 1262
Cdd:PTZ00121 1834 EVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
998-1271 |
8.22e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 998 LETKVKSLETD-------LATAVEQR-------ERLGKEKKQLE-ERLNEVTD---QLTEEEEKTKSLNKLKNKQEAVIA 1059
Cdd:pfam10174 420 LKERVKSLQTDssntdtaLTTLEEALsekeriiERLKEQREREDrERLEELESlkkENKDLKEKVSALQPELTEKESSLI 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1060 DLEERLKREEQGRLEQEKFKRRMESEAMEAQEQLSDLG--MLSSELRGSLAQKEKEITSLQGRLEEEGARRAEAQRSLRE 1137
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLEnqLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQA 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1138 ALSQVSELKEEVENERGMRERaeKQRRDLSEELEALRTELEDTLDSTAAQQELRSRREAELSELQRCVEEETRRH-ETQL 1216
Cdd:pfam10174 580 EVERLLGILREVENEKNDKDK--KIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSqQLQL 657
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774933 1217 SELrvkhsaaldslqeqLDNSKRARQSLEKAKATLEEERQNLTSELKSLQASRSE 1271
Cdd:pfam10174 658 EEL--------------MGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAE 698
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1025-1201 |
8.30e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.81 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1025 QLEERLNEVTDQLTEEEEKTKSLNKLKNKQEAVIADLEERLK------REEQGRLEQEKfKRRMESEAMEAQEQLSDLGM 1098
Cdd:COG1842 34 DMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARlalekgREDLAREALER-KAELEAQAEALEAQLAQLEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1099 LSSELRGSLAQKEKEITSLQGRLEEEGAR--RAEAQRSLREALSQVSElkeevENERGMRERAEKQRRDLSEELEALRT- 1175
Cdd:COG1842 113 QVEKLKEALRQLESKLEELKAKKDTLKARakAAKAQEKVNEALSGIDS-----DDATSALERMEEKIEEMEARAEAAAEl 187
|
170 180
....*....|....*....|....*.
gi 1988774933 1176 ELEDTLDSTAAQQELRSRREAELSEL 1201
Cdd:COG1842 188 AAGDSLDDELAELEADSEVEDELAAL 213
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
992-1152 |
9.74e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 992 LLEKVTLETKVKSLETDLATAVEQRERLGKEKKQleERLNEVTDQLTEEEEKTKSLNKLKNKQeavIADLEERLKREEQg 1071
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKK--EALLEAKEEIHKLRNEFEKELRERRNE---LQKLEKRLLQKEE- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1072 RLEQ-----EKFKRRMESEAMEAQEQLSDLGMLSSELRGSLAQKEKEITSLQGrLEEEGAR-------RAEAQrslREAL 1139
Cdd:PRK12704 97 NLDRklellEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG-LTAEEAKeillekvEEEAR---HEAA 172
|
170
....*....|...
gi 1988774933 1140 SQVSELKEEVENE 1152
Cdd:PRK12704 173 VLIKEIEEEAKEE 185
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
991-1180 |
9.95e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 991 LLLEKVTLETKVKSLETDLATAVEQRERLGKEKKQLEERLNEvtdqlteeeektksLNKLKNKQEAVIADLEERLKREEQ 1070
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESE--------------LAISRQDYDGATAQLRAAQAAVKA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774933 1071 GRLEQEKfkrrmESEAMEAQEQLSDLGMLSSElrgslaqkekeitslqgRLEEEGARRAEAQRSLREALSQVSELKEEVE 1150
Cdd:pfam00529 115 AQAQLAQ-----AQIDLARRRVLAPIGGISRE-----------------SLVTAGALVAQAQANLLATVAQLDQIYVQIT 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1988774933 1151 NE--------RGMRERAEKQRRDLSEELEALRTELEDT 1180
Cdd:pfam00529 173 QSaaenqaevRSELSGAQLQIAEAEAELKLAKLDLERT 210
|
|
| |
